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Sample records for absolute protein concentrations

  1. Under proper control, oxidation of proteins with known chemical structure provides an accurate and absolute method for the determination of their molar concentration.

    PubMed

    Guermant, C; Azarkan, M; Smolders, N; Baeyens-Volant, D; Nijs, M; Paul, C; Brygier, J; Vincentelli, J; Looze, Y

    2000-01-01

    Oxidation at 120 degrees C of inorganic and organic (including amino acids, di- and tripeptides) model compounds by K(2)Cr(2)O(7) in the presence of H(2)SO(4) (mass fraction: 0.572), Ag(2)SO(4) (catalyst), and HgSO(4) results in the quantitative conversion of their C-atoms into CO(2) within 24 h or less. Under these stressed, well-defined conditions, the S-atoms present in cysteine and cystine residues are oxidized into SO(3) while, interestingly, the oxidation states of all the other (including the N-) atoms normally present in a protein do remain quite unchanged. When the chemical structure of a given protein is available, the total number of electrons the protein is able to transfer to K(2)Cr(2)O(7) and thereof, the total number of moles of Cr(3+) ions which the protein is able to generate upon oxidation can be accurately calculated. In such cases, unknown protein molar concentrations can thus be determined through straightforward spectrophotometric measurements of Cr(3+) concentrations. The values of molar absorption coefficients for several well-characterized proteins have been redetermined on this basis and observed to be in excellent agreement with the most precise values reported in the literature, which fully assesses the validity of the method. When applied to highly purified proteins of known chemical structure (more generally of known atomic composition), this method is absolute and accurate (+/-1%). Furthermore, it is well adapted to series measurements since available commercial kits for chemical oxygen demand (COD) measurements can readily be adapted to work under the experimental conditions recommended here for the protein assay. PMID:10610688

  2. Absolute determination of local tropospheric OH concentrations

    NASA Technical Reports Server (NTRS)

    Armerding, Wolfgang; Comes, Franz-Josef

    1994-01-01

    Long path absorption (LPA) according to Lambert Beer's law is a method to determine absolute concentrations of trace gases such as tropospheric OH. We have developed a LPA instrument which is based on a rapid tuning of the light source which is a frequency doubled dye laser. The laser is tuned across two or three OH absorption features around 308 nm with a scanning speed of 0.07 cm(exp -1)/microsecond and a repetition rate of 1.3 kHz. This high scanning speed greatly reduces the fluctuation of the light intensity caused by the atmosphere. To obtain the required high sensitivity the laser output power is additionally made constant and stabilized by an electro-optical modulator. The present sensitivity is of the order of a few times 10(exp 5) OH per cm(exp 3) for an acquisition time of a minute and an absorption path length of only 1200 meters so that a folding of the optical path in a multireflection cell was possible leading to a lateral dimension of the cell of a few meters. This allows local measurements to be made. Tropospheric measurements have been carried out in 1991 resulting in the determination of OH diurnal variation at specific days in late summer. Comparison with model calculations have been made. Interferences are mainly due to SO2 absorption. The problem of OH self generation in the multireflection cell is of minor extent. This could be shown by using different experimental methods. The minimum-maximum signal to noise ratio is about 8 x 10(exp -4) for a single scan. Due to the small size of the absorption cell the realization of an open air laboratory is possible in which by use of an additional UV light source or by additional fluxes of trace gases the chemistry can be changed under controlled conditions allowing kinetic studies of tropospheric photochemistry to be made in open air.

  3. Absolute nutrient concentration measurements in cell culture media: (1)H q-NMR spectra and data to compare the efficiency of pH-controlled protein precipitation versus CPMG or post-processing filtering approaches.

    PubMed

    Goldoni, Luca; Beringhelli, Tiziana; Rocchia, Walter; Realini, Natalia; Piomelli, Daniele

    2016-09-01

    The NMR spectra and data reported in this article refer to the research article titled "A simple and accurate protocol for absolute polar metabolite quantification in cell cultures using q-NMR" [1]. We provide the (1)H q-NMR spectra of cell culture media (DMEM) after removal of serum proteins, which show the different efficiency of various precipitating solvents, the solvent/DMEM ratios, and pH of the solution. We compare the data of the absolute nutrient concentrations, measured by PULCON external standard method, before and after precipitation of serum proteins and those obtained using CPMG (Carr-Purcell-Meiboom-Gill) sequence or applying post-processing filtering algorithms to remove, from the (1)H q-NMR spectra, the proteins signal contribution. For each of these approaches, the percent error in the absolute value of every measurement for all the nutrients is also plotted as accuracy assessment. PMID:27331118

  4. Absolute concentration measurements inside a jet plume using video digitization

    NASA Astrophysics Data System (ADS)

    Vauquelin, O.

    An experimental system based on digitized video image analysis is used to measure the local value of the concentration inside a plume. Experiments are carried out in a wind-tunnel for a smoke-seeded turbulent jet plume illuminated with a laser beam. Each test is filmed, subsequently video images are digitized and analysed in order to determine the smoke absolute concentration corresponding to each pixel gray level. This non-intrusive measurement technique is first calibrated and different laws connecting gray level to concentration are established. As a first application, concentration measurements are made inside a turbulent jet plume and compared with measurements conducted using a classic gas analysis method. We finally present and discuss the possibilities offered for the measurements of absolute concentration fluctuations.

  5. Non-invasive quantification of brain glycogen absolute concentration

    PubMed Central

    van Heeswijk, Ruud B.; Xin, Lijing; Laus, Sabrina; Frenkel, Hanne; Lei, Hongxia; Gruetter, Rolf

    2009-01-01

    The only currently available method to measure brain glycogen in vivo is 13C NMR spectroscopy. Incorporation of 13C-labeled glucose (Glc) is necessary to allow glycogen measurement, but might be affected by turnover changes. Our aim was to measure glycogen absolute concentration in the rat brain by eliminating label turnover as variable. The approach is based on establishing an increased, constant 13C isotopic enrichment (IE). 13C-Glc infusion is then performed at the IE of brain glycogen. As glycogen IE cannot be assessed in vivo, we validated that it can be inferred from that of N-acetyl-aspartate IE in vivo: After [1-13C]-Glc ingestion, glycogen IE was 2.2 ± 0.1 fold that of N-acetyl-aspartate (n = 11, R2 = 0.77). After subsequent Glc infusion, glycogen IE equaled brain Glc IE (n = 6, paired t-test, p = 0.37), implying isotopic steady-state achievement and complete turnover of the glycogen molecule. Glycogen concentration measured in vivo by 13C NMR (mean ± SD: 5.8 ± 0.7 μmol/g) was in excellent agreement with that in vitro (6.4 ± 0.6 μmol/g, n = 5). When insulin was administered, the stability of glycogen concentration was analogous to previous biochemical measurements implying that glycogen turnover is activated by insulin. We conclude that the entire glycogen molecule is turned over and that insulin activates glycogen turnover. PMID:19013831

  6. Method for determining the absolute number concentration of nanoparticles from electrospray sources.

    PubMed

    Li, Mingdong; Guha, Suvajyoti; Zangmeister, Rebecca; Tarlov, Michael J; Zachariah, Michael R

    2011-12-20

    We have developed a simple, fast, and accurate method to measure the absolute number concentration of nanoparticles in solution. The method combines electrospray differential mobility analysis (ES-DMA) with a statistical analysis of droplet-induced oligomer formation. A key feature of the method is that it allows determination of the absolute number concentration of particles by knowing only the droplet size generated from a particular ES source, thereby eliminating the need for sample-specific calibration standards or detailed analysis of transport losses. The approach was validated by comparing the total number concentration of monodispersed Au nanoparticles determined by ES-DMA with UV/vis measurements. We also show that this approach is valid for protein molecules by quantifying the absolute number concentration of Rituxan monoclonal antibody in solution. The methodology is applicable for quantification of any electrospray process coupled to an analytical tool that can distinguish monomers from higher order oligomers. The only requirement is that the droplet size distribution be evaluated. For users only interested in implementation of the theory, we provide a section that summarizes the relevant formulas. This method eliminates the need for sample-specific calibration standards or detailed analysis of transport losses.

  7. ICP-MS for multiplex absolute determinations of proteins.

    PubMed

    Sanz-Medel, Alfredo

    2010-11-01

    In the last few years MS-based proteomics has been turning quantitative because only the quantity of existing proteins or changes of their abundance in a studied sample reflect the actual status and the extent of possible changes in a given biological system. So far, however, only relative quantifications are common place. Recently, the ideal analytical features of ICP-MS that allow robust, accurate and precise absolute determinations of heteroelements (present in proteins and their peptides) have opened the door to its use, as a complementary ion source of MALDI- and/or ESI-(MS), in achieving the "absolute" quantification of a protein. Unfortunately, so far such "heteroatom-tagged proteomics" applications deal with only single-heteroatom measurements. Thus, the outstanding capability of ICP-MS for multi-element (-isotope) simultaneous determinations is somewhat wasted. On the other hand, multiplexed determinations of proteins (e.g. in common or new multiplexed formats) today constitute a pressing need in medical science (e.g. to determine accurately many biomarkers at a time). This is a clear trend in analytical science where ICP-MS could eventually play an important role. Therefore, reported approaches to multiplex protein determinations using ICP-MS, with liquid sample nebulisation and with laser direct sampling from a solid, are discussed here. Apart from such multiplex bioassays for absolute protein determinations, efforts to simultaneously quantitate enzyme activities are also discussed. It appears that the time is ripe to combine the multi-isotopic character of ICP-MS with well-known multi-analyte separation techniques (e.g. HPLC or multiplex immunoassays) to tackle the challenge of analysing abundances and activities of several proteins and enzymes, respectively, in a single assay. Many attractive opportunities for creative work and interdisciplinary developments for analytical atomic spectroscopists seem to lie ahead related to multiplexed quantitative

  8. Estimation of absolute protein quantities of unlabeled samples by selected reaction monitoring mass spectrometry.

    PubMed

    Ludwig, Christina; Claassen, Manfred; Schmidt, Alexander; Aebersold, Ruedi

    2012-03-01

    , such as high sensitivity, selectivity, reproducibility, and dynamic range, and estimates absolute protein concentrations of selected proteins at minimized costs.

  9. Behavior of Multiclass Pesticide Residue Concentrations during the Transformation from Rose Petals to Rose Absolute.

    PubMed

    Tascone, Oriane; Fillâtre, Yoann; Roy, Céline; Meierhenrich, Uwe J

    2015-05-27

    This study investigates the concentrations of 54 multiclass pesticides during the transformation processes from rose petal to concrete and absolute using roses spiked with pesticides as a model. The concentrations of the pesticides were followed during the process of transforming the spiked rose flowers from an organic field into concrete and then into absolute. The rose flowers, the concrete, and the absolute, as well as their transformation intermediates, were analyzed for pesticide content using gas chromatography/tandem mass spectrometry. We observed that all the pesticides were extracted and concentrated in the absolute, with the exception of three molecules: fenthion, fenamiphos, and phorate. Typical pesticides were found to be concentrated by a factor of 100-300 from the rose flowers to the rose absolute. The observed effect of pesticide enrichment was also studied in roses and their extracts from four classically phytosanitary treated fields. Seventeen pesticides were detected in at least one of the extracts. Like the case for the spiked samples in our model, the pesticides present in the rose flowers from Turkey were concentrated in the absolute. Two pesticides, methidathion and chlorpyrifos, were quantified in the rose flowers at approximately 0.01 and 0.01-0.05 mg kg(-1), respectively, depending on the treated field. The concentrations determined for the corresponding rose absolutes were 4.7 mg kg(-1) for methidathion and 0.65-27.25 mg kg(-1) for chlorpyrifos.

  10. Behavior of Multiclass Pesticide Residue Concentrations during the Transformation from Rose Petals to Rose Absolute.

    PubMed

    Tascone, Oriane; Fillâtre, Yoann; Roy, Céline; Meierhenrich, Uwe J

    2015-05-27

    This study investigates the concentrations of 54 multiclass pesticides during the transformation processes from rose petal to concrete and absolute using roses spiked with pesticides as a model. The concentrations of the pesticides were followed during the process of transforming the spiked rose flowers from an organic field into concrete and then into absolute. The rose flowers, the concrete, and the absolute, as well as their transformation intermediates, were analyzed for pesticide content using gas chromatography/tandem mass spectrometry. We observed that all the pesticides were extracted and concentrated in the absolute, with the exception of three molecules: fenthion, fenamiphos, and phorate. Typical pesticides were found to be concentrated by a factor of 100-300 from the rose flowers to the rose absolute. The observed effect of pesticide enrichment was also studied in roses and their extracts from four classically phytosanitary treated fields. Seventeen pesticides were detected in at least one of the extracts. Like the case for the spiked samples in our model, the pesticides present in the rose flowers from Turkey were concentrated in the absolute. Two pesticides, methidathion and chlorpyrifos, were quantified in the rose flowers at approximately 0.01 and 0.01-0.05 mg kg(-1), respectively, depending on the treated field. The concentrations determined for the corresponding rose absolutes were 4.7 mg kg(-1) for methidathion and 0.65-27.25 mg kg(-1) for chlorpyrifos. PMID:25942486

  11. Sulfur-based absolute quantification of proteins using isotope dilution inductively coupled plasma mass spectrometry

    NASA Astrophysics Data System (ADS)

    Lee, Hyun-Seok; Heun Kim, Sook; Jeong, Ji-Seon; Lee, Yong-Moon; Yim, Yong-Hyeon

    2015-10-01

    An element-based reductive approach provides an effective means of realizing International System of Units (SI) traceability for high-purity biological standards. Here, we develop an absolute protein quantification method using double isotope dilution (ID) inductively coupled plasma mass spectrometry (ICP-MS) combined with microwave-assisted acid digestion for the first time. We validated the method and applied it to certify the candidate protein certified reference material (CRM) of human growth hormone (hGH). The concentration of hGH was determined by analysing the total amount of sulfur in hGH. Next, the size-exclusion chromatography method was used with ICP-MS to characterize and quantify sulfur-containing impurities. By subtracting the contribution of sulfur-containing impurities from the total sulfur content in the hGH CRM, we obtained a SI-traceable certification value. The quantification result obtained with the present method based on sulfur analysis was in excellent agreement with the result determined via a well-established protein quantification method based on amino acid analysis using conventional acid hydrolysis combined with an ID liquid chromatography-tandem mass spectrometry. The element-based protein quantification method developed here can be generally used for SI-traceable absolute quantification of proteins, especially pure-protein standards.

  12. Absolute quantitation of isoforms of post-translationally modified proteins in transgenic organism.

    PubMed

    Li, Yaojun; Shu, Yiwei; Peng, Changchao; Zhu, Lin; Guo, Guangyu; Li, Ning

    2012-08-01

    Post-translational modification isoforms of a protein are known to play versatile biological functions in diverse cellular processes. To measure the molar amount of each post-translational modification isoform (P(isf)) of a target protein present in the total protein extract using mass spectrometry, a quantitative proteomic protocol, absolute quantitation of isoforms of post-translationally modified proteins (AQUIP), was developed. A recombinant ERF110 gene overexpression transgenic Arabidopsis plant was used as the model organism for demonstration of the proof of concept. Both Ser-62-independent (14)N-coded synthetic peptide standards and (15)N-coded ERF110 protein standard isolated from the heavy nitrogen-labeled transgenic plants were employed simultaneously to determine the concentration of all isoforms (T(isf)) of ERF110 in the whole plant cell lysate, whereas a pair of Ser-62-dependent synthetic peptide standards were used to quantitate the Ser-62 phosphosite occupancy (R(aqu)). The P(isf) was finally determined by integrating the two empirically measured variables using the following equation: P(isf) = T(isf) · R(aqu). The absolute amount of Ser-62-phosphorylated isoform of ERF110 determined using AQUIP was substantiated with a stable isotope labeling in Arabidopsis-based relative and accurate quantitative proteomic approach. The biological role of the Ser-62-phosphorylated isoform was demonstrated in transgenic plants.

  13. Direct and Absolute Quantification of over 1800 Yeast Proteins via Selected Reaction Monitoring*

    PubMed Central

    Lawless, Craig; Holman, Stephen W.; Brownridge, Philip; Lanthaler, Karin; Harman, Victoria M.; Watkins, Rachel; Hammond, Dean E.; Miller, Rebecca L.; Sims, Paul F. G.; Grant, Christopher M.; Eyers, Claire E.; Beynon, Robert J.

    2016-01-01

    Defining intracellular protein concentration is critical in molecular systems biology. Although strategies for determining relative protein changes are available, defining robust absolute values in copies per cell has proven significantly more challenging. Here we present a reference data set quantifying over 1800 Saccharomyces cerevisiae proteins by direct means using protein-specific stable-isotope labeled internal standards and selected reaction monitoring (SRM) mass spectrometry, far exceeding any previous study. This was achieved by careful design of over 100 QconCAT recombinant proteins as standards, defining 1167 proteins in terms of copies per cell and upper limits on a further 668, with robust CVs routinely less than 20%. The selected reaction monitoring-derived proteome is compared with existing quantitative data sets, highlighting the disparities between methodologies. Coupled with a quantification of the transcriptome by RNA-seq taken from the same cells, these data support revised estimates of several fundamental molecular parameters: a total protein count of ∼100 million molecules-per-cell, a median of ∼1000 proteins-per-transcript, and a linear model of protein translation explaining 70% of the variance in translation rate. This work contributes a “gold-standard” reference yeast proteome (including 532 values based on high quality, dual peptide quantification) that can be widely used in systems models and for other comparative studies. PMID:26750110

  14. In situ measurement of leaf chlorophyll concentration: analysis of the optical/absolute relationship.

    PubMed

    Parry, Christopher; Blonquist, J Mark; Bugbee, Bruce

    2014-11-01

    In situ optical meters are widely used to estimate leaf chlorophyll concentration, but non-uniform chlorophyll distribution causes optical measurements to vary widely among species for the same chlorophyll concentration. Over 30 studies have sought to quantify the in situ/in vitro (optical/absolute) relationship, but neither chlorophyll extraction nor measurement techniques for in vitro analysis have been consistent among studies. Here we: (1) review standard procedures for measurement of chlorophyll; (2) estimate the error associated with non-standard procedures; and (3) implement the most accurate methods to provide equations for conversion of optical to absolute chlorophyll for 22 species grown in multiple environments. Tests of five Minolta (model SPAD-502) and 25 Opti-Sciences (model CCM-200) meters, manufactured from 1992 to 2013, indicate that differences among replicate models are less than 5%. We thus developed equations for converting between units from these meter types. There was no significant effect of environment on the optical/absolute chlorophyll relationship. We derive the theoretical relationship between optical transmission ratios and absolute chlorophyll concentration and show how non-uniform distribution among species causes a variable, non-linear response. These results link in situ optical measurements with in vitro chlorophyll concentration and provide insight to strategies for radiation capture among diverse species.

  15. Airborne concentrations of peanut protein.

    PubMed

    Johnson, Rodney M; Barnes, Charles S

    2013-01-01

    Food allergy to peanut is a significant health problem, and there are reported allergic reactions to peanuts despite not eating or having physical contact with peanuts. It is presumed that an allergic reaction may have occurred from inhalation of airborne peanut allergens. The purpose of this study was to detect the possible concentrations of airborne peanut proteins for various preparations and during specific activities. Separate Ara h 1 and Ara h 2 monoclonal enzyme-linked immunosorbent assays and a polyclonal sandwich enzyme immunoassay for peanuts were used to detect the amount of airborne peanut protein collected using a Spincon Omni 3000 air collector (Sceptor Industries, Inc., Kansas City, MO) under different peanut preparation methods and situations. Air samples were measured for multiple peanut preparations and scenarios. Detectable amounts of airborne peanut protein were measured using a whole peanut immunoassay when removing the shells of roasted peanut. No airborne peanut allergen (Ara h 1 or Ara h 2) or whole peanut protein above the LLD was measured in any of the other peanut preparation collections. Ara h 1, Ara h 2, and polyclonal peanut proteins were detected from water used to boil peanuts. Small amounts of airborne peanut protein were detected in the scenario of removing shells from roasted peanuts; however, Ara h 1 and Ara h 2 proteins were unable to be consistently detected. Although airborne peanut proteins were detected, the concentration of airborne peanut protein that is necessary to elicit a clinical allergic reaction is unknown.

  16. Airborne concentrations of peanut protein.

    PubMed

    Johnson, Rodney M; Barnes, Charles S

    2013-01-01

    Food allergy to peanut is a significant health problem, and there are reported allergic reactions to peanuts despite not eating or having physical contact with peanuts. It is presumed that an allergic reaction may have occurred from inhalation of airborne peanut allergens. The purpose of this study was to detect the possible concentrations of airborne peanut proteins for various preparations and during specific activities. Separate Ara h 1 and Ara h 2 monoclonal enzyme-linked immunosorbent assays and a polyclonal sandwich enzyme immunoassay for peanuts were used to detect the amount of airborne peanut protein collected using a Spincon Omni 3000 air collector (Sceptor Industries, Inc., Kansas City, MO) under different peanut preparation methods and situations. Air samples were measured for multiple peanut preparations and scenarios. Detectable amounts of airborne peanut protein were measured using a whole peanut immunoassay when removing the shells of roasted peanut. No airborne peanut allergen (Ara h 1 or Ara h 2) or whole peanut protein above the LLD was measured in any of the other peanut preparation collections. Ara h 1, Ara h 2, and polyclonal peanut proteins were detected from water used to boil peanuts. Small amounts of airborne peanut protein were detected in the scenario of removing shells from roasted peanuts; however, Ara h 1 and Ara h 2 proteins were unable to be consistently detected. Although airborne peanut proteins were detected, the concentration of airborne peanut protein that is necessary to elicit a clinical allergic reaction is unknown. PMID:23406937

  17. Absolute tracer dye concentration using airborne laser-induced water Raman backscatter

    NASA Technical Reports Server (NTRS)

    Hoge, F. E.; Swift, R. N.

    1981-01-01

    The use of simultaneous airborne-laser-induced dye fluorescence and water Raman backscatter to measure the absolute concentration of an ocean-dispersed tracer dye is discussed. Theoretical considerations of the calculation of dye concentration by the numerical comparison of airborne laser-induced fluorescence spectra with laboratory spectra for known dye concentrations using the 3400/cm OH-stretch water Raman scatter as a calibration signal are presented which show that minimum errors are obtained and no data concerning water mass transmission properties are required when the laser wavelength is chosen to yield a Raman signal near the dye emission band. Results of field experiments conducted with an airborne conical scan lidar over a site in New York Bight into which rhodamine dye had been injected in a study of oil spill dispersion are then indicated which resulted in a contour map of dye concentrations, with a minimum detectable dye concentration of approximately 2 ppb by weight.

  18. Microfabricated Collector-Generator Electrode Sensor for Measuring Absolute pH and Oxygen Concentrations.

    PubMed

    Dengler, Adam K; Wightman, R Mark; McCarty, Gregory S

    2015-10-20

    Fast-scan cyclic voltammetry (FSCV) has attracted attention for studying in vivo neurotransmission due to its subsecond temporal resolution, selectivity, and sensitivity. Traditional FSCV measurements use background subtraction to isolate changes in the local electrochemical environment, providing detailed information on fluctuations in the concentration of electroactive species. This background subtraction removes information about constant or slowly changing concentrations. However, determination of background concentrations is still important for understanding functioning brain tissue. For example, neural activity is known to consume oxygen and produce carbon dioxide which affects local levels of oxygen and pH. Here, we present a microfabricated microelectrode array which uses FSCV to detect the absolute levels of oxygen and pH in vitro. The sensor is a collector-generator electrode array with carbon microelectrodes spaced 5 μm apart. In this work, a periodic potential step is applied at the generator producing transient local changes in the electrochemical environment. The collector electrode continuously performs FSCV enabling these induced changes in concentration to be recorded with the sensitivity and selectivity of FSCV. A negative potential step applied at the generator produces a transient local pH shift at the collector. The generator-induced pH signal is detected using FSCV at the collector and correlated to absolute solution pH by postcalibration of the anodic peak position. In addition, in oxygenated solutions a negative potential step at the generator produces hydrogen peroxide by reducing oxygen. Hydrogen peroxide is detected with FSCV at the collector electrode, and the magnitude of the oxidative peak is proportional to absolute oxygen concentrations. Oxygen interference on the pH signal is minimal and can be accounted for with a postcalibration.

  19. Using Absolute Humidity and Radiochemical Analyses of Water Vapor Samples to Correct Underestimated Atmospheric Tritium Concentrations

    SciTech Connect

    Eberhart, C.F.

    1999-06-01

    Los Alamos National Laboratory (LANL) emits a wide variety of radioactive air contaminants. An extensive ambient air monitoring network, known as AIRNET, is operated on-site and in surrounding communities to estimate radioactive doses to the public. As part of this monitoring network, water vapor is sampled continuously at more than 50 sites. These water vapor samples are collected every two weeks by absorbing the water vapor in the sampled air with silica gel and then radiochemically analyzing the water for tritium. The data have consistently indicated that LANL emissions cause a small, but measurable impact on local concentrations of tritium. In early 1998, while trying to independently verify the presumed 100% water vapor collection efficiency, the author found that this efficiency was normally lower and reached a minimum of 10 to 20% in the middle of summer. This inefficient collection was discovered by comparing absolute humidity (g/m{sup 3}) calculated from relative humidity and temperature to the amount of water vapor collected by the silica gel per cubic meter of air sampled. Subsequent experiments confirmed that the elevated temperature inside the louvered housing was high enough to reduce the capacity of the silica gel by more than half. In addition, their experiments also demonstrated that, even under optimal conditions, there is not enough silica gel present in the sampling canister to absorb all of the moisture during the higher humidity periods. However, there is a solution to this problem. Ambient tritium concentrations have been recalculated by using the absolute humidity values and the tritium analyses. These recalculated tritium concentrations were two to three times higher than previously reported. Future tritium concentrations will also be determined in the same manner. Finally, the water vapor collection process will be changed by relocating the sampling canister outside the housing to increase collection efficiency and, therefore

  20. Mass spectrometry-based absolute quantification reveals rhythmic variation of mouse circadian clock proteins.

    PubMed

    Narumi, Ryohei; Shimizu, Yoshihiro; Ukai-Tadenuma, Maki; Ode, Koji L; Kanda, Genki N; Shinohara, Yuta; Sato, Aya; Matsumoto, Katsuhiko; Ueda, Hiroki R

    2016-06-14

    Absolute values of protein expression levels in cells are crucial information for understanding cellular biological systems. Precise quantification of proteins can be achieved by liquid chromatography (LC)-mass spectrometry (MS) analysis of enzymatic digests of proteins in the presence of isotope-labeled internal standards. Thus, development of a simple and easy way for the preparation of internal standards is advantageous for the analyses of multiple target proteins, which will allow systems-level studies. Here we describe a method, termed MS-based Quantification By isotope-labeled Cell-free products (MS-QBiC), which provides the simple and high-throughput preparation of internal standards by using a reconstituted cell-free protein synthesis system, and thereby facilitates both multiplexed and sensitive quantification of absolute amounts of target proteins. This method was applied to a systems-level dynamic analysis of mammalian circadian clock proteins, which consist of transcription factors and protein kinases that govern central and peripheral circadian clocks in mammals. Sixteen proteins from 20 selected circadian clock proteins were successfully quantified from mouse liver over a 24-h time series, and 14 proteins had circadian variations. Quantified values were applied to detect internal body time using a previously developed molecular timetable method. The analyses showed that single time-point data from wild-type mice can predict the endogenous state of the circadian clock, whereas data from clock mutant mice are not applicable because of the disappearance of circadian variation. PMID:27247408

  1. Global absolute quantification reveals tight regulation of protein expression in single Xenopus eggs

    PubMed Central

    Smits, Arne H.; Lindeboom, Rik G.H.; Perino, Matteo; van Heeringen, Simon J.; Veenstra, Gert Jan C.; Vermeulen, Michiel

    2014-01-01

    While recent developments in genomic sequencing technology have enabled comprehensive transcriptome analyses of single cells, single cell proteomics has thus far been restricted to targeted studies. Here, we perform global absolute protein quantification of fertilized Xenopus laevis eggs using mass spectrometry-based proteomics, quantifying over 5800 proteins in the largest single cell proteome characterized to date. Absolute protein amounts in single eggs are highly consistent, thus indicating a tight regulation of global protein abundance. Protein copy numbers in single eggs range from tens of thousands to ten trillion copies per cell. Comparison between the single-cell proteome and transcriptome reveal poor expression correlation. Finally, we identify 439 proteins that significantly change in abundance during early embryogenesis. Downregulated proteins include ribosomal proteins and upregulated proteins include basal transcription factors, among others. Many of these proteins do not show regulation at the transcript level. Altogether, our data reveal that the transcriptome is a poor indicator of the proteome and that protein levels are tightly controlled in X. laevis eggs. PMID:25056316

  2. Absolute protein quantification of the yeast chaperome under conditions of heat shock

    PubMed Central

    Mackenzie, Rebecca J.; Lawless, Craig; Holman, Stephen W.; Lanthaler, Karin; Beynon, Robert J.; Grant, Chris M.; Hubbard, Simon J.

    2016-01-01

    Chaperones are fundamental to regulating the heat shock response, mediating protein recovery from thermal‐induced misfolding and aggregation. Using the QconCAT strategy and selected reaction monitoring (SRM) for absolute protein quantification, we have determined copy per cell values for 49 key chaperones in Saccharomyces cerevisiae under conditions of normal growth and heat shock. This work extends a previous chemostat quantification study by including up to five Q‐peptides per protein to improve confidence in protein quantification. In contrast to the global proteome profile of S. cerevisiae in response to heat shock, which remains largely unchanged as determined by label‐free quantification, many of the chaperones are upregulated with an average two‐fold increase in protein abundance. Interestingly, eight of the significantly upregulated chaperones are direct gene targets of heat shock transcription factor‐1. By performing absolute quantification of chaperones under heat stress for the first time, we were able to evaluate the individual protein‐level response. Furthermore, this SRM data was used to calibrate label‐free quantification values for the proteome in absolute terms, thus improving relative quantification between the two conditions. This study significantly enhances the largely transcriptomic data available in the field and illustrates a more nuanced response at the protein level. PMID:27252046

  3. A targeted proteomics toolkit for high-throughput absolute quantification of Escherichia coli proteins.

    PubMed

    Batth, Tanveer S; Singh, Pragya; Ramakrishnan, Vikram R; Sousa, Mirta M L; Chan, Leanne Jade G; Tran, Huu M; Luning, Eric G; Pan, Eva H Y; Vuu, Khanh M; Keasling, Jay D; Adams, Paul D; Petzold, Christopher J

    2014-11-01

    Transformation of engineered Escherichia coli into a robust microbial factory is contingent on precise control of metabolism. Yet, the throughput of omics technologies used to characterize cell components has lagged far behind our ability to engineer novel strains. To expand the utility of quantitative proteomics for metabolic engineering, we validated and optimized targeted proteomics methods for over 400 proteins from more than 20 major pathways in E. coli metabolism. Complementing these methods, we constructed a series of synthetic genes to produce concatenated peptides (QconCAT) for absolute quantification of the proteins and made them available through the Addgene plasmid repository (www.addgene.org). To facilitate high sample throughput, we developed a fast, analytical-flow chromatography method using a 5.5-min gradient (10 min total run time). Overall this toolkit provides an invaluable resource for metabolic engineering by increasing sample throughput, minimizing development time and providing peptide standards for absolute quantification of E. coli proteins.

  4. Absolute Binding Free Energy Calculations: On the Accuracy of Computational Scoring of Protein-ligand Interactions

    PubMed Central

    Singh, Nidhi; Warshel, Arieh

    2010-01-01

    Calculating the absolute binding free energies is a challenging task. Reliable estimates of binding free energies should provide a guide for rational drug design. It should also provide us with deeper understanding of the correlation between protein structure and its function. Further applications may include identifying novel molecular scaffolds and optimizing lead compounds in computer-aided drug design. Available options to evaluate the absolute binding free energies range from the rigorous but expensive free energy perturbation to the microscopic Linear Response Approximation (LRA/β version) and its variants including the Linear Interaction Energy (LIE) to the more approximated and considerably faster scaled Protein Dipoles Langevin Dipoles (PDLD/S-LRA version), as well as the less rigorous Molecular Mechanics Poisson–Boltzmann/Surface Area (MM/PBSA) and Generalized Born/Surface Area (MM/GBSA) to the less accurate scoring functions. There is a need for an assessment of the performance of different approaches in terms of computer time and reliability. We present a comparative study of the LRA/β, the LIE, the PDLD/S-LRA/β and the more widely used MM/PBSA and assess their abilities to estimate the absolute binding energies. The LRA and LIE methods perform reasonably well but require specialized parameterization for the non-electrostatic term. On the average, the PDLD/S-LRA/β performs effectively. Our assessment of the MM/PBSA is less optimistic. This approach appears to provide erroneous estimates of the absolute binding energies due to its incorrect entropies and the problematic treatment of electrostatic energies. Overall, the PDLD/S-LRA/β appears to offer an appealing option for the final stages of massive screening approaches. PMID:20186976

  5. In situ TDLAS measurement of absolute acetylene concentration profiles in a non-premixed laminar counter-flow flame

    NASA Astrophysics Data System (ADS)

    Wagner, S.; Klein, M.; Kathrotia, T.; Riedel, U.; Kissel, T.; Dreizler, A.; Ebert, V.

    2012-06-01

    Acetylene (C2H2), as an important precursor for chemiluminescence species, is a key to understand, simulate and model the chemiluminescence and the related reaction paths. Hence we developed a high resolution spectrometer based on direct Tunable Diode Laser Absorption Spectroscopy (TDLAS) allowing the first quantitative, calibration-free and spatially resolved in situ C2H2 measurement in an atmospheric non-premixed counter-flow flame supported on a Tsuji burner. A fiber-coupled distributed feedback diode laser near 1535 nm was used to measure several absolute C2H2 concentration profiles (peak concentrations up to 9700 ppm) in a laminar non-premixed CH4/air flame ( T up to 1950 K) supported on a modified Tsuji counter-flow burner with N2 purge slots to minimize end flames. We achieve a fractional optical resolution of up to 5×10-5 OD (1 σ) in the flame, resulting in temperature-dependent acetylene detection limits for the P17e line at 6513 cm-1 of up to 2.1 ppmṡm. Absolute C2H2 concentration profiles were obtained by translating the burner through the laser beam using a DC motor with 100 μm step widths. Intercomparisons of the experimental C2H2 profiles with simulations using our new hydrocarbon oxidation mechanisms show excellent agreement in position, shape and in the absolute C2H2 values.

  6. Targeted absolute quantification of intact proteins by reversed phase liquid chromatography-mass spectrometry, charge reduced electrospray, and condensation particle counting.

    PubMed

    Adou, Kouame; Johnston, Murray V; Dykins, John L

    2012-08-21

    A novel approach involving the use of reversed phase liquid chromatography-mass spectrometry (RPLC-MS), charge reduced electrospray (CRES), and condensation particle counting (CPC) for the absolute quantification of intact proteins in liquid solutions is introduced. Under analysis conditions optimized for the quantification of select proteins within their predetermined linear ranges, a set of at least five protein standards with molecular weights (MW) spanning the dynamic ranges of both a quadrupole time-of-flight (QTOF) MS and a suitably selected RPLC column is used to generate a calibration curve of CPC detection efficiency (DE) as a function of the square root of MW. Next, the sample of interest is analyzed, and from the MS-generated MW data, the DE of each target protein is determined from the calibration curve. On the basis of MW, DE, and number concentration (molecules/unit volume), absolute quantification is achieved for each protein of interest. Application of this approach to the absolute quantification of cytochrome C (as target compound) in a commercial protein mixture is demonstrated with a deviation of 8%, a coefficient of variation (CV) of 5%, and a quantification limit of 432 fmol. For nontarget components of the mixture (ribonuclease A, holotransferrin, and apomyoglobin), the percent deviation from the stated concentrations and the CV varied from 0.20 to 23 and from 4.1 to 18, respectively. Performance of the method was further assessed by analyzing a laboratory quality control mixture comprising 0.33 μM of cytochrome C. The calculated value was 0.34 (CV: 5.1%). Universal in essence, the new technique holds strong promise for the absolute quantification of select proteins in liquid samples under conditions of good peak resolution and stable baseline.

  7. Concentrating membrane proteins using ultrafiltration without concentrating detergents.

    PubMed

    Feroz, Hasin; Vandervelden, Craig; Ikwuagwu, Bon; Ferlez, Bryan; Baker, Carol S; Lugar, Daniel J; Grzelakowski, Mariusz; Golbeck, John H; Zydney, Andrew L; Kumar, Manish

    2016-10-01

    Membrane proteins (MPs) are of rapidly growing interest in the design of pharmaceutical products, novel sensors, and synthetic membranes. Ultrafiltration (UF) using commercially available centrifugal concentrators is typically employed for laboratory-scale concentration of low-yield MPs, but its use is accompanied by a concomitant increase in concentration of detergent micelles. We present a detailed analysis of the hydrodynamic processes that control detergent passage during ultrafiltration of MPs and propose methods to optimize detergent passage during protein concentration in larger-scale membrane processes. Experiments were conducted using nonionic detergents, octyl-β-D glucoside (OG), and decyl-β-D maltoside (DM) with the bacterial water channel protein, Aquaporin Z (AqpZ) and the light driven chloride pump, halorhodopsin (HR), respectively. The observed sieving coefficient (So ), a measure of detergent passage, was evaluated in both stirred cell and centrifugal systems. So for DM and OG increased with increasing filtrate flux and decreasing shear rates in the stirred cell, that is, with increasing concentration polarization (CP). Similar effects were observed during filtration of MP-detergent (MPD) micelles. However, lower transmission was observed in the centrifugal system for both detergent and MPD systems. This is attributed to free convection-induced shear and hence reduced CP along the membrane surface during centrifugal UF. Thus to concentrate MPs without retention of detergent, design of UF systems that promote CP is required. Biotechnol. Bioeng. 2016;113: 2122-2130. © 2016 Wiley Periodicals, Inc. PMID:27563851

  8. Two-Photon Lifetime Imaging of Voltage Indicating Proteins as a Probe of Absolute Membrane Voltage.

    PubMed

    Brinks, Daan; Klein, Aaron J; Cohen, Adam E

    2015-09-01

    Genetically encoded voltage indicators (GEVIs) can report cellular electrophysiology with high resolution in space and time. Two-photon (2P) fluorescence has been explored as a means to image voltage in tissue. Here, we used the 2P electronic excited-state lifetime to probe absolute membrane voltage in a manner that is insensitive to the protein expression level, illumination intensity, or photon detection efficiency. First, we tested several GEVIs for 2P brightness, response speed, and voltage sensitivity. ASAP1 and a previously described citrine-Arch electrochromic Förster resonance energy transfer sensor (dubbed CAESR) showed the best characteristics. We then characterized the voltage-dependent lifetime of ASAP1, CAESR, and ArcLight under voltage-clamp conditions. ASAP1 and CAESR showed voltage-dependent lifetimes, whereas ArcLight did not. These results establish 2P fluorescence lifetime imaging as a viable means of measuring absolute membrane voltage. We discuss the prospects and improvements necessary for applications in tissue.

  9. Two-Photon Lifetime Imaging of Voltage Indicating Proteins as a Probe of Absolute Membrane Voltage.

    PubMed

    Brinks, Daan; Klein, Aaron J; Cohen, Adam E

    2015-09-01

    Genetically encoded voltage indicators (GEVIs) can report cellular electrophysiology with high resolution in space and time. Two-photon (2P) fluorescence has been explored as a means to image voltage in tissue. Here, we used the 2P electronic excited-state lifetime to probe absolute membrane voltage in a manner that is insensitive to the protein expression level, illumination intensity, or photon detection efficiency. First, we tested several GEVIs for 2P brightness, response speed, and voltage sensitivity. ASAP1 and a previously described citrine-Arch electrochromic Förster resonance energy transfer sensor (dubbed CAESR) showed the best characteristics. We then characterized the voltage-dependent lifetime of ASAP1, CAESR, and ArcLight under voltage-clamp conditions. ASAP1 and CAESR showed voltage-dependent lifetimes, whereas ArcLight did not. These results establish 2P fluorescence lifetime imaging as a viable means of measuring absolute membrane voltage. We discuss the prospects and improvements necessary for applications in tissue. PMID:26331249

  10. Noninvasive imaging of absolute PpIX concentration distribution in nonmelanoma skin tumors at pre-PDT

    NASA Astrophysics Data System (ADS)

    Sunar, Ulas; Rohrbach, Daniel; Morgan, Janet; Zeitouni, Natalie

    2013-03-01

    Photodynamic Therapy (PDT) has proven to be an effective treatment option for nonmelanoma skin cancers. The ability to quantify the concentration of drug in the treated area is crucial for effective treatment planning as well as predicting outcomes. We utilized spatial frequency domain imaging for quantifying the accurate concentration of protoporphyrin IX (PpIX) in phantoms and in vivo. We correct fluorescence against the effects of native tissue absorption and scattering parameters. First we quantified the absorption and scattering of the tissue non-invasively. Then, we corrected raw fluorescence signal by compensating for optical properties to get the absolute drug concentration. After phantom experiments, we used basal cell carcinoma (BCC) model in Gli mice to determine optical properties and drug concentration in vivo at pre-PDT.

  11. Pyridine Hemochromagen Assay for Determining the Concentration of Heme in Purified Protein Solutions

    PubMed Central

    Barr, Ian; Guo, Feng

    2016-01-01

    Heme is a common cofactor in proteins, found in hemoglobin, myoglobin, cytochrome P450, DGCR8, and nitric oxide synthase, among others. This protocol describes a method for quantifying heme that works best in purified protein samples. This protocol might be used to, for example, determine whether a given heme-binding protein is fully occupied by heme, thus allowing correlation of heme content with activity. This requires the absolute heme concentration and an accurate protein concentration. Another use is to determine the extinction coefficients of a heme-bound protein. This assay is fast, easy, and reproducible if done correctly. PMID:27390766

  12. Protein gelation kinetics near the overlap concentration

    NASA Astrophysics Data System (ADS)

    Tabatabai, Pasha; Partlow, Benjamin; Kaplan, David; Blair, Daniel

    Proteins can be crosslinked to form gel networks either as a tool to study biological problems or as a method for creating novel materials. The bulk mechanical properties of protein gels in steady state are a manifestation of the gel structure, but the polymerization kinetics are often disregarded. Using the gelation of an aqueous denatured silk protein solution as a model polymer system, we probe the gelation kinetics (modulus vs. time) and find two regimes that depend on whether the initial protein concentration (c) is near or below the overlap concentration (c *) . We find that systems with c / c * ~ 1 exhibit immediate and single-mode modulus growth until the completion of polymerization that can be scaled onto a characteristic polymerization curve. However, systems with c / c * < 1 display delayed modulus development followed by two-stage modulus growth that can be normalized onto a separate distinctive polymerization curve. These two regimes are probed by changing both the initial concentration and the overlap concentration separately, emphasizing the importance of the overlap concentration on the assembly of polymeric/complex fluids.

  13. Metal-tag labeling coupled with multiple reaction monitoring-mass spectrometry for absolute quantitation of proteins.

    PubMed

    Wang, Xueying; Wang, Xin; Qin, Weijie; Lin, Hongjun; Wang, Jifeng; Wei, Junying; Zhang, Yangjun; Qian, Xiaohong

    2013-09-21

    Mass spectrometry-based quantitative proteomics, consisting of relative and absolute parts, has been used to discover and validate proteins with key functions related to physiological and pathological processes. Currently, stable isotope dilution-multiple reaction monitoring-mass spectrometry (SID-MRM-MS) is the most commonly used method for the absolute determination of proteins in a biological sample. A prerequisite for this method is obtaining internal standards with isotope labels. Although many approaches have been developed for the labeling and preparation of internal peptides, expensive stable isotope labeling coupled with SID-MRM-MS has limited the application and development of an absolute quantitative method. Recently, a low-cost strategy using metal-tag labeling and MS has been developed for relative quantification of peptides or proteins. The introduction of labeling using metal tags has the merits of allowing multiple labeling and enlarging the mass shift to overcome the overlap of adjacent isotope clusters. However, most papers described MRM-MS for protein absolute quantification based on the metal in its peptides labelled with metal by inductively coupled plasma mass spectrometry (ICP MS) but not on its peptides labelled with metal. In this work, a novel approach based on metal-tag labeling coupled with MRM-MS was established for the absolute quantification of peptides or proteins. The principle of the method is that a bifunctional chelator, 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid bearing an N-hydroxysuccinimide ester (DOTA-NHS ester), is used to modify the N-termini of signature peptides from a target protein, and the modified peptides then chelate a certain metal, such as thulium, to form metal-tagged peptides (Tm-DOTA-P). Internal peptides are chemically synthesized and labeled with another metal, such as terbium (Tb-DOTA-P), as the internal standard. Both the Tb-DOTA- and Tm-DOTA-labeled peptides in samples can be analysed via

  14. Determining the Absolute Concentration of Nanoparticles without Calibration Factor by Visualizing the Dynamic Processes of Interfacial Adsorption.

    PubMed

    Wo, Xiang; Li, Zhimin; Jiang, Yingyan; Li, Minghe; Su, Yu-Wen; Wang, Wei; Tao, Nongjian

    2016-02-16

    Previous approaches of determining the molar concentration of nanoparticles often relied on the calibration factors extracted from standard samples or required prior knowledge regarding the geometry, optical, or chemical properties. In the present work, we proposed an absolute quantification method that determined the molar concentration of nano-objects without any calibration factor or prior knowledge. It was realized by monitoring the dynamic adsorption processes of individual nanoparticles with a high-speed surface plasmon resonance microscopy. In this case, diffusing nano-objects stochastically collided onto an adsorption interface and stayed there ("hit-n-stay" scenario), resulting in a semi-infinite diffusion system. The dynamic processes were analyzed with a theoretical model consisting of Fick's laws of diffusion and random-walk assumption. The quantification of molar concentration was achieved on the basis of an analytical expression, which involved only physical constants and experimental parameters. By using spherical polystyrene nanoparticles as a model, the present approach provided a molar concentration with excellent accuracy. PMID:26781326

  15. Easy Absolute Values? Absolutely

    ERIC Educational Resources Information Center

    Taylor, Sharon E.; Mittag, Kathleen Cage

    2015-01-01

    The authors teach a problem-solving course for preservice middle-grades education majors that includes concepts dealing with absolute-value computations, equations, and inequalities. Many of these students like mathematics and plan to teach it, so they are adept at symbolic manipulations. Getting them to think differently about a concept that they…

  16. Serum protein concentrations in Plasmodium falciparum malaria.

    PubMed

    Graninger, W; Thalhammer, F; Hollenstein, U; Zotter, G M; Kremsner, P G

    1992-12-01

    In patients with uncomplicated Plasmodium falciparum infection cytokine-mediated serum protein levels of C-reactive protein (CRP), coeruloplasmin (COE), beta 2-microglobulin (B2M), alpha 1-acid glycoprotein (AAG), alpha 1-antitrypsin (AAT), haptoglobin (HPT), prealbumin (PRE), retinol binding protein (RBP), albumin (ALB) and transferrin (TRF) were measured in an endemic area of the Amazonian rain forest. Semi-immune (SI) and nonimmune (NI) patients were investigated. In both patient groups the serum concentrations of CRP, COE and B2M were elevated on admission. In addition AAG and AAT concentrations were increased in NI patients compared to control subjects. Significantly lower serum concentrations of HPT, PRE, RBP, ALB and TRF were seen in both patient groups during the acute phase of the disease, and were more pronounced in NI patients. After a 28-day follow-up, AAT and B2M were normal in SI patients but HPT, AAT and B2M were still significantly altered in NI patients.

  17. Measuring protein concentration with entangled photons

    NASA Astrophysics Data System (ADS)

    Crespi, Andrea; Lobino, Mirko; Matthews, Jonathan C. F.; Politi, Alberto; Neal, Chris R.; Ramponi, Roberta; Osellame, Roberto; O'Brien, Jeremy L.

    2012-06-01

    Optical interferometry is amongst the most sensitive techniques for precision measurement. By increasing the light intensity, a more precise measurement can usually be made. However, if the sample is light sensitive entangled states can achieve the same precision with less exposure. This concept has been demonstrated in measurements of known optical components. Here, we use two-photon entangled states to measure the concentration of a blood protein in an aqueous buffer solution. We use an opto-fluidic device that couples a waveguide interferometer with a microfluidic channel. These results point the way to practical applications of quantum metrology to light-sensitive samples.

  18. A "proteomic ruler" for protein copy number and concentration estimation without spike-in standards.

    PubMed

    Wiśniewski, Jacek R; Hein, Marco Y; Cox, Jürgen; Mann, Matthias

    2014-12-01

    Absolute protein quantification using mass spectrometry (MS)-based proteomics delivers protein concentrations or copy numbers per cell. Existing methodologies typically require a combination of isotope-labeled spike-in references, cell counting, and protein concentration measurements. Here we present a novel method that delivers similar quantitative results directly from deep eukaryotic proteome datasets without any additional experimental steps. We show that the MS signal of histones can be used as a "proteomic ruler" because it is proportional to the amount of DNA in the sample, which in turn depends on the number of cells. As a result, our proteomic ruler approach adds an absolute scale to the MS readout and allows estimation of the copy numbers of individual proteins per cell. We compare our protein quantifications with values derived via the use of stable isotope labeling by amino acids in cell culture and protein epitope signature tags in a method that combines spike-in protein fragment standards with precise isotope label quantification. The proteomic ruler approach yields quantitative readouts that are in remarkably good agreement with results from the precision method. We attribute this surprising result to the fact that the proteomic ruler approach omits error-prone steps such as cell counting or protein concentration measurements. The proteomic ruler approach is readily applicable to any deep eukaryotic proteome dataset-even in retrospective analysis-and we demonstrate its usefulness with a series of mouse organ proteomes.

  19. Whey protein concentrate market enhancement. Final report

    SciTech Connect

    Hudson, L.

    1982-09-01

    Whey protein concentrate (WPC) was studied to see whether or not there was sufficient depth in the marketplace to accommodate increased WPC production in the event more whey was converted into alcohol. It was concluded that the current market for WPC is still immature and ample room exists in the marketplace to produce and dispose of WPC. In addition, WPC literature was reviewed so as to evaluate the current state of the art producing WPC. Considerable evidence suggests that more product formulation work is needed to move WPC into the general marketplace. Concurrent to the market and ltierature study WPC was incorporated into select categories of foods where finished goods were enhanced by having WPC incorporated in their formulations. Formulations were produced to demonstrate the fact that products such as ice cream, breedings and batters for fish sticks, and orange juice can be enhanced by using WPC.

  20. Sterile Filtration of Highly Concentrated Protein Formulations: Impact of Protein Concentration, Formulation Composition, and Filter Material.

    PubMed

    Allmendinger, Andrea; Mueller, Robert; Huwyler, Joerg; Mahler, Hanns-Christian; Fischer, Stefan

    2015-10-01

    Differences in filtration behavior of concentrated protein formulations were observed during aseptic drug product manufacturing of biologics dependent on formulation composition. The present study investigates filtration forces of monoclonal antibody formulations in a small-scale set-up using polyvinylidene difluoride (PVDF) or polyethersulfone (PES) filters. Different factors like formulation composition and protein concentration related to differences in viscosity, as well as different filtration rates were evaluated. The present study showed that filtration behavior was influenced by the presence or absence of a surfactant in the formulation, which defines the interaction between filter membrane and surface active formulation components. This can lead to a change in filter resistance (PES filter) independent on the buffer system used. Filtration behavior was additionally defined by rheological non-Newtonian flow behavior. The data showed that high shear rates resulting from small pore sizes and filtration pressure up to 1.0 bar led to shear-thinning behavior for highly concentrated protein formulations. Differences in non-Newtonian behavior were attributed to ionic strength related to differences in repulsive and attractive interactions. The present study showed that the interplay of formulation composition, filter material, and filtration rate can explain differences in filtration behavior/filtration flux observed for highly concentrated protein formulations thus guiding filter selection.

  1. Sterile Filtration of Highly Concentrated Protein Formulations: Impact of Protein Concentration, Formulation Composition, and Filter Material.

    PubMed

    Allmendinger, Andrea; Mueller, Robert; Huwyler, Joerg; Mahler, Hanns-Christian; Fischer, Stefan

    2015-10-01

    Differences in filtration behavior of concentrated protein formulations were observed during aseptic drug product manufacturing of biologics dependent on formulation composition. The present study investigates filtration forces of monoclonal antibody formulations in a small-scale set-up using polyvinylidene difluoride (PVDF) or polyethersulfone (PES) filters. Different factors like formulation composition and protein concentration related to differences in viscosity, as well as different filtration rates were evaluated. The present study showed that filtration behavior was influenced by the presence or absence of a surfactant in the formulation, which defines the interaction between filter membrane and surface active formulation components. This can lead to a change in filter resistance (PES filter) independent on the buffer system used. Filtration behavior was additionally defined by rheological non-Newtonian flow behavior. The data showed that high shear rates resulting from small pore sizes and filtration pressure up to 1.0 bar led to shear-thinning behavior for highly concentrated protein formulations. Differences in non-Newtonian behavior were attributed to ionic strength related to differences in repulsive and attractive interactions. The present study showed that the interplay of formulation composition, filter material, and filtration rate can explain differences in filtration behavior/filtration flux observed for highly concentrated protein formulations thus guiding filter selection. PMID:26149748

  2. Relationship between asparagine metabolism and protein concentration in soybean seed

    Technology Transfer Automated Retrieval System (TEKTRAN)

    The relationship between asparagine metabolism and protein concentration was investigated in soybean seed. Phenotyping of a population of recombinant inbred lines adapted to Illinois confirmed a positive correlation between free asparagine levels in developing seeds and protein concentration at matu...

  3. Absolute measurement of cerebral optical coefficients, hemoglobin concentration and oxygen saturation in old and young adults with near-infrared spectroscopy

    Technology Transfer Automated Retrieval System (TEKTRAN)

    We present near-infrared spectroscopy measurement of absolute cerebral hemoglobin concentration and saturation in a large sample of 36 healthy elderly (mean age, 85 ± 6 years) and 19 young adults (mean age, 28 ± 4 years). Non-invasive measurements were obtained on the forehead using a commercially a...

  4. 21 CFR 172.385 - Whole fish protein concentrate.

    Code of Federal Regulations, 2013 CFR

    2013-04-01

    ... 21 Food and Drugs 3 2013-04-01 2013-04-01 false Whole fish protein concentrate. 172.385 Section... HUMAN CONSUMPTION Special Dietary and Nutritional Additives § 172.385 Whole fish protein concentrate. The food additive whole fish protein concentrate may be safely used as a food supplement in...

  5. 21 CFR 172.385 - Whole fish protein concentrate.

    Code of Federal Regulations, 2012 CFR

    2012-04-01

    ... 21 Food and Drugs 3 2012-04-01 2012-04-01 false Whole fish protein concentrate. 172.385 Section... HUMAN CONSUMPTION Special Dietary and Nutritional Additives § 172.385 Whole fish protein concentrate. The food additive whole fish protein concentrate may be safely used as a food supplement in...

  6. 21 CFR 172.385 - Whole fish protein concentrate.

    Code of Federal Regulations, 2011 CFR

    2011-04-01

    ... 21 Food and Drugs 3 2011-04-01 2011-04-01 false Whole fish protein concentrate. 172.385 Section... HUMAN CONSUMPTION Special Dietary and Nutritional Additives § 172.385 Whole fish protein concentrate. The food additive whole fish protein concentrate may be safely used as a food supplement in...

  7. Novel isotopic N, N-dimethyl leucine (iDiLeu) reagents enable absolute quantification of peptides and proteins using a standard curve approach

    PubMed Central

    Greer, Tyler; Lietz, Christopher B.; Xiang, Feng; Li, Lingjun

    2014-01-01

    Absolute quantification of protein targets using liquid chromatography-mass spectrometry (LC-MS) is a key component of candidate biomarker validation. One popular method combines multiple reaction monitoring (MRM) using a triple quadrupole instrument with stable isotope-labeled standards (SIS) for absolute quantification (AQUA). LC-MRM AQUA assays are sensitive and specific, but they are also expensive due to the cost of synthesizing stable isotope peptide standards. While the chemical modification approach using Mass Differential Tags for Relative and Absolute Quantification (mTRAQ) represents a more economical approach when quantifying large numbers of peptides, these reagents are costly and still suffer from lower throughput because only two concentration values per peptide can be obtained in a single LC-MS run. Here, we have developed and applied a set of five novel mass difference reagents, isotopic N,N-dimethyl leucine (iDiLeu). These labels contain an amine reactive group, triazine ester, are cost effective due to their synthetic simplicity, and have increased throughput compared to previous LC-MS quantification methods by allowing construction of a four-point standard curve in one run. iDiLeu-labeled peptides show remarkably similar retention time shifts, slightly lower energy thresholds for higher-energy collisional dissociation (HCD) fragmentation, and high quantification accuracy for trypsin-digested protein samples (median errors <15%). By spiking in an iDiLeu-labeled neuropeptide, allatostatin, into mouse urine matrix, two quantification methods are validated. The first uses one labeled peptide as an internal standard to normalize labeled peptide peak areas across runs (<19% error) while the second enables standard curve creation and analyte quantification in one run (<8% error). PMID:25377360

  8. 21 CFR 172.385 - Whole fish protein concentrate.

    Code of Federal Regulations, 2014 CFR

    2014-04-01

    ... 21 Food and Drugs 3 2014-04-01 2014-04-01 false Whole fish protein concentrate. 172.385 Section... Nutritional Additives § 172.385 Whole fish protein concentrate. The food additive whole fish protein...) The additive is derived from whole, wholesome hake and hakelike fish, herring of the genera...

  9. The revised human liver cytochrome P450 "Pie": absolute protein quantification of CYP4F and CYP3A enzymes using targeted quantitative proteomics.

    PubMed

    Michaels, Scott; Wang, Michael Zhuo

    2014-08-01

    The CYP4F subfamily of enzymes has been identified recently to be involved in the metabolism of endogenous compounds (arachidonic acid and leukotriene B4), nutrients (vitamins K1 and E), and xenobiotics (pafuramidine and fingolimod). CYP4F2 and CYP4F3B are reported to be expressed in the human liver. However, absolute concentrations of these enzymes in human liver microsomes (HLMs) and their interindividual variability have yet to be determined because of the lack of specific antibodies. Here, an liquid chromatography with tandem mass spectrometry (LC-MS/MS)-based targeted quantitative proteomic approach was employed to determine the absolute protein concentrations of CYP4F2 and CYP4F3B compared with CYP3A in two panels of HLMs (n = 31). As a result, the human hepatic cytochrome P450 (P450) "pie" has been revised to include the contribution of CYP4F enzymes, which amounts to 15% of the total hepatic cytochrome P450 enzymes. CYP4F3B displayed low interindividual variability (3.3-fold) in the HLM panels whereas CYP4F2 displayed large variability (21-fold). However, CYP4F2 variability decreased to 3.4-fold if the two donors with the lowest expression were excluded. In contrast, CYP3A exhibited 29-fold interindividual variability in the same HLM panels. The proposed marker reaction for CYP4F enzymes pafuramidine/DB289 M1 formation did not correlate with CYP4F protein content, suggesting alternate metabolic pathways for DB289 M1 formation in HLMs. In conclusion, CYP4F enzymes are highly expressed in the human liver and their physiologic and pharmacologic roles warrant further investigation.

  10. Absolute quantification of protein and post-translational modification abundance with stable isotope–labeled synthetic peptides

    PubMed Central

    Kettenbach, Arminja N; Rush, John; Gerber, Scott A

    2013-01-01

    In the analysis of biological systems, it is of interest to identify the components of the system and to monitor their changes in abundance under different conditions. The AQUA (for ‘absolute quantification’) method allows sensitive and specific targeted quantification of protein and post-translational modifications in complex protein mixtures using stable isotope–labeled peptides as internal standards. Each AQUA experiment is composed of two stages: method development and application to a biological scenario. In the method development stage, peptides from the protein of interest are chosen and then synthesized with stable isotopes such as 13C, 2H or 15N. The abundance of these internal standards and their endogenous counterparts can be measured by mass spectrometry with selected reaction monitoring or selected ion monitoring methods. Once an AQUA method is established, it can be rapidly applied to a wide range of biological samples, from tissue culture cells to human plasma and tissue. After AQUA peptide synthesis, the development, optimization and application of AQUA analyses to a specific biological problem can be achieved in ~1 week. Here we demonstrate the usefulness of this method by monitoring both Polo-like kinase 1 (Plk1) protein abundance in multiple lung cancer cell lines and the extent of Plk1 activation loop phosphorylation (pThr-210) during release from S phase. PMID:21293459

  11. Absolute quantification of norovirus capsid protein in food, water, and soil using synthetic peptides with electrospray and MALDI mass spectrometry.

    PubMed

    Hartmann, Erica M; Colquhoun, David R; Schwab, Kellogg J; Halden, Rolf U

    2015-04-01

    Norovirus infections are one of the most prominent public health problems of microbial origin in the U.S. and other industrialized countries. Surveillance is necessary to prevent secondary infection, confirm successful cleanup after outbreaks, and track the causative agent. Quantitative mass spectrometry, based on absolute quantitation with stable-isotope labeled peptides, is a promising tool for norovirus monitoring because of its speed, sensitivity, and robustness in the face of environmental inhibitors. In the current study, we present two new methods for the detection of the norovirus genogroup I capsid protein using electrospray and matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. The peptide TLDPIEVPLEDVR was used to quantify norovirus-like particles down to 500 attomoles with electrospray and 100 attomoles with MALDI. With MALDI, we also demonstrate a detection limit of 1 femtomole and a quantitative dynamic range of 5 orders of magnitude in the presence of an environmental matrix effect. Due to the rapid processing time and applicability to a wide range of environmental sample types (bacterial lysate, produce, milk, soil, and groundwater), mass spectrometry-based absolute quantitation has a strong potential for use in public health and environmental sciences.

  12. Absolute Quantification of Norovirus Capsid Protein in Food, Water, and Soil Using Synthetic Peptides with Electrospray and MALDI Mass Spectrometry

    PubMed Central

    Hartmann, Erica M.; Colquhoun, David R.; Schwab, Kellogg J.; Halden, Rolf U.

    2015-01-01

    Norovirus infections are one of the most prominent public health problems of microbial origin in the U.S. and other industrialized countries. Surveillance is necessary to prevent secondary infection, confirm successful cleanup after outbreaks, and track the causative agent. Quantitative mass spectrometry, based on absolute quantitation with stable-isotope labeled peptides, is a promising tool for norovirus monitoring because of its speed, sensitivity, and robustness in the face of environmental inhibitors. In the current study, we present two new methods for the detection of the norovirus genogroup I capsid protein using electrospray and matrixassisted laser desorption/ionization (MALDI) mass spectrometry. The peptide TLDPIEVPLEDVR was used to quantify norovirus-like particles down to 500 attomoles with electrospray and 100 attomoles with MALDI. With MALDI, we also demonstrate a detection limit of 1 femtomole and a quantitative dynamic range of 5 orders of magnitude in the presence of an environmental matrix effect. Due to the rapid processing time and applicability to a wide range of environmental sample types (bacterial lysate, produce, milk, soil, and groundwater), mass spectrometry-based absolute quantitation has a strong potential for use in public health and environmental sciences. PMID:25603302

  13. Improved method for measuring absolute O2(a1Δg) concentration by O2(a1Δg-->X3Σg-) IR radiation

    NASA Astrophysics Data System (ADS)

    Deng, Liezheng; Shi, Wenbo; Yang, Heping; Sha, Guohe; Zhang, Cunhao

    2004-11-01

    We describe an improved technique for measuring the absolute O2(a1Δ) concentration via the quantitative determination of IR radiation from O2(a1Δg→X3Σg-) transition. An exact geometrical optical model was first established, in which the influence of reflection and refraction on the radiation characteristics of a luminous volume source was given full consideration, making possible the accurate calculation of the coupling efficiency between the volume source and a receiving area. Then, an IR radiation receiving apparatus (IRRRA) was constructed and its responsivity (mV/W) to the power of IR radiation calibrated by a tungsten standard lamp. An optical detection system was, in turn, built according to the optical model with fine alignment between the IRRRA and an optical cell. We then demonstrate the procedure to obtain the absolute concentration of O2(a1Δ) flowing through the optical cell from a jet singlet oxygen generator from the signal of the IRRRA, the optical cell volume, and the coupling efficiency between the cell and the IRRRA. Moreover, to verify the accuracy of this method, the absolute O2(a1Δ) concentration was compared to that measured by an established isothermal calorimetry method. Based on the comparison of the O2(a1Δ) concentrations determined by the two methods, the Einstein A-coefficient was estimated as (2.70±0.84)×10-4 s-1, which agrees with Badger's value of 2.58×10-4, Špalek's of 2.24×10-4, Newman's of 2.19×10-4, and Miller's of 2.3×10-4 within the uncertainty of the experimental techniques. The method advanced in this article is worthwhile for the measurement of absolute O2(a1Δ) concentration in a chemical oxygen iodine laser or a singlet oxygen generator. It can also provide a general technique for the measurement of absolute concentrations of long-lifetime luminous species other than O2(a1Δ).

  14. 21 CFR 184.1979c - Whey protein concentrate.

    Code of Federal Regulations, 2010 CFR

    2010-04-01

    ...) FOOD FOR HUMAN CONSUMPTION (CONTINUED) DIRECT FOOD SUBSTANCES AFFIRMED AS GENERALLY RECOGNIZED AS SAFE Listing of Specific Substances Affirmed as GRAS § 184.1979c Whey protein concentrate. (a) Whey protein concentrate is the substance obtained by the removal of sufficient nonprotein constituents from whey so...

  15. Absolute concentrations of highly vibrationally excited OH(υ = 9 + 8) in the mesopause region derived from the TIMED/SABER instrument

    NASA Astrophysics Data System (ADS)

    Mast, Jeffrey; Mlynczak, Martin G.; Hunt, Linda A.; Marshall, B. Thomas; Mertens, Christoper J.; Russell, James M.; Thompson, R. Earl; Gordley, Larry L.

    2013-02-01

    Abstract <span class="hlt">Absolute</span> <span class="hlt">concentrations</span> (cm-3) of highly vibrationally excited hydroxyl (OH) are derived from measurements of the volume emission rate of the υ = 9 + 8 states of the OH radical made by the SABER instrument on the TIMED satellite. SABER has exceptionally sensitive measurement precision that corresponds to an ability to detect changes in volume emission rate on the order of ~5 excited OH molecules per cm3. Peak zonal annual mean <span class="hlt">concentrations</span> observed by SABER exceed 1000 cm-3 at night and 225 cm-3 during the day. Measurements since 2002 show an apparent altitude-dependent variation of the night OH(υ = 9 + 8) <span class="hlt">concentrations</span> with the 11 year solar cycle, with <span class="hlt">concentrations</span> decreasing below ~ 95 km from 2002 to 2008. These observations provide a global database for evaluating photochemical model computations of OH abundance, reaction kinetics, and rates and mechanisms responsible for maintaining vibrationally excited OH in the mesopause region.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2012JBO....17h1406H','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2012JBO....17h1406H"><span id="translatedtitle"><span class="hlt">Absolute</span> measurement of cerebral optical coefficients, hemoglobin <span class="hlt">concentration</span> and oxygen saturation in old and young adults with near-infrared spectroscopy</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Hallacoglu, Bertan; Sassaroli, Angelo; Wysocki, Michael; Guerrero-Berroa, Elizabeth; Schnaider Beeri, Michal; Haroutunian, Vahram; Shaul, Merav; Rosenberg, Irwin H.; Troen, Aron M.; Fantini, Sergio</p> <p>2012-08-01</p> <p>We present near-infrared spectroscopy measurement of <span class="hlt">absolute</span> cerebral hemoglobin <span class="hlt">concentration</span> and saturation in a large sample of 36 healthy elderly (mean age, 85±6 years) and 19 young adults (mean age, 28±4 years). Non-invasive measurements were obtained on the forehead using a commercially available multi-distance frequency-domain system and analyzed using a diffusion theory model for a semi-infinite, homogeneous medium with semi-infinite boundary conditions. Our study included repeat measurements, taken five months apart, on 16 elderly volunteers that demonstrate intra-subject reproducibility of the <span class="hlt">absolute</span> measurements with cross-correlation coefficients of 0.9 for absorption coefficient (μa), oxy-hemoglobin <span class="hlt">concentration</span> ([HbO2]), and total hemoglobin <span class="hlt">concentration</span> ([HbT]), 0.7 for deoxy-hemoglobin <span class="hlt">concentration</span> ([Hb]), 0.8 for hemoglobin oxygen saturation (StO2), and 0.7 for reduced scattering coefficient (). We found significant differences between the two age groups. Compared to young subjects, elderly subjects had lower cerebral [HbO2], [Hb], [HbT], and StO2 by 10±4 μM, 4±3 μM, 14±5 μM, and 6%±5%, respectively. Our results demonstrate the reliability and robustness of multi-distance near-infrared spectroscopy measurements based on a homogeneous model in the human forehead on a large sample of human subjects. <span class="hlt">Absolute</span>, non-invasive optical measurements on the brain, such as those presented here, can significantly advance the development of NIRS technology as a tool for monitoring resting/basal cerebral perfusion, hemodynamics, oxygenation, and metabolism.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26139249','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26139249"><span id="translatedtitle">Methods to <span class="hlt">Concentrate</span> <span class="hlt">Proteins</span> for <span class="hlt">Protein</span> Isolation, Proteomic, and Peptidomic Evaluation.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Goldring, J P Dean</p> <p>2015-01-01</p> <p>In <span class="hlt">protein</span> isolation, proteomic, or peptidomic procedures, <span class="hlt">protein</span> solutions are often <span class="hlt">concentrated</span> to remove solvents and undesirable molecules, to separate <span class="hlt">protein</span> fractions or to increase <span class="hlt">protein</span> <span class="hlt">concentrations</span>. <span class="hlt">Proteins</span> can be <span class="hlt">concentrated</span> by precipitation from solution with ammonium sulfate, polyethylene glycol, organic solvent, trichloroacetic acid, potassium chloride/sodium dodecyl sulfate, and three-phase partitioning. Solvents can be removed by passage through a semipermeable barrier where <span class="hlt">protein</span> solutions are forced against the barrier in a centrifuge tube or with increased pressure <span class="hlt">concentrating</span> <span class="hlt">protein</span> in the remaining solution. The semipermeable barrier can be surrounded by a hygroscopic reagent to draw the solvent across the membrane. <span class="hlt">Proteins</span> can be <span class="hlt">concentrated</span> by freeze-drying (lyophilization). All these methods to <span class="hlt">concentrate</span> <span class="hlt">proteins</span> are discussed.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/18465883','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/18465883"><span id="translatedtitle">Towards <span class="hlt">absolute</span> quantification of therapeutic monoclonal antibody in serum by LC-MS/MS using isotope-labeled antibody standard and <span class="hlt">protein</span> cleavage isotope dilution mass spectrometry.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Heudi, Olivier; Barteau, Samuel; Zimmer, Dieter; Schmidt, Joerg; Bill, Kurt; Lehmann, Natalie; Bauer, Christian; Kretz, Olivier</p> <p>2008-06-01</p> <p>Although LC-MS methods are increasingly used for the <span class="hlt">absolute</span> quantification of <span class="hlt">proteins</span>, the lack of appropriate internal standard (IS) hinders the development of rapid and standardized analytical methods for both in vitro and in vivo studies. Here, we have developed a novel method for the <span class="hlt">absolute</span> quantification of a therapeutic <span class="hlt">protein</span>, which is monoclonal antibody (mAb). The method combines liquid chromatography tandem mass spectrometry (LC-MS/MS) and <span class="hlt">protein</span> cleavage isotope dilution mass spectrometry with the isotope-labeled mAb as IS. The latter was identical to the analyzed mAb with the exception that each threonine contains four (13)C atoms and one (15)N atom. Serum samples were spiked with IS prior to the overnight trypsin digestion and subsequent sample cleanup. Sample extracts were analyzed on a C18 ACE column (150 mm x 4.6 mm) using an LC gradient time of 11 min. Endogenous mAb <span class="hlt">concentrations</span> were determined by calculating the peak height ratio of its signature peptide to the corresponding isotope-labeled peptide. The linear dynamic range was established between 5.00 and 1000 microg/mL mAb with accuracy and precision within +/-15% at all <span class="hlt">concentrations</span> and below +/-20% at the LLOQ (lower limit of quantification). The overall method recovery in terms of mAb was 14%. The losses due to sample preparation (digestion and purification) were 72% from which about 32% was due to the first step of the method, the sample digestion. This huge loss during sample preparation strongly emphasizes the necessity to employ an IS right from the beginning. Our method was successfully applied to the mAb quantification in marmoset serum study samples, and the precision obtained on duplicate samples was, in most cases, below 20%. The comparison with enzyme-linked immunosorbent assay (ELISA) showed higher exposure in terms of AUC and Cmax with the LC-MS/MS method. Possible reasons for this discrepancy are discussed in this study. The results of this study indicate that our LC</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=297213','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=297213"><span id="translatedtitle">Influence of Bleaching on Flavor of 34% Whey <span class="hlt">Protein</span> <span class="hlt">Concentrate</span> and Residual Benzoic Acid <span class="hlt">Concentration</span> in Dried Whey <span class="hlt">Proteins</span></span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>Previous studies have shown that bleaching negatively affects the flavor of 70% whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC70), but bleaching effects on lower-<span class="hlt">protein</span> products have not been established. Benzoyl peroxide (BP), a whey bleaching agent, degrades to benzoic acid (BA) and may elevate BA <span class="hlt">concentrations</span>...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1189533','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1189533"><span id="translatedtitle">Study of the effect of total serum <span class="hlt">protein</span> and albumin <span class="hlt">concentrations</span> on canine fructosamine <span class="hlt">concentration</span>.</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Loste, A; Marca, M C</p> <p>1999-01-01</p> <p>The relationship among serum fructosamine <span class="hlt">concentration</span> and total serum <span class="hlt">protein</span> and albumin <span class="hlt">concentrations</span> were evaluated in healthy and sick dogs (diabetics and dogs with insulinoma were not included). Fructosamine was determined using a commercial colorimetric nitroblue tetrazolium method applied to the Technicon RA-500 (Bayer). Serum fructosamine <span class="hlt">concentration</span> was not correlated to total <span class="hlt">protein</span> in normoproteinemic (r = 0.03) and hyperproteinemic dogs (r = 0.29), but there was a high correlation (r = 0.73) in hypoproteinemic dogs. Similar comparison between serum fructosamine and albumin <span class="hlt">concentrations</span> showed middle correlation (r = 0.49) in normoalbuminemic dogs and high degree of correlation (r = 0.67) in hypoalbuminemic dogs. These results showed the importance of recognizing serum glucose <span class="hlt">concentration</span> as well as total serum <span class="hlt">protein</span> and albumin <span class="hlt">concentrations</span> in the assay of canine serum fructosamine <span class="hlt">concentration</span>. PMID:10369572</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_1");'>1</a></li> <li><a href="#" onclick='return showDiv("page_2");'>2</a></li> <li class="active"><span>3</span></li> <li><a href="#" onclick='return showDiv("page_4");'>4</a></li> <li><a href="#" onclick='return showDiv("page_5");'>5</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_3 --> <div id="page_4" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_2");'>2</a></li> <li><a href="#" onclick='return showDiv("page_3");'>3</a></li> <li class="active"><span>4</span></li> <li><a href="#" onclick='return showDiv("page_5");'>5</a></li> <li><a href="#" onclick='return showDiv("page_6");'>6</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="61"> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/24423263','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/24423263"><span id="translatedtitle">Quantification of <span class="hlt">protein</span> <span class="hlt">concentration</span> using UV absorbance and Coomassie dyes.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Noble, James E</p> <p>2014-01-01</p> <p>The measurement of a solubilized <span class="hlt">protein</span> <span class="hlt">concentration</span> in solution is an important assay in biochemistry research and development labs for applications ranging from enzymatic studies to providing data for biopharmaceutical lot release. Spectrophotometric <span class="hlt">protein</span> quantification assays are methods that use UV and visible spectroscopy to rapidly determine the <span class="hlt">concentration</span> of <span class="hlt">protein</span>, relative to a standard, or using an assigned extinction coefficient. Where multiple samples need measurement, and/or the sample volume and <span class="hlt">concentration</span> is limited, preparations of the Coomassie dye commonly known as the Bradford assay can be used. PMID:24423263</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26211901','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26211901"><span id="translatedtitle">Calculation of injection forces for highly <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Fischer, Ingo; Schmidt, Astrid; Bryant, Andrew; Besheer, Ahmed</p> <p>2015-09-30</p> <p><span class="hlt">Protein</span> solutions often manifest a high viscosity at high solution <span class="hlt">concentrations</span>, thus impairing injectability. Accordingly, accurate prediction of the injection force based on solution viscosity can greatly support <span class="hlt">protein</span> formulation and device development. In this study, the shear-dependent viscosity of three <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions is reported, and calculated injection forces obtained by two different mathematical models are compared against measured values. The results show that accurate determination of the needle dimensions and the shear-thinning behavior of the <span class="hlt">protein</span> solutions is vital for injection force prediction. Additionally, one model delivered more accurate results, particularly for solutions with prominent shear-thinning behavior.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4256500','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4256500"><span id="translatedtitle">A “Proteomic Ruler” for <span class="hlt">Protein</span> Copy Number and <span class="hlt">Concentration</span> Estimation without Spike-in Standards*</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Wiśniewski, Jacek R.; Hein, Marco Y.; Cox, Jürgen; Mann, Matthias</p> <p>2014-01-01</p> <p><span class="hlt">Absolute</span> <span class="hlt">protein</span> quantification using mass spectrometry (MS)-based proteomics delivers <span class="hlt">protein</span> <span class="hlt">concentrations</span> or copy numbers per cell. Existing methodologies typically require a combination of isotope-labeled spike-in references, cell counting, and <span class="hlt">protein</span> <span class="hlt">concentration</span> measurements. Here we present a novel method that delivers similar quantitative results directly from deep eukaryotic proteome datasets without any additional experimental steps. We show that the MS signal of histones can be used as a “proteomic ruler” because it is proportional to the amount of DNA in the sample, which in turn depends on the number of cells. As a result, our proteomic ruler approach adds an <span class="hlt">absolute</span> scale to the MS readout and allows estimation of the copy numbers of individual <span class="hlt">proteins</span> per cell. We compare our <span class="hlt">protein</span> quantifications with values derived via the use of stable isotope labeling by amino acids in cell culture and <span class="hlt">protein</span> epitope signature tags in a method that combines spike-in <span class="hlt">protein</span> fragment standards with precise isotope label quantification. The proteomic ruler approach yields quantitative readouts that are in remarkably good agreement with results from the precision method. We attribute this surprising result to the fact that the proteomic ruler approach omits error-prone steps such as cell counting or <span class="hlt">protein</span> <span class="hlt">concentration</span> measurements. The proteomic ruler approach is readily applicable to any deep eukaryotic proteome dataset—even in retrospective analysis—and we demonstrate its usefulness with a series of mouse organ proteomes. PMID:25225357</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2014SPIE.9268E..0VC','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2014SPIE.9268E..0VC"><span id="translatedtitle">Mapping the microvascular and the associated <span class="hlt">absolute</span> values of oxy-hemoglobin <span class="hlt">concentration</span> through turbid media via local off-set diffuse optical imaging</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Chen, Chen; Klämpfl, Florian; Stelzle, Florian; Schmidt, Michael</p> <p>2014-11-01</p> <p>An imging resolution of micron-scale has not yet been discovered by diffuse optical imaging (DOI), while a superficial response was eliminated. In this work, we report on a new approach of DOI with a local off-set alignment to subvert the common boundary conditions of the modified Beer-Lambert Law (MBLL). It can resolve a superficial target in micron scale under a turbid media. To validate both major breakthroughs, this system was used to recover a subsurface microvascular mimicking structure under an skin equivalent phantom. This microvascular was included with oxy-hemoglobin solution in variant <span class="hlt">concentrations</span> to distiguish the <span class="hlt">absolute</span> values of CtRHb and CtHbO2 . Experimental results confirmed the feasibility of recovering the target vascular of 50 µm in diameter, and graded the values of the <span class="hlt">concentrations</span> of oxy-hemoglobin from 10 g/L to 50 g/L <span class="hlt">absolutely</span>. Ultimately, this approach could evolve into a non-invasive imaging system to map the microvascular pattern and the associated oximetry under a human skin in-vivo.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2012ApPhB.108..393M','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2012ApPhB.108..393M"><span id="translatedtitle"><span class="hlt">Absolute</span> OH <span class="hlt">concentration</span> profiles measurements in high pressure counterflow flames by coupling LIF, PLIF, and absorption techniques</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Matynia, A.; Idir, M.; Molet, J.; Roche, C.; de Persis, S.; Pillier, L.</p> <p>2012-08-01</p> <p>A high-pressure combustion chamber enclosing counterflow burners was set-up at ICARE-CNRS laboratory. It allows the stabilization of flat twin premixed flames at atmospheric and high pressure. In this study, lean and stoichiometric methane/air counterflow premixed flames were studied at various pressures (0.1 MPa to 0.7 MPa). Relative OH <span class="hlt">concentration</span> profiles were measured by Laser Induced Fluorescence. Great care was attached to the determination of the fluorescence signal by taking into account the line broadening and deexcitation by quenching which both arise at high pressure. Subsequently, OH profiles were calibrated in <span class="hlt">concentration</span> by laser absorption technique associated with planar laser induced fluorescence. Results are successfully compared with literature. The good quality of the results attests of the experimental set-up ability to allow the study of flame structure at high pressure.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/15738219','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/15738219"><span id="translatedtitle">Physical properties of ice cream containing milk <span class="hlt">protein</span> <span class="hlt">concentrates</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Alvarez, V B; Wolters, C L; Vodovotz, Y; Ji, T</p> <p>2005-03-01</p> <p>Two milk <span class="hlt">protein</span> <span class="hlt">concentrates</span> (MPC, 56 and 85%) were studied as substitutes for 20 and 50% of the <span class="hlt">protein</span> content in ice cream mix. The basic mix formula had 12% fat, 11% nonfat milk solids, 15% sweetener, and 0.3% stabilizer/emulsifier blend. <span class="hlt">Protein</span> levels remained constant, and total solids were compensated for in MPC mixes by the addition of polydextrose. Physical properties investigated included apparent viscosity, fat globule size, melting rate, shape retention, and freezing behavior using differential scanning calorimetry. Milk <span class="hlt">protein</span> <span class="hlt">concentrate</span> formulations had higher mix viscosity, larger amount of fat destabilization, narrower ice melting curves, and greater shape retention compared with the control. Milk <span class="hlt">protein</span> <span class="hlt">concentrates</span> did not offer significant modifications of ice cream physical properties on a constant <span class="hlt">protein</span> basis when substituted for up to 50% of the <span class="hlt">protein</span> supplied by nonfat dry milk. Milk <span class="hlt">protein</span> <span class="hlt">concentrates</span> may offer ice cream manufacturers an alternative source of milk solids non-fat, especially in mixes reduced in lactose or fat, where higher milk solids nonfat are needed to compensate other losses of total solids.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=311660','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=311660"><span id="translatedtitle">Behavior of whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> under extreme storage conditions</span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>The overseas demand for whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> (WPC) has increased steadily in recent years. Emergency aid foods often include WPC, but shelf-life studies of whey <span class="hlt">proteins</span> under different shipment and storage conditions have not been conducted in the last 50 yr. Microbial quality, compound form...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/biblio/7124206','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/biblio/7124206"><span id="translatedtitle">Preparation of <span class="hlt">protein</span> <span class="hlt">concentrates</span> from whey and seed products</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>Saunders, R.M.; Kohler, G.O.</p> <p>1980-01-01</p> <p>Whey is mixed with a seed product (e.g., cereal, legumes, oil seeds, flour, etc.) and the pH of the mixture adjusted to 9-10. The resultant mixture is treated to separate a juice from the fibrous residue; in a preferred embodiment of the subsequent process, a <span class="hlt">protein</span> <span class="hlt">concentrate</span> is recovered from the juice by adding an acid to it to adjust the pH to 3-4 and subsequently adding sodium hexametaphosphate in an amount sufficient to precipitate the <span class="hlt">protein</span> product. After adjustment of the pH to 7, a <span class="hlt">protein</span> <span class="hlt">concentrate</span> may be obtained by drying the alkaline extract.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/3343935','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/3343935"><span id="translatedtitle">Pleural <span class="hlt">protein</span> <span class="hlt">concentration</span> and liquid volume in spontaneously hypertensive rats.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Lai-Fook, S J; Kaplowitz, M R</p> <p>1988-01-01</p> <p>To determine the effect of systemic vascular hypertension on fluid balance in the pleural space, we studied the spontaneously hypertensive rat (SHR) and its genetic normotensive control, the Wistar-Kyoto rat (WKY). We measured arterial and venous pressures, total <span class="hlt">protein</span> and albumin <span class="hlt">concentrations</span> of pleural liquid and plasma, pleural space thickness, and pleural surface pressure in SHR and WKY that were matched for weight (260-300 g). <span class="hlt">Protein</span> <span class="hlt">concentration</span> was measured by a manual Biuret test and albumin <span class="hlt">concentration</span> was measured by the bromcresol green colorimetric method. Pleural liquid thickness was measured in situ using light microscopy. Pleural surface pressure was assumed to equal pleural liquid pressure. In the SHR, total <span class="hlt">protein</span> and albumin <span class="hlt">concentrations</span> in pleural liquid were lower than in WKY, and pleural space thickness was larger in SHR than in WKY. These results are consistent with a higher capillary pressure and greater fluid filtration in SHR.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=322379','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=322379"><span id="translatedtitle">The relationship between peritubular capillary <span class="hlt">protein</span> <span class="hlt">concentration</span> and fluid reabsorption by the renal proximal tubule</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Brenner, Barry M.; Falchuk, Kenneth H.; Keimowitz, Robert I.; Berliner, Robert W.</p> <p>1969-01-01</p> <p>The relationship between peritubular capillary <span class="hlt">protein</span> <span class="hlt">concentration</span> and rate of sodium reabsorption by the rat proximal tubule was examined using free-flow recollection micropuncture techniques. Tubule fluid-to-plasma inulin ratios were measured before, during, and at successive intervals after brief (15-25 sec) intra-aortic injections (at the level of the renal artery) of colloid-free, isoncotic, and hyperoncotic solutions. Arterial hematocrit and <span class="hlt">protein</span> <span class="hlt">concentrations</span> were measured simultaneously in these rats. In other rats, total <span class="hlt">protein</span> <span class="hlt">concentration</span> of peritubular capillary blood plasma was determined before, during, and after these same infusions with a newly described submicroliter fiber-optic colorimeter. In the 15-25 sec interval necessary to infuse 2 ml of these test solutions, fractional and <span class="hlt">absolute</span> sodium reabsorption varied directly with peritubular capillary colloid osmotic pressure, declining during infusion of colloid-free solutions, increasing during hyperoncotic infusions, and remaining unchanged during isoncotic infusions. In the subsequent 20-min interval after intra-aortic injection of these test solutions, capillary <span class="hlt">protein</span> <span class="hlt">concentration</span> remained at (isoncotic infusions) or returned to (colloid-free and hyperoncotic fluids) control values. Whereas reabsorption after colloid-free solutions returned to base line levels in parallel with the return in capillary <span class="hlt">protein</span> <span class="hlt">concentration</span>, after colloid infusions (which resulted in continued expansion of extracellular fluid volume), a progressive decline in reabsorption was observed. These results afford strong evidence that peritubular capillary colloid osmotic pressure is one important determinant of proximal sodium reabsorption. Nevertheless it is apparent that mechanisms other than or in addition to this must be invoked to explain the delayed inhibition of reabsorption that accompanies expansion of extracellular fluid volume by colloid solutions. PMID:5796362</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27322723','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27322723"><span id="translatedtitle"><span class="hlt">Protein</span> abundance changes of Zygosaccharomyces rouxii in different sugar <span class="hlt">concentrations</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Guo, Hong; Niu, Chen; Liu, Bin; Wei, JianPing; Wang, HuXuan; Yuan, YaHong; Yue, TianLi</p> <p>2016-09-16</p> <p>Zygosaccharomyces rouxii is a yeast which can cause spoilage in the <span class="hlt">concentrated</span> juice industries. It exhibits resistance to high sugar <span class="hlt">concentrations</span> but genome- and proteome-wide studies on Z. rouxii in response to high sugar <span class="hlt">concentrations</span> have been poorly investigated. Herein, by using a 2-D electrophoresis based workflow, the proteome of a wild strain of Z. rouxii under different sugar <span class="hlt">concentrations</span> has been analyzed. <span class="hlt">Proteins</span> were extracted, quantified, and subjected to 2-DE analysis in the pH range 4-7. Differences in growth (lag phase), <span class="hlt">protein</span> content (13.97-19.23mg/g cell dry weight) and number of resolved spots (196-296) were found between sugar <span class="hlt">concentrations</span>. ANOVA test showed that 168 spots were different, and 47 spots, corresponding to 40 unique gene products have been identified. These <span class="hlt">protein</span> species are involved in carbohydrate and energy metabolism, amino acid metabolism, response to stimulus, <span class="hlt">protein</span> transport and vesicle organization, cell morphogenesis regulation, transcription and translation, nucleotide metabolism, amino-sugar nucleotide-sugar pathways, oxidoreductases balancing, and ribosome biogenesis. The present study provides important information about how Z. rouxii acts to cope with high sugar <span class="hlt">concentration</span> at molecular levels, which might enhance our global understanding of Z. rouxii's high sugar-tolerance trait. PMID:27322723</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4783657','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4783657"><span id="translatedtitle">Dependence of fluorescent <span class="hlt">protein</span> brightness on <span class="hlt">protein</span> <span class="hlt">concentration</span> in solution and enhancement of it</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Morikawa, Takamitsu J.; Fujita, Hideaki; Kitamura, Akira; Horio, Takashi; Yamamoto, Johtaro; Kinjo, Masataka; Sasaki, Akira; Machiyama, Hiroaki; Yoshizawa, Keiko; Ichimura, Taro; Imada, Katsumi; Nagai, Takeharu; Watanabe, Tomonobu M.</p> <p>2016-01-01</p> <p>Fluorescent <span class="hlt">proteins</span> have been widely used in biology because of their compatibility and varied applications in living specimens. Fluorescent <span class="hlt">proteins</span> are often undesirably sensitive to intracellular conditions such as pH and ion <span class="hlt">concentration</span>, generating considerable issues at times. However, harnessing these intrinsic sensitivities can help develop functional probes. In this study, we found that the fluorescence of yellow fluorescent <span class="hlt">protein</span> (YFP) depends on the <span class="hlt">protein</span> <span class="hlt">concentration</span> in the solution and that this dependence can be enhanced by adding a glycine residue in to the YFP; we applied this finding to construct an intracellular <span class="hlt">protein</span>-crowding sensor. A Förster resonance energy transfer (FRET) pair, involving a cyan fluorescent <span class="hlt">protein</span> (CFP) insensitive to <span class="hlt">protein</span> <span class="hlt">concentration</span> and a glycine-inserted YFP, works as a genetically encoded probe to evaluate intracellular crowding. By measuring the fluorescence of the present FRET probe, we were able to detect dynamic changes in <span class="hlt">protein</span> crowding in living cells. PMID:26956628</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/biblio/6340999','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/biblio/6340999"><span id="translatedtitle">An analyzer for the determination of <span class="hlt">protein</span> <span class="hlt">concentration</span> in corn</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>Nazarov, V.M.; Ostrovnaya, T.M.; Pavlov, S.S.; Sysoev, V.P. )</p> <p>1992-01-01</p> <p>A neutron capture gamma-ray analyzer has been constructed for rapid determination of <span class="hlt">protein</span> <span class="hlt">concentration</span> in corn. In contrast to the well-known methods of <span class="hlt">protein</span> determination (e.g., chemical method of Kjeldahl, infrared method), the present method uses large volume samples and does not require special sample preparation, thereby achieving a measurement time reduction by several times. The neutron capture gamma-ray analysis is based on the determination of nitrogen because the <span class="hlt">protein</span> <span class="hlt">concentration</span> is directly proportional to the nitrogen <span class="hlt">concentration</span> with different proportionality constant for different types of corn. Fast neutrons from a [sup 252]Cf neutron source are moderated by the corn itself to thermal energies. The measurement chamber is a sphere with double walls. The spherical annulus is filled with a biological shield. The sample is placed inside the inner sphere, and the neutron source is placed at the center of the sample sphere.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=191886','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=191886"><span id="translatedtitle">Poliovirus <span class="hlt">protein</span> 2BC increases cytosolic free calcium <span class="hlt">concentrations</span>.</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Aldabe, R; Irurzun, A; Carrasco, L</p> <p>1997-01-01</p> <p>Poliovirus-infected cells undergo an increase in cytoplasmic calcium <span class="hlt">concentrations</span> from the 4th h postinfection. The <span class="hlt">protein</span> responsible for this effect was identified by the expression of different poliovirus nonstructural <span class="hlt">proteins</span> in HeLa cells by using a recombinant vaccinia virus system. Synthesis of <span class="hlt">protein</span> 2BC enhances cytoplasmic calcium <span class="hlt">concentrations</span> in a manner similar to that observed in poliovirus-infected cells. To identify the regions in 2BC involved in modifying cytoplasmic calcium levels, several 2BC variants were generated. Regions present in both 2B and 2C are necessary to augment cellular free calcium levels. Therefore, in addition to inducing proliferation of membranous vesicles, poliovirus <span class="hlt">protein</span> 2BC also alters cellular calcium homeostasis. PMID:9223520</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/15747729','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/15747729"><span id="translatedtitle">Effect of <span class="hlt">protein</span> <span class="hlt">concentration</span>, pH, lactose content and pasteurization on thermal gelation of acid caprine whey <span class="hlt">protein</span> <span class="hlt">concentrates</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Bordenave-Juchereau, Stéphanie; Almeida, Bruno; Piot, Jean-Marie; Sannier, Frédéric</p> <p>2005-02-01</p> <p>The influence of pH (4.5-6.5), sodium chloride content (125-375 mM), calcium chloride content (10-30 mM), <span class="hlt">protein</span> <span class="hlt">concentration</span> (70-90 g/l) and lactose content on the gel hardness of goat whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (GWPC) in relation to the origin of the acid whey (raw or pasteurized milk) was studied using a factorial design. Gels were obtained after heat treatment (90 degrees C, 30 min). Gel hardness was measured using texture analyser. Only <span class="hlt">protein</span> <span class="hlt">concentration</span> and pH were found to have a statistically significant effect on the gel hardness. An increase in the <span class="hlt">protein</span> <span class="hlt">concentration</span> resulted in an increase in the gel hardness. GWPC containing 800g/kg <span class="hlt">protein</span> formed gels with a hardness maximum at the pHi, whereas GWPC containing 300 g/kg <span class="hlt">protein</span> did not form true gels. Whey from pasteurized milk formed softer gels than whey from raw milk. A high lactose content (approximately 360 g/kg) also reduced the gelation performance of GWPC. PMID:15747729</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/2260497','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/2260497"><span id="translatedtitle">Changes in the <span class="hlt">concentrations</span> of urinary <span class="hlt">proteins</span> after physical exercise.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Miyai, T; Ogata, M</p> <p>1990-10-01</p> <p>The influence of physical exercise on the urinary excretion of <span class="hlt">proteins</span> was examined in 17 male high school baseball players. Their urine was collected before and after exercise to determine the <span class="hlt">concentrations</span> of total <span class="hlt">protein</span>, albumin, beta 2-microglobulin and creatinine along with the activity of N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30). <span class="hlt">Concentrations</span> of total <span class="hlt">protein</span>, albumin, beta 2-microglobulin and creatinine increased significantly (p less than 0.01) after exercise, while N-acetyl-beta-D-glucosaminidase activity did not increase. Similar results were obtained when the <span class="hlt">concentrations</span> of these urinary components were calculated on the basis of a urinary density of 1.024, and when they were expressed relative to the amount of creatinine. Positive correlations were seen among total <span class="hlt">protein</span>, albumin, beta 2-microglobulin and creatinine <span class="hlt">concentrations</span>, but not between the beta 2-microglobulin <span class="hlt">concentration</span> and N-acetyl-beta-D-glucosaminidase activity. Isoenzyme activities of N-acetyl-beta-D-glucosaminidase in the urine were determined by electrophoresis on cellulose acetate plates. After exercise, the A-form increased slightly, and the B-form decreased slightly, but these changes were not statistically significant.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/24838764','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/24838764"><span id="translatedtitle">APols-aided <span class="hlt">protein</span> precipitation: a rapid method for <span class="hlt">concentrating</span> <span class="hlt">proteins</span> for proteomic analysis.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Ning, Zhibin; Hawley, Brett; Seebun, Deeptee; Figeys, Daniel</p> <p>2014-10-01</p> <p>Amphipols (APols) are a newly designed and milder class of detergent. They have been used primarily in <span class="hlt">protein</span> structure analysis for membrane <span class="hlt">protein</span> trapping and stabilization. We have recently demonstrated that APols can be used as an alternative detergent for proteome extraction and digestion, to achieve a "One-stop" single-tube workflow for proteomics. In this workflow, APols are removed by precipitation after <span class="hlt">protein</span> digestion without depleting the digested peptides. Here, we took further advantage of this precipitation characteristic of APols to <span class="hlt">concentrate</span> <span class="hlt">proteins</span> from diluted samples. In contrast with tryptic peptides, a decrease in pH leads to the unbiased co-precipitation of APols with <span class="hlt">proteins</span>, including globular hydrophilic <span class="hlt">proteins</span>. We demonstrated that this precipitation is a combined effect of acid precipitation and the APols' <span class="hlt">protein</span> interactions. Also, we have been able to demonstrate that APols-aided <span class="hlt">protein</span> precipitation works well on diluted samples, such as secretome sample, and provides a rapid method for <span class="hlt">protein</span> <span class="hlt">concentration</span>.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2016APS..MAR.G1327P','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2016APS..MAR.G1327P"><span id="translatedtitle"><span class="hlt">Absolute</span> Summ</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Phillips, Alfred, Jr.</p> <p></p> <p>Summ means the entirety of the multiverse. It seems clear, from the inflation theories of A. Guth and others, that the creation of many universes is plausible. We argue that <span class="hlt">Absolute</span> cosmological ideas, not unlike those of I. Newton, may be consistent with dynamic multiverse creations. As suggested in W. Heisenberg's uncertainty principle, and with the Anthropic Principle defended by S. Hawking, et al., human consciousness, buttressed by findings of neuroscience, may have to be considered in our models. Predictability, as A. Einstein realized with Invariants and General Relativity, may be required for new ideas to be part of physics. We present here a two postulate model geared to an <span class="hlt">Absolute</span> Summ. The seedbed of this work is part of Akhnaton's philosophy (see S. Freud, Moses and Monotheism). Most important, however, is that the structure of human consciousness, manifest in Kenya's Rift Valley 200,000 years ago as Homo sapiens, who were the culmination of the six million year co-creation process of Hominins and Nature in Africa, allows us to do the physics that we do. .</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=323945','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=323945"><span id="translatedtitle">Whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> storage at elevated temperature and humidity</span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>Dairy processors are finding new export markets for whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC), a byproduct of cheesemaking, but they need to know if full-sized bags of this powder will withstand high temperature and relative humidity (RH) levels during unrefrigerated storage under tropical conditions. To answ...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.gpo.gov/fdsys/pkg/CFR-2011-title21-vol3/pdf/CFR-2011-title21-vol3-sec184-1979c.pdf','CFR2011'); return false;" href="https://www.gpo.gov/fdsys/pkg/CFR-2011-title21-vol3/pdf/CFR-2011-title21-vol3-sec184-1979c.pdf"><span id="translatedtitle">21 CFR 184.1979c - Whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="http://www.gpo.gov/fdsys/browse/collectionCfr.action?selectedYearFrom=2011&page.go=Go">Code of Federal Regulations, 2011 CFR</a></p> <p></p> <p>2011-04-01</p> <p>... incorporated by reference in accordance with 5 U.S.C. 552(a) and 1 CFR part 51, is given in paragraphs (b)(1)(i... 1 CFR part 51. Copies are available from the National Academy Press, Box 285, 2101 Constitution Ave... 21 Food and Drugs 3 2011-04-01 2011-04-01 false Whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>. 184.1979c Section...</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_2");'>2</a></li> <li><a href="#" onclick='return showDiv("page_3");'>3</a></li> <li class="active"><span>4</span></li> <li><a href="#" onclick='return showDiv("page_5");'>5</a></li> <li><a href="#" onclick='return showDiv("page_6");'>6</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_4 --> <div id="page_5" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_3");'>3</a></li> <li><a href="#" onclick='return showDiv("page_4");'>4</a></li> <li class="active"><span>5</span></li> <li><a href="#" onclick='return showDiv("page_6");'>6</a></li> <li><a href="#" onclick='return showDiv("page_7");'>7</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="81"> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/21476549','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/21476549"><span id="translatedtitle"><span class="hlt">Concentrating</span> membrane <span class="hlt">proteins</span> using asymmetric traps and AC electric fields.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Cheetham, Matthew R; Bramble, Jonathan P; McMillan, Duncan G G; Krzeminski, Lukasz; Han, Xiaojun; Johnson, Benjamin R G; Bushby, Richard J; Olmsted, Peter D; Jeuken, Lars J C; Marritt, Sophie J; Butt, Julea N; Evans, Stephen D</p> <p>2011-05-01</p> <p>Membrane <span class="hlt">proteins</span> are key components of the plasma membrane and are responsible for control of chemical ionic gradients, metabolite and nutrient transfer, and signal transduction between the interior of cells and the external environment. Of the genes in the human genome, 30% code for membrane <span class="hlt">proteins</span> (Krogh et al. J. Mol. Biol.2001, 305, 567). Furthermore, many FDA-approved drugs target such <span class="hlt">proteins</span> (Overington et al. Nat. Rev. Drug Discovery 2006, 5, 993). However, the structure-function relationships of these are notably sparse because of difficulties in their purification and handling outside of their membranous environment. Methods that permit the manipulation of membrane components while they are still in the membrane would find widespread application in separation, purification, and eventual structure-function determination of these species (Poo et al. Nature 1977, 265, 602). Here we show that asymmetrically patterned supported lipid bilayers in combination with AC electric fields can lead to efficient manipulation of charged components. We demonstrate the <span class="hlt">concentration</span> and trapping of such components through the use of a "nested trap" and show that this method is capable of yielding an approximately 30-fold increase in the average <span class="hlt">protein</span> <span class="hlt">concentration</span>. Upon removal of the field, the material remains trapped for several hours as a result of topographically restricted diffusion. Our results indicate that this method can be used for <span class="hlt">concentrating</span> and trapping charged membrane components while they are still within their membranous environment. We anticipate that our approach could find widespread application in the manipulation and study of membrane <span class="hlt">proteins</span>.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/21476549','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/21476549"><span id="translatedtitle"><span class="hlt">Concentrating</span> membrane <span class="hlt">proteins</span> using asymmetric traps and AC electric fields.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Cheetham, Matthew R; Bramble, Jonathan P; McMillan, Duncan G G; Krzeminski, Lukasz; Han, Xiaojun; Johnson, Benjamin R G; Bushby, Richard J; Olmsted, Peter D; Jeuken, Lars J C; Marritt, Sophie J; Butt, Julea N; Evans, Stephen D</p> <p>2011-05-01</p> <p>Membrane <span class="hlt">proteins</span> are key components of the plasma membrane and are responsible for control of chemical ionic gradients, metabolite and nutrient transfer, and signal transduction between the interior of cells and the external environment. Of the genes in the human genome, 30% code for membrane <span class="hlt">proteins</span> (Krogh et al. J. Mol. Biol.2001, 305, 567). Furthermore, many FDA-approved drugs target such <span class="hlt">proteins</span> (Overington et al. Nat. Rev. Drug Discovery 2006, 5, 993). However, the structure-function relationships of these are notably sparse because of difficulties in their purification and handling outside of their membranous environment. Methods that permit the manipulation of membrane components while they are still in the membrane would find widespread application in separation, purification, and eventual structure-function determination of these species (Poo et al. Nature 1977, 265, 602). Here we show that asymmetrically patterned supported lipid bilayers in combination with AC electric fields can lead to efficient manipulation of charged components. We demonstrate the <span class="hlt">concentration</span> and trapping of such components through the use of a "nested trap" and show that this method is capable of yielding an approximately 30-fold increase in the average <span class="hlt">protein</span> <span class="hlt">concentration</span>. Upon removal of the field, the material remains trapped for several hours as a result of topographically restricted diffusion. Our results indicate that this method can be used for <span class="hlt">concentrating</span> and trapping charged membrane components while they are still within their membranous environment. We anticipate that our approach could find widespread application in the manipulation and study of membrane <span class="hlt">proteins</span>. PMID:21476549</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25352046','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25352046"><span id="translatedtitle">Phenylketonuria: brain phenylalanine <span class="hlt">concentrations</span> relate inversely to cerebral <span class="hlt">protein</span> synthesis.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>de Groot, Martijn J; Sijens, Paul E; Reijngoud, Dirk-Jan; Paans, Anne M; van Spronsen, Francjan J</p> <p>2015-02-01</p> <p>In phenylketonuria, elevated plasma phenylalanine <span class="hlt">concentrations</span> may disturb blood-to-brain large neutral amino acid (LNAA) transport and cerebral <span class="hlt">protein</span> synthesis (CPS). We investigated the associations between these processes, using data obtained by positron emission tomography with l-[1-(11)C]-tyrosine ((11)C-Tyr) as a tracer. Blood-to-brain transport of non-Phe LNAAs was modeled by the rate constant for (11)C-Tyr transport from arterial plasma to brain tissue (K1), while CPS was modeled by the rate constant for (11)C-Tyr incorporation into cerebral <span class="hlt">protein</span> (k3). Brain phenylalanine <span class="hlt">concentrations</span> were measured by magnetic resonance spectroscopy in three volumes of interest (VOIs): supraventricular brain tissue (VOI 1), ventricular brain tissue (VOI 2), and fluid-containing ventricular voxels (VOI 3). The associations between k3 and each predictor variable were analyzed by multiple linear regression. The rate constant k3 was inversely associated with brain phenylalanine <span class="hlt">concentrations</span> in VOIs 2 and 3 (adjusted R(2)=0.826, F=19.936, P=0.021). Since brain phenylalanine <span class="hlt">concentrations</span> in these VOIs highly correlated with each other, the specific associations of each predictor with k3 could not be determined. The associations between k3 and plasma phenylalanine <span class="hlt">concentration</span>, K1, and brain phenylalanine <span class="hlt">concentrations</span> in VOI 1 were nonsignificant. In conclusion, our study shows an inverse association between k3 and increased brain phenylalanine <span class="hlt">concentrations</span>.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2015ChPhB..24k4204Y','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2015ChPhB..24k4204Y"><span id="translatedtitle">Quantitative measurements of one-dimensional OH <span class="hlt">absolute</span> <span class="hlt">concentration</span> profiles in a methane/air flat flame by bi-directional laser-induced fluorescence</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Yu, Xin; Yang, Zhen; Peng, Jiang-Bo; Zhang, Lei; Ma, Yu-Fei; Yang, Chao-Bo; Li, Xiao-Hui; Sun, Rui</p> <p>2015-11-01</p> <p>The one-dimensional (1D) spatial distributions of OH <span class="hlt">absolute</span> <span class="hlt">concentration</span> in methane/air laminar premixed flat flame under different equivalence ratios at atmospheric pressure are investigated by using bi-directional laser-induced fluorescence (LIF) detection scheme combined with the direct absorption spectroscopy. The effective peak absorption cross section and the average temperature at a height of 2 mm above the burner are obtained by exciting absorption on the Q1(8) rotational line in the A2Σ+ (ʋ‧ = 0) ← X2Π (ʋ″ = 0) at 309.240 nm. The measured values are 1.86×10-15 cm2 and 1719 K, respectively. Spatial filtering and frequency filtering methods of reducing noise are used to deal with the experimental data, and the smoothing effects are also compared using the two methods. The spatial distribution regularities of OH <span class="hlt">concentration</span> are obtained with the equivalence ratios ranging from 0.8 to 1.3. The spatial resolution of the measured result is 84 μm. Finally, a comparison is made between the experimental result of this paper and other relevant study results. Project supported by the National Key Scientific Instrument and Equipment Development Projects of China (Grant No. 2012YQ040164), the National Natural Science Foundation of China (Grant Nos. 61275127 and 91441130), the China Postdoctoral Science Foundation (Grant No. 2014M560262), and the Postdoctoral Fellowship in Heilongjiang Province, China (Grant No. LBH-Z14074).</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2008APS..MARH17002H','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2008APS..MARH17002H"><span id="translatedtitle"><span class="hlt">Concentration</span>-dependent Cu(II) binding to prion <span class="hlt">protein</span></span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Hodak, Miroslav; Lu, Wenchang; Bernholc, Jerry</p> <p>2008-03-01</p> <p>The prion <span class="hlt">protein</span> plays a causative role in several neurodegenerative diseases, including mad cow disease in cattle and Creutzfeldt-Jakob disease in humans. The normal function of the prion <span class="hlt">protein</span> is unknown, but it has been linked to its ability to bind copper ions. Experimental evidence suggests that copper can be bound in three distinct modes depending on its <span class="hlt">concentration</span>, but only one of those binding modes has been fully characterized experimentally. Using a newly developed hybrid DFT/DFT method [1], which combines Kohn-Sham DFT with orbital-free DFT, we have examined all the binding modes and obtained their detailed binding geometries and copper ion binding energies. Our results also provide explanation for experiments, which have found that when the copper <span class="hlt">concentration</span> increases the copper binding mode changes, surprisingly, from a stronger to a weaker one. Overall, our results indicate that prion <span class="hlt">protein</span> can function as a copper buffer. 1. Hodak, Lu, Bernholc, JCP, in press.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27473483','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27473483"><span id="translatedtitle">Affinity Monolith-Integrated Microchips for <span class="hlt">Protein</span> Purification and <span class="hlt">Concentration</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Gao, Changlu; Sun, Xiuhua; Wang, Huaixin; Qiao, Wei; Hu, Bo</p> <p>2016-01-01</p> <p>Affinity chromatography is a valuable method to purify and <span class="hlt">concentrate</span> minute amount of <span class="hlt">proteins</span>. Monoliths with epoxy groups for affinity immobilization were prepared by direct in-situ photopolymerization of glycidyl methacrylate and ethylene glycol dimethacrylate in porogenic solvents consisting of 1-dodecanol and cyclohexanol. By integrating affinity monoliths onto a microfluidic system, targeted biomolecules can be captured and retained on affinity column, while other biomolecules having no specific interactions toward the immobilized ligands flow through the microchannel. Therefore, <span class="hlt">proteins</span> which remain on the affinity column are purified and <span class="hlt">concentrated</span>, and then eluted by appropriate solutions and finally, separated by microchip capillary electrophoresis. This integrated microfluidic device has been applied to the purification and separation of specific <span class="hlt">proteins</span> (FITC-labeled human serum albumin and IgG) in a mixture.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27473483','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27473483"><span id="translatedtitle">Affinity Monolith-Integrated Microchips for <span class="hlt">Protein</span> Purification and <span class="hlt">Concentration</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Gao, Changlu; Sun, Xiuhua; Wang, Huaixin; Qiao, Wei; Hu, Bo</p> <p>2016-01-01</p> <p>Affinity chromatography is a valuable method to purify and <span class="hlt">concentrate</span> minute amount of <span class="hlt">proteins</span>. Monoliths with epoxy groups for affinity immobilization were prepared by direct in-situ photopolymerization of glycidyl methacrylate and ethylene glycol dimethacrylate in porogenic solvents consisting of 1-dodecanol and cyclohexanol. By integrating affinity monoliths onto a microfluidic system, targeted biomolecules can be captured and retained on affinity column, while other biomolecules having no specific interactions toward the immobilized ligands flow through the microchannel. Therefore, <span class="hlt">proteins</span> which remain on the affinity column are purified and <span class="hlt">concentrated</span>, and then eluted by appropriate solutions and finally, separated by microchip capillary electrophoresis. This integrated microfluidic device has been applied to the purification and separation of specific <span class="hlt">proteins</span> (FITC-labeled human serum albumin and IgG) in a mixture. PMID:27473483</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/22435609','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/22435609"><span id="translatedtitle">Leaf <span class="hlt">protein</span> <span class="hlt">concentrate</span> as food supplement from arid zone plants.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Rathore, Mala</p> <p>2010-06-01</p> <p>In arid and semi-arid areas where prevalence of droughts and famines is a recurring feature, forest cover can in general make valuable contributions to food security and provide income to the rural poor. <span class="hlt">Protein</span> and calorie malnutrition is widespread in these areas leading to high child mortality rate. Plant species can play an important role in overcoming this by being used as a source of leaf <span class="hlt">protein</span> <span class="hlt">concentrate</span> (LPC), a highly nutritious food. LPC should be considered seriously as it can serve as an additional <span class="hlt">protein</span> source in the case of non-ruminants and man, especially in drought prone areas. The use of LPC in developing countries as an alternative <span class="hlt">protein</span> source to fishmeal in broiler diet holds tremendous promise as it can substantially lower high cost of fishmeal and eventually the acute shortage of animal <span class="hlt">protein</span> supply. Potential tropical plants for LPC production have been evaluated and selected for further research by United States Department of Agriculture. The present study was aimed to determine the potential of arid zone plants for preparation of LPC. Extraction characteristics of the several plant species have been studied and the quality of LPC prepared from them was investigated. Different fractions, chloroplastic and cytoplasmic <span class="hlt">proteins</span>, were analyzed for their crude <span class="hlt">protein</span> contents. Analysis of LPC shows considerable differences in their <span class="hlt">protein</span> contents, which was found to range from 13.7 to 88.9%. Based on this, Achyranthes aspera and Tephrosia purpurea were found to be the best suited plants for LPC preparation.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26748454','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26748454"><span id="translatedtitle">Microstructural Changes in High-<span class="hlt">Protein</span> Nutrition Bars Formulated with Extruded or Toasted Milk <span class="hlt">Protein</span> <span class="hlt">Concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Banach, J C; Clark, S; Lamsal, B P</p> <p>2016-02-01</p> <p>Milk <span class="hlt">protein</span> <span class="hlt">concentrates</span> with more than 80% <span class="hlt">protein</span> (that is, MPC80) are underutilized as the primary <span class="hlt">protein</span> source in high-<span class="hlt">protein</span> nutrition bars as they impart crumbliness and cause hardening during storage. High-<span class="hlt">protein</span> nutrition bar texture changes are often associated with internal <span class="hlt">protein</span> aggregations and macronutrient phase separation. These changes were investigated in model high-<span class="hlt">protein</span> nutrition bars formulated with MPC80 and physically modified MPC80s. High-<span class="hlt">protein</span> nutrition bars formulated with extruded MPC80s hardened slower than those formulated with toasted or unmodified MPC80. Extruded MPC80 had reduced free sulfhydryl group exposure, whereas measurable increases were seen in the toasted MPC80. High-<span class="hlt">protein</span> nutrition bar textural performance may be related to the number of exposed free sulfhydryl groups in MPC80. <span class="hlt">Protein</span> aggregations resulting from ingredient modification and high-<span class="hlt">protein</span> nutrition bar storage were studied with sodium dodecyl sulfate polyacrylamide gel electrophoresis. Disulfide-based <span class="hlt">protein</span> aggregations and changes in free sulfhydryl <span class="hlt">concentration</span> were not consistently relatable to high-<span class="hlt">protein</span> nutrition bar texture change. However, the high-<span class="hlt">protein</span> nutrition bars formulated with extruded MPC80 were less prone to phase separations, as depicted by confocal laser scanning microscopy, and underwent less texture change during storage than those formulated with toasted or unmodified MPC80.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/23792543','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/23792543"><span id="translatedtitle">Interaction of silver nanoparticles with <span class="hlt">proteins</span>: a characteristic <span class="hlt">protein</span> <span class="hlt">concentration</span> dependent profile of SPR signal.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Banerjee, Victor; Das, K P</p> <p>2013-11-01</p> <p>Silver nanoparticles are finding increasing applications in biological systems, for example as antimicrobial agents and potential candidates for control drug release systems. In all such applications, silver nanoparticles interact with <span class="hlt">proteins</span> and other biomolecules. Hence, the study of such interactions is of considerable importance. While BSA has been extensively used as a model <span class="hlt">protein</span> for the study of interaction with the silver nanoparticles, studies using other <span class="hlt">proteins</span> are rather limited. The interaction of silver nanoparticles with light leads to collective oscillation of the conducting electrons giving rise to surface plasmon resonance (SPR). Here, we have studied the <span class="hlt">protein</span> <span class="hlt">concentration</span> dependence of the SPR band profiles for a number of <span class="hlt">proteins</span>. We found that for all the <span class="hlt">proteins</span>, with increase in <span class="hlt">concentration</span>, the SPR band intensity initially decreased, reaching minima and then increased again leading to a characteristic "dip and rise" pattern. Minimum point of the pattern appeared to be related to the isoelectric point of the <span class="hlt">proteins</span>. Detailed dynamic light scattering and transmission electron microscopy studies revealed that the consistency of SPR profile was dependent on the average particle size and state of association of the silver nanoparticles with the change in the <span class="hlt">protein</span> <span class="hlt">concentration</span>. Fluorescence spectroscopic studies showed the binding constants of the <span class="hlt">proteins</span> with the silver nanoparticles were in the nano molar range with more than one nanoparticle binding to <span class="hlt">protein</span> molecule. Structural studies demonstrate that <span class="hlt">protein</span> retains its native-like structure on the nanoparticle surface unless the molar ratio of silver nanoparticles to <span class="hlt">protein</span> exceeds 10. Our study reveals that nature of the <span class="hlt">protein</span> <span class="hlt">concentration</span> dependent profile of SPR signal is a general phenomena and mostly independent of the size and structure of the <span class="hlt">proteins</span>.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/22413971','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/22413971"><span id="translatedtitle">Trypsin immobilization on hairy polymer chains hybrid magnetic nanoparticles for ultra fast, highly efficient proteome digestion, facile 18O labeling and <span class="hlt">absolute</span> <span class="hlt">protein</span> quantification.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Qin, Weijie; Song, Zifeng; Fan, Chao; Zhang, Wanjun; Cai, Yun; Zhang, Yangjun; Qian, Xiaohong</p> <p>2012-04-01</p> <p>In recent years, quantitative proteomic research attracts great attention because of the urgent needs in biological and clinical research, such as biomarker discovery and verification. Currently, mass spectrometry (MS) based bottom up strategy has become the method of choice for proteomic quantification. In this strategy, the amount of <span class="hlt">proteins</span> is determined by quantifying the corresponding proteolytic peptides of the <span class="hlt">proteins</span>, therefore highly efficient and complete <span class="hlt">protein</span> digestion is crucial for achieving accurate quantification results. However, the digestion efficiency and completeness obtained using conventional free protease digestion is not satisfactory for highly complex proteomic samples. In this work, we developed a new type of immobilized trypsin using hairy noncross-linked polymer chains hybrid magnetic nanoparticle as the matrix aiming at ultra fast, highly efficient proteomic digestion and facile (18)O labeling for <span class="hlt">absolution</span> <span class="hlt">protein</span> quantification. The hybrid nanoparticle is synthesized by in situ growth of hairy polymer chains from the magnetic nanoparticle surface using surface initiated atom transfer radical polymerization technique. The flexible noncross-linked polymer chains not only provide large amount of binding sites but also work as scaffolds to support three-dimensional trypsin immobilization which leads to increased loading amount and improved accessibility of the immobilized trypsin. For complex proteomic samples, obviously increased digestion efficiency and completeness was demonstrated by 27.2% and 40.8% increase in the number of identified <span class="hlt">proteins</span> and peptides as well as remarkably reduced undigested <span class="hlt">proteins</span> residues compared with that obtained using conventional free trypsin digestion. The successful application in <span class="hlt">absolute</span> <span class="hlt">protein</span> quantification of enolase from Thermoanaerobacter tengcongensis <span class="hlt">protein</span> extracts using (18)O labeling and MRM strategy further demonstrated the potential of this hybrid nanoparticle immobilized trypsin</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4823792','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4823792"><span id="translatedtitle"><span class="hlt">Concentration</span> Dependent Ion-<span class="hlt">Protein</span> Interaction Patterns Underlying <span class="hlt">Protein</span> Oligomerization Behaviours</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Batoulis, Helena; Schmidt, Thomas H.; Weber, Pascal; Schloetel, Jan-Gero; Kandt, Christian; Lang, Thorsten</p> <p>2016-01-01</p> <p>Salts and <span class="hlt">proteins</span> comprise two of the basic molecular components of biological materials. Kosmotropic/chaotropic co-solvation and matching ion water affinities explain basic ionic effects on <span class="hlt">protein</span> aggregation observed in simple solutions. However, it is unclear how these theories apply to <span class="hlt">proteins</span> in complex biological environments and what the underlying ionic binding patterns are. Using the positive ion Ca2+ and the negatively charged membrane <span class="hlt">protein</span> SNAP25, we studied ion effects on <span class="hlt">protein</span> oligomerization in solution, in native membranes and in molecular dynamics (MD) simulations. We find that <span class="hlt">concentration</span>-dependent ion-induced <span class="hlt">protein</span> oligomerization is a fundamental chemico-physical principle applying not only to soluble but also to membrane-anchored <span class="hlt">proteins</span> in their native environment. Oligomerization is driven by the interaction of Ca2+ ions with the carboxylate groups of aspartate and glutamate. From low up to middle <span class="hlt">concentrations</span>, salt bridges between Ca2+ ions and two or more <span class="hlt">protein</span> residues lead to increasingly larger oligomers, while at high <span class="hlt">concentrations</span> oligomers disperse due to overcharging effects. The insights provide a conceptual framework at the interface of physics, chemistry and biology to explain binding of ions to charged <span class="hlt">protein</span> surfaces on an atomistic scale, as occurring during <span class="hlt">protein</span> solubilisation, aggregation and oligomerization both in simple solutions and membrane systems. PMID:27052788</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26048645','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26048645"><span id="translatedtitle">Functional Characteristics of Milk <span class="hlt">Protein</span> <span class="hlt">Concentrates</span> and Their Modification.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Uluko, Hankie; Liu, Lu; Lv, Jia-Ping; Zhang, Shu-Wen</p> <p>2016-05-18</p> <p>A major deterrent to the usage of milk <span class="hlt">protein</span> <span class="hlt">concentrate</span> (MPC), a high-<span class="hlt">protein</span> milk product with increasing demand as a food and sports drink ingredient, has been its poor functional characteristics when compared with other milk <span class="hlt">protein</span> products such as whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> and sodium caseinates. This review discusses the recent research on functional properties of MPC, focusing on factors that may contribute to the poor functional characteristics before, during, and after production. Current research, methods employed, and new understanding on the causes of poor solubility of MPC at mild temperatures (about 20°C) has been presented, including loss of solubility during storage as these areas have received unprecedented attention over the past decade, and also affects other useful functional properties of MPC, such as emulsifying properties, gelation, and foaming. Processing methods, which include heat treatment, high-pressure application, microwave heating, ultrasound application, and enzyme and salts modification, have been used or have potential to modify or improve the functional properties of MPCs. Future research on the effects of these processing methods on the functional properties, including effects of enzyme hydrolysis on bitterness and bioactivity, has also been discussed. PMID:26048645</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26048645','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26048645"><span id="translatedtitle">Functional Characteristics of Milk <span class="hlt">Protein</span> <span class="hlt">Concentrates</span> and Their Modification.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Uluko, Hankie; Liu, Lu; Lv, Jia-Ping; Zhang, Shu-Wen</p> <p>2016-05-18</p> <p>A major deterrent to the usage of milk <span class="hlt">protein</span> <span class="hlt">concentrate</span> (MPC), a high-<span class="hlt">protein</span> milk product with increasing demand as a food and sports drink ingredient, has been its poor functional characteristics when compared with other milk <span class="hlt">protein</span> products such as whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> and sodium caseinates. This review discusses the recent research on functional properties of MPC, focusing on factors that may contribute to the poor functional characteristics before, during, and after production. Current research, methods employed, and new understanding on the causes of poor solubility of MPC at mild temperatures (about 20°C) has been presented, including loss of solubility during storage as these areas have received unprecedented attention over the past decade, and also affects other useful functional properties of MPC, such as emulsifying properties, gelation, and foaming. Processing methods, which include heat treatment, high-pressure application, microwave heating, ultrasound application, and enzyme and salts modification, have been used or have potential to modify or improve the functional properties of MPCs. Future research on the effects of these processing methods on the functional properties, including effects of enzyme hydrolysis on bitterness and bioactivity, has also been discussed.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3691662','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3691662"><span id="translatedtitle">A study protocol for quantitative targeted <span class="hlt">absolute</span> proteomics (QTAP) by LC-MS/MS: application for inter-strain differences in <span class="hlt">protein</span> expression levels of transporters, receptors, claudin-5, and marker <span class="hlt">proteins</span> at the blood–brain barrier in ddY, FVB, and C57BL/6J mice</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p></p> <p>2013-01-01</p> <p>Proteomics has opened a new horizon in biological sciences. Global proteomic analysis is a promising technology for the discovery of thousands of <span class="hlt">proteins</span>, post-translational modifications, polymorphisms, and molecular interactions in a variety of biological systems. The activities and roles of the identified <span class="hlt">proteins</span> must also be elucidated, but this is complicated by the inability of conventional proteomic methods to yield quantitative information for <span class="hlt">protein</span> expression. Thus, a variety of biological systems remain “black boxes”. Quantitative targeted <span class="hlt">absolute</span> proteomics (QTAP) enables the determination of <span class="hlt">absolute</span> expression levels (mol) of any target <span class="hlt">protein</span>, including low-abundance functional <span class="hlt">proteins</span>, such as transporters and receptors. Therefore, QTAP will be useful for understanding the activities and roles of individual <span class="hlt">proteins</span> and their differences, including normal/disease, human/animal, or in vitro/in vivo. Here, we describe the study protocols and precautions for QTAP experiments including in silico target peptide selection, determination of peptide <span class="hlt">concentration</span> by amino acid analysis, setup of selected/multiple reaction monitoring (SRM/MRM) analysis in liquid chromatography–tandem mass spectrometry, preparation of <span class="hlt">protein</span> samples (brain capillaries and plasma membrane fractions) followed by the preparation of peptide samples, simultaneous <span class="hlt">absolute</span> quantification of target <span class="hlt">proteins</span> by SRM/MRM analysis, data analysis, and troubleshooting. An application of QTAP in biological sciences was introduced that utilizes data from inter-strain differences in the <span class="hlt">protein</span> expression levels of transporters, receptors, tight junction <span class="hlt">proteins</span> and marker <span class="hlt">proteins</span> at the blood–brain barrier in ddY, FVB, and C57BL/6J mice. Among 18 molecules, 13 (abcb1a/mdr1a/P-gp, abcc4/mrp4, abcg2/bcrp, slc2a1/glut1, slc7a5/lat1, slc16a1/mct1, slc22a8/oat3, insr, lrp1, tfr1, claudin-5, Na+/K+-ATPase, and γ-gtp) were detected in the isolated brain capillaries, and their</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/biblio/5676756','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/biblio/5676756"><span id="translatedtitle"><span class="hlt">Protein</span>-lipid interactions in <span class="hlt">concentrated</span> infant formula</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>Rowley, B.O.; Richardson, T.</p> <p>1985-12-01</p> <p>Radiolabeled milk <span class="hlt">proteins</span> ((carbon-14) ..beta..-lactoglobulin or (carbon-14) kappa-casein) were added to raw skim milk used to prepare <span class="hlt">concentrated</span> humanized infant formula. Ultracentrifugation of the sterilized product allowed separation of three fractions: lipids and the <span class="hlt">proteins</span> associated with them; free casein micelles and other dense particles; and the fluid phase. Distribution of radiolabeled tracer <span class="hlt">proteins</span> or of <span class="hlt">protein</span> measured by chemical methods among these three phases varied significantly with differences in processing conditions (time and temperature of sterilization) or amount of certain additives (potassium hydroxide or urea). In the range of 0 to 8 meq/L of potassium hydroxide added to the formula after homogenization but before sterilization, the lipid layer content of carbon-14 from (carbon-14) kappa-casein in the sterilized product decreased by 4.7% for each 1 meq/L of added potassium hydroxide. Lipid layer content of <span class="hlt">protein</span> decreased by 2 g/L ( of a total of 32 g/L) for each 1 meq/L potassium hydroxide.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25796981','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25796981"><span id="translatedtitle">Application of an LC-MS/MS method for the simultaneous quantification of human intestinal transporter <span class="hlt">proteins</span> <span class="hlt">absolute</span> abundance using a QconCAT technique.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Harwood, M D; Achour, B; Russell, M R; Carlson, G L; Warhurst, G; Rostami-Hodjegan, A</p> <p>2015-06-10</p> <p>Transporter <span class="hlt">proteins</span> expressed in the gastrointestinal tract play a major role in the oral absorption of some drugs, and their involvement may lead to drug-drug interaction (DDI) susceptibility when given in combination with drugs known to inhibit gut wall transporters. Anticipating such liabilities and predicting the magnitude of the impact of transporter <span class="hlt">proteins</span> on oral drug absorption and DDIs requires quantification of their expression in human intestine, and linking these to data obtained through in vitro experiments. A quantitative targeted <span class="hlt">absolute</span> proteomic method employing liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) together with a quantitative concatenation (QconCAT) strategy to provide proteotypic peptide standards has been applied to quantify ATP1A1 (sodium/potassium-ATPase; Na/K-ATPase), CDH17 (human peptide transporter 1; HPT1), ABCB1 (P-glycoprotein; P-gp), ABCG2 (breast cancer resistance <span class="hlt">protein</span>; BCRP), ABCC2 (multidrug resistance-associated <span class="hlt">protein</span> 2; MRP2) and SLC51A (Organic Solute Transporter subunit alpha; OST-α), in human distal jejunum (n=3) and distal ileum (n=1) enterocyte membranes. Previously developed selected reaction monitoring (SRM) schedules were optimised to enable quantification of the proteotypic peptides for each transporter. After harvesting enterocytes by calcium chelation elution and generating a total membrane fraction, the <span class="hlt">proteins</span> were subjected to proteolytic digestion. To account for losses of peptides during the digestion procedure, a gravimetric method is also presented. The linearity of quantifying the QconCAT from an internal standard (correlation coefficient, R(2)=0.998) and quantification of all target peptides in a pooled intestinal quality control sample (R(2)≥ 0.980) was established. The assay was also assessed for within and between-day precision, demonstrating a <15% coefficient of variation for all peptides across 3 separate analytical runs, over 2 days. The methods were applied to</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26367331','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26367331"><span id="translatedtitle">Whey <span class="hlt">Protein</span> <span class="hlt">Concentrate</span> Hydrolysate Prevents Bone Loss in Ovariectomized Rats.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Kim, Jonggun; Kim, Hyung Kwan; Kim, Saehun; Imm, Ji-Young; Whang, Kwang-Youn</p> <p>2015-12-01</p> <p>Milk is known as a safe food and contains easily absorbable minerals and <span class="hlt">proteins</span>, including whey <span class="hlt">protein</span>, which has demonstrated antiosteoporotic effects on ovariectomized rats. This study evaluated the antiosteoporotic effect of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> hydrolysate (WPCH) digested with fungal protease and whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC). Two experiments were conducted to determine (1) efficacy of WPCH and WPC and (2) dose-dependent impact of WPCH in ovariectomized rats (10 weeks old). In Experiment I, ovariectomized rats (n=45) were allotted into three dietary treatments of 10 g/kg diet of WPC, 10 g/kg diet of WPCH, and a control diet. In Experiment II, ovariectomized rats (n=60) were fed four different diets (0, 10, 20, and 40 g/kg of WPCH). In both experiments, sham-operated rats (n=15) were also fed a control diet containing the same amount of amino acids and minerals as dietary treatments. After 6 weeks, dietary WPCH prevented loss of bone, physical properties, mineral density, and mineral content, and improved breaking strength of femurs, with similar effect to WPC. The bone resorption enzyme activity (tartrate resistance acid phosphatase) in tibia epiphysis decreased in response to WPCH supplementation, while bone formation enzyme activity (alkaline phosphatase) was unaffected by ovariectomy and dietary treatment. Bone properties and strength increased as the dietary WPCH level increased (10 and 20 g/kg), but there was no difference between the 20 and 40 g/kg treatment. WPCH and WPC supplementation ameliorated bone loss induced by ovariectomy in rats. PMID:26367331</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26367331','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26367331"><span id="translatedtitle">Whey <span class="hlt">Protein</span> <span class="hlt">Concentrate</span> Hydrolysate Prevents Bone Loss in Ovariectomized Rats.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Kim, Jonggun; Kim, Hyung Kwan; Kim, Saehun; Imm, Ji-Young; Whang, Kwang-Youn</p> <p>2015-12-01</p> <p>Milk is known as a safe food and contains easily absorbable minerals and <span class="hlt">proteins</span>, including whey <span class="hlt">protein</span>, which has demonstrated antiosteoporotic effects on ovariectomized rats. This study evaluated the antiosteoporotic effect of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> hydrolysate (WPCH) digested with fungal protease and whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC). Two experiments were conducted to determine (1) efficacy of WPCH and WPC and (2) dose-dependent impact of WPCH in ovariectomized rats (10 weeks old). In Experiment I, ovariectomized rats (n=45) were allotted into three dietary treatments of 10 g/kg diet of WPC, 10 g/kg diet of WPCH, and a control diet. In Experiment II, ovariectomized rats (n=60) were fed four different diets (0, 10, 20, and 40 g/kg of WPCH). In both experiments, sham-operated rats (n=15) were also fed a control diet containing the same amount of amino acids and minerals as dietary treatments. After 6 weeks, dietary WPCH prevented loss of bone, physical properties, mineral density, and mineral content, and improved breaking strength of femurs, with similar effect to WPC. The bone resorption enzyme activity (tartrate resistance acid phosphatase) in tibia epiphysis decreased in response to WPCH supplementation, while bone formation enzyme activity (alkaline phosphatase) was unaffected by ovariectomy and dietary treatment. Bone properties and strength increased as the dietary WPCH level increased (10 and 20 g/kg), but there was no difference between the 20 and 40 g/kg treatment. WPCH and WPC supplementation ameliorated bone loss induced by ovariectomy in rats.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/biblio/5868616','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/biblio/5868616"><span id="translatedtitle">Utilization of <span class="hlt">concentrated</span> cheese whey for the production of <span class="hlt">protein</span> <span class="hlt">concentrate</span> fuel alcohol and alcoholic beverages</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>Krishnamurti, R.</p> <p>1983-01-01</p> <p>The objective of this investigation was to recover the major components of whey and to develop food applications for their incorporation/conversion into acceptable products of commercial value. Reconstituted dried sweet whey with 36% solids was ultrafiltered to yield a <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) and a permeate containing 24% lactose and 3.7% ash. Orange juice fortified up to 2.07% and chocolate milks fortified up to 5.88% total <span class="hlt">protein</span> levels with WPC containing 45% total <span class="hlt">protein</span> were acceptable to about 90% of a panel of 24 individuals. Fermentation of demineralized permeate at 30/sup 0/C with Kluyveromyces fragilis NRRL Y 2415 adapted to 24% lactose levels, led to 13.7% (v/v) ethanol in the medium at the end of 34 hours. Batch productivity was 3.2 gms. ethanol per liter per hour and conversion efficiency was 84.26% of the theoretical maximum. Alcoholic fermentation of permeate and subsequent distillation produced compounds with desirable aroma characters in such products. This study suggests that there is potential for the production of <span class="hlt">protein</span> fortified non-alcoholic products and alcoholic beverages of commercial value from whey, thus providing a cost effective solution to the whey utilization problem.</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_3");'>3</a></li> <li><a href="#" onclick='return showDiv("page_4");'>4</a></li> <li class="active"><span>5</span></li> <li><a href="#" onclick='return showDiv("page_6");'>6</a></li> <li><a href="#" onclick='return showDiv("page_7");'>7</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_5 --> <div id="page_6" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_4");'>4</a></li> <li><a href="#" onclick='return showDiv("page_5");'>5</a></li> <li class="active"><span>6</span></li> <li><a href="#" onclick='return showDiv("page_7");'>7</a></li> <li><a href="#" onclick='return showDiv("page_8");'>8</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="101"> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=271697','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=271697"><span id="translatedtitle">Influence of bleaching on flavor of 34% whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> and residual benzoic acid <span class="hlt">concentration</span> in dried whey products</span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>Previous studies have shown that bleaching negatively affects the flavor of 70% whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC70), but bleaching effects on lower-<span class="hlt">protein</span> products have not been established. Benzoyl peroxide (BP), a whey bleaching agent, degrades to benzoic acid (BA) and may elevate BA <span class="hlt">concentrations</span>...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25862728','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25862728"><span id="translatedtitle">A Novel Function for Arabidopsis CYCLASE1 in Programmed Cell Death Revealed by Isobaric Tags for Relative and <span class="hlt">Absolute</span> Quantitation (iTRAQ) Analysis of Extracellular Matrix <span class="hlt">Proteins</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Smith, Sarah J; Kroon, Johan T M; Simon, William J; Slabas, Antoni R; Chivasa, Stephen</p> <p>2015-06-01</p> <p>Programmed cell death is essential for plant development and stress adaptation. A detailed understanding of the signal transduction pathways that regulate plant programmed cell death requires identification of the underpinning <span class="hlt">protein</span> networks. Here, we have used a protagonist and antagonist of programmed cell death triggered by fumonisin B1 as probes to identify key cell death regulatory <span class="hlt">proteins</span> in Arabidopsis. Our hypothesis was that changes in the abundance of cell death-regulatory <span class="hlt">proteins</span> induced by the protagonist should be blocked or attenuated by concurrent treatment with the antagonist. We focused on <span class="hlt">proteins</span> present in the mobile phase of the extracellular matrix on the basis that they are important for cell-cell communications during growth and stress-adaptive responses. Salicylic acid, a plant hormone that promotes programmed cell death, and exogenous ATP, which can block fumonisin B1-induced cell death, were used to treat Arabidopsis cell suspension cultures prior to isobaric-tagged relative and <span class="hlt">absolute</span> quantitation analysis of secreted <span class="hlt">proteins</span>. A total of 33 <span class="hlt">proteins</span>, whose response to salicylic acid was suppressed by ATP, were identified as putative cell death-regulatory <span class="hlt">proteins</span>. Among these was CYCLASE1, which was selected for further analysis using reverse genetics. Plants in which CYCLASE1 gene expression was knocked out by insertion of a transfer-DNA sequence manifested dramatically increased cell death when exposed to fumonisin B1 or a bacterial pathogen that triggers the defensive hypersensitive cell death. Although pathogen inoculation altered CYCLASE1 gene expression, multiplication of bacterial pathogens was indistinguishable between wild type and CYCLASE1 knockout plants. However, remarkably severe chlorosis symptoms developed on gene knockout plants in response to inoculation with either a virulent bacterial pathogen or a disabled mutant that is incapable of causing disease in wild type plants. These results show that CYCLASE1, which</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/15158476','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/15158476"><span id="translatedtitle">Use of <span class="hlt">protein</span>-acrylamide copolymer hydrogels for measuring <span class="hlt">protein</span> <span class="hlt">concentration</span> and activity.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Brueggemeier, Shawn B; Kron, Stephen J; Palecek, Sean P</p> <p>2004-06-15</p> <p>We report the development and characterization of a polyacrylamide-based <span class="hlt">protein</span> immobilization strategy for surface-bound <span class="hlt">protein</span> assays, including <span class="hlt">concentration</span> detection, binding affinity, and enzyme kinetics. Glutathione S-transferase (GST) fusion <span class="hlt">proteins</span> have been labeled with an acrylic moiety and attached to acrylic-functionalized glass surfaces through copolymerization with acrylic monomer. The specific attachment of GST-green fluorescent <span class="hlt">protein</span> (GFP) fusion <span class="hlt">protein</span> was more than sevenfold greater than the nonspecific attachment of nonacrylic-labeled GST-GFP; 0.32 ng/mm(2) of surface-attached GST-GFP was detectable by direct measurement of GFP fluorescence and this lower detection limit was reduced to 0.080 ng/mm(2) using indirect antibody-based detection. The polyacrylamide-based surface attachment strategy was also used to measure the kinetics of substrate phosphorylation by the kinase c-Src. Michaelis-Menten kinetic constants for the reaction occurring in solution were K(m) = 2.7 +/- 1.0 microM and V(max) = 8.1 +/- 3.1 (arbitrary units). Kinetic values for the reaction utilizing surface-immobilized substrate were K(m) = 0.36 +/- 0.033 microM and V(max) = 9.7 +/- 0.63 and were found to be independent of the acrylamide <span class="hlt">concentration</span> within the copolymer. Such a surface attachment strategy should be applicable to the proteomics field and addresses denaturation and dehydration problems associated with <span class="hlt">protein</span> microarray development.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/14740857','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/14740857"><span id="translatedtitle">Estimation of the <span class="hlt">protein</span> content of US imports of milk <span class="hlt">protein</span> <span class="hlt">concentrates</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Bailey, K W</p> <p>2003-12-01</p> <p>Recent declines in milk prices in the United States have sparked renewed concern that imports of milk <span class="hlt">protein</span> <span class="hlt">concentrates</span> (MPC) are increasingly entering the United States with very low tariff rates and is having an adverse impact on the US dairy industry. Milk <span class="hlt">protein</span> <span class="hlt">concentrates</span> are used in the United States in many different products, including the starter culture of cheese, or in nonstandard cheeses such as baker's cheese, ricotta, Feta and Hispanic cheese, processed cheese foods, and nutritional products. One of the difficult aspects of trying to assess the impact of MPC imports on the US dairy industry is to quantify the <span class="hlt">protein</span> content of these imports. The <span class="hlt">protein</span> content of MPC imports typically ranges from 40 to 88%. The purpose of this study is to develop a methodology that can be used to estimate the <span class="hlt">protein</span> content of MPC on a country by country basis. Such an estimate would not only provide information regarding the quantity of <span class="hlt">protein</span> entering the United States, but would also provide a profile of low- and high-value MPC importers. This is critical for market analysis, since it is the lower valued MPC imports that more directly displaces US-produced skim milk powder.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/15158476','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/15158476"><span id="translatedtitle">Use of <span class="hlt">protein</span>-acrylamide copolymer hydrogels for measuring <span class="hlt">protein</span> <span class="hlt">concentration</span> and activity.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Brueggemeier, Shawn B; Kron, Stephen J; Palecek, Sean P</p> <p>2004-06-15</p> <p>We report the development and characterization of a polyacrylamide-based <span class="hlt">protein</span> immobilization strategy for surface-bound <span class="hlt">protein</span> assays, including <span class="hlt">concentration</span> detection, binding affinity, and enzyme kinetics. Glutathione S-transferase (GST) fusion <span class="hlt">proteins</span> have been labeled with an acrylic moiety and attached to acrylic-functionalized glass surfaces through copolymerization with acrylic monomer. The specific attachment of GST-green fluorescent <span class="hlt">protein</span> (GFP) fusion <span class="hlt">protein</span> was more than sevenfold greater than the nonspecific attachment of nonacrylic-labeled GST-GFP; 0.32 ng/mm(2) of surface-attached GST-GFP was detectable by direct measurement of GFP fluorescence and this lower detection limit was reduced to 0.080 ng/mm(2) using indirect antibody-based detection. The polyacrylamide-based surface attachment strategy was also used to measure the kinetics of substrate phosphorylation by the kinase c-Src. Michaelis-Menten kinetic constants for the reaction occurring in solution were K(m) = 2.7 +/- 1.0 microM and V(max) = 8.1 +/- 3.1 (arbitrary units). Kinetic values for the reaction utilizing surface-immobilized substrate were K(m) = 0.36 +/- 0.033 microM and V(max) = 9.7 +/- 0.63 and were found to be independent of the acrylamide <span class="hlt">concentration</span> within the copolymer. Such a surface attachment strategy should be applicable to the proteomics field and addresses denaturation and dehydration problems associated with <span class="hlt">protein</span> microarray development. PMID:15158476</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/21854907','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/21854907"><span id="translatedtitle">Influence of bleaching on flavor of 34% whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> and residual benzoic acid <span class="hlt">concentration</span> in dried whey <span class="hlt">proteins</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Listiyani, M A D; Campbell, R E; Miracle, R E; Dean, L O; Drake, M A</p> <p>2011-09-01</p> <p>Previous studies have shown that bleaching negatively affects the flavor of 70% whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC70), but bleaching effects on lower-<span class="hlt">protein</span> products have not been established. Benzoyl peroxide (BP), a whey bleaching agent, degrades to benzoic acid (BA) and may elevate BA <span class="hlt">concentrations</span> in dried whey products. No legal limit exists in the United States for BP use in whey, but international concerns exist. The objectives of this study were to determine the effect of hydrogen peroxide (HP) or BP bleaching on the flavor of 34% WPC (WPC34) and to evaluate residual BA in commercial and experimental WPC bleached with and without BP. Cheddar whey was manufactured in duplicate. Pasteurized fat-separated whey was subjected to hot bleaching with either HP at 500 mg/kg, BP at 50 or 100 mg/kg, or no bleach. Whey was ultrafiltered and spray dried into WPC34. Color [L*(lightness), a* (red-green), and b* (yellow-blue)] measurements and norbixin extractions were conducted to compare bleaching efficacy. Descriptive sensory and instrumental volatile analyses were used to evaluate bleaching effects on flavor. Benzoic acid was extracted from experimental and commercial WPC34 and 80% WPC (WPC80) and quantified by HPLC. The b* value and norbixin <span class="hlt">concentration</span> of BP-bleached WPC34 were lower than HP-bleached and control WPC34. Hydrogen peroxide-bleached WPC34 displayed higher cardboard flavor and had higher volatile lipid oxidation products than BP-bleached or control WPC34. Benzoyl peroxide-bleached WPC34 had higher BA <span class="hlt">concentrations</span> than unbleached and HP-bleached WPC34 and BA <span class="hlt">concentrations</span> were also higher in BP-bleached WPC80 compared with unbleached and HP-bleached WPC80, with smaller differences than those observed in WPC34. Benzoic acid extraction from permeate showed that WPC80 permeate contained more BA than did WPC34 permeate. Benzoyl peroxide is more effective in color removal of whey and results in fewer flavor side effects compared with HP and residual BA is</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1369645','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1369645"><span id="translatedtitle">The polypyrimidine tract binding <span class="hlt">protein</span> (PTB) requirement for internal initiation of translation of cardiovirus RNAs is conditional rather than <span class="hlt">absolute</span>.</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Kaminski, A; Jackson, R J</p> <p>1998-01-01</p> <p>Picornavirus RNAs are translated by an unusual mechanism of internal ribosome entry that requires a substantial segment of the viral 5'-untranslated region, generally known as the internal ribosome entry segment (IRES), and in some circumstances may require cellular trans-acting <span class="hlt">proteins</span>, particularly polypyrimidine tract binding <span class="hlt">protein</span> (PTB). It is shown here that for encephalomyocarditis virus (EMCV), the PTB dependence of IRES function in vitro is determined partly by the nature of the reporter cistron, and more especially by the size of an A-rich bulge in the IRES. With a wild-type EMCV IRES (which has a bulge of 6 As), translation is effectively independent of PTB provided the IRES is driving the synthesis of EMCV viral polyprotein. With an enlarged (7A) bulge and heterologous reporters, translation is highly dependent on PTB. Intermediate levels of PTB dependence are seen with a 7A bulge IRES driving viral polyprotein synthesis or a wild-type (6A) bulge IRES linked to a heterologous reporter. None of these parameters influenced the binding of PTB to the high-affinity site in the IRES. These results argue that PTB is not an essential and universal internal initiation factor, but, rather, that when it is required, its binding to the IRES helps to maintain the appropriate higher-order structure and to reverse distortions caused, for example, by an enlarged A-rich bulge. PMID:9622122</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/14673136','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/14673136"><span id="translatedtitle">Urban renewal in the nucleus: is <span class="hlt">protein</span> turnover by proteasomes <span class="hlt">absolutely</span> required for nuclear receptor-regulated transcription?</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Nawaz, Zafar; O'Malley, Bert W</p> <p>2004-03-01</p> <p>The importance of the ubiquitin proteasome pathway in higher eukaryotes has been well established in cell cycle regulation, signal transduction, and cell differentiation, but has only recently been linked to nuclear hormone receptor-regulated gene transcription. Characterization of a number of ubiquitin proteasome pathway enzymes as coactivators and observations that several nuclear receptors are ubiquitinated and degraded in the course of their nuclear activities provide evidence that ubiquitin proteasome-mediated <span class="hlt">protein</span> degradation plays an integral role in eukaryotic transcription. In addition to receptors, studies have revealed that coactivators are ubiquitinated and degraded via the proteasome. The notion that the ubiquitin proteasome pathway is involved in gene transcription is further strengthened by the fact that ubiquitin proteasome pathway enzymes are recruited to the promoters of target genes and that proteasome-dependent degradation of nuclear receptors is required for efficient transcriptional activity. These findings suggest that <span class="hlt">protein</span> degradation is coupled with nuclear receptor coactivation activity. It is possible that the ubiquitin proteasome pathway modulates transcription by promoting remodeling and turnover of the nuclear receptor-transcription complex. In this review, we discus the possible role of the ubiquitin proteasome pathway in nuclear hormone receptor-regulated gene transcription.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://eric.ed.gov/?q=stallings&id=EJ1000865','ERIC'); return false;" href="http://eric.ed.gov/?q=stallings&id=EJ1000865"><span id="translatedtitle">Teaching <span class="hlt">Absolute</span> Value Meaningfully</span></a></p> <p><a target="_blank" href="http://www.eric.ed.gov/ERICWebPortal/search/extended.jsp?_pageLabel=advanced">ERIC Educational Resources Information Center</a></p> <p>Wade, Angela</p> <p>2012-01-01</p> <p>What is the meaning of <span class="hlt">absolute</span> value? And why do teachers teach students how to solve <span class="hlt">absolute</span> value equations? <span class="hlt">Absolute</span> value is a concept introduced in first-year algebra and then reinforced in later courses. Various authors have suggested instructional methods for teaching <span class="hlt">absolute</span> value to high school students (Wei 2005; Stallings-Roberts…</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/23733825','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/23733825"><span id="translatedtitle">Methods to obtain <span class="hlt">protein</span> <span class="hlt">concentrates</span> from jumbo squid (Dosidicus gigas) and evaluation of their functionality.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Galvez-Rongel, A; Ezquerra-Brauer, J M; Ocano-Higuera, V M; Ramirez-Wong, B; Torres-Arreola, W; Rouzaud-Sandez, O; Marquez-Rios, E</p> <p>2014-03-01</p> <p>Jumbo squid is an important fishery resource in Mexico, and its muscle is lean and white and it has a very low price in the market. It is abundant, but with little or nothing added value, therefore is necessary to search alternatives of processing. Due to muscle characteristics, the aim of this study was to obtain <span class="hlt">protein</span> <span class="hlt">concentrates</span> using different methods. They were obtained by means of acidic (acid <span class="hlt">protein</span> <span class="hlt">concentrates</span>) and alkaline (alkaline <span class="hlt">protein</span> <span class="hlt">concentrates</span>) dissolution. Moreover, a <span class="hlt">protein</span> <span class="hlt">concentrate</span> was obtained by direct isoelectric precipitation and by the traditional method (neutral <span class="hlt">protein</span> <span class="hlt">concentrates</span>). The yield with better results was alkaline <span class="hlt">protein</span> <span class="hlt">concentrates</span> (63.58 ± 1.8%). The gel hardness was significantly different (p < 0.05), especially for the alkaline <span class="hlt">protein</span> <span class="hlt">concentrates</span>. The acid <span class="hlt">protein</span> <span class="hlt">concentrates</span>, isoelectric precipitation and alkaline <span class="hlt">protein</span> <span class="hlt">concentrates</span> were better with regard to the neutral <span class="hlt">protein</span> <span class="hlt">concentrates</span>, concerning the emulsifying and foaming properties. The <span class="hlt">protein</span> <span class="hlt">concentrates</span> by means of alkaline dissolution gave a better gelling property, but all the processes had the potential to obtain <span class="hlt">protein</span> with emulsifying and foaming properties.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4094339','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4094339"><span id="translatedtitle"><span class="hlt">ABSOLUTE</span> BIOAVAILABILITY OF ISOFLAVONES FROM SOY <span class="hlt">PROTEIN</span> ISOLATE-CONTAINING FOOD IN FEMALE BALB/C MICE</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Andrade, Juan E.; Twaddle, Nathan C.; Helferich, William G.; Doerge, Daniel R.</p> <p>2014-01-01</p> <p>Soy isoflavones, genistein and daidzein, are widely consumed in soy-based foods and dietary supplements for their putative health benefits; however, evidence for potential adverse effects has been obtained from experimental animal studies. An important prerequisite for understanding the pharmacodynamics of isoflavones is better information about pharmacokinetics and bioavailability. This study determined the bioavailability of genistein and daidzein in a mouse model by comparing plasma pharmacokinetics of their aglycone and conjugated forms following administration of identical doses (1.2 mg/kg genistein and 0.55 mg/kg daidzein) by either an intravenous injection (IV) or gavage of the aglycones in 90% aqueous solution vs. a bolus administration of equimolar doses delivered in a food pellet prepared using commercial soy <span class="hlt">protein</span> isolate (SPI) as the isoflavone source. The bioavailability of genistein and daidzein were equivalent for the gavage and dietary routes of administration despite the use of isoflavone aglycones in the former and SPI-derived glucosides in the latter. While absorption of total isoflavones was nearly quantitative from both oral routes (>84% of AUCs for IV), presystemic and systemic Phase II conjugation greatly attenuated internal exposures to the receptor-active aglycone isoflavones (9–14% for genistein and 29–34% for daidzein based on AUCs for IV). These results show that SPI is an efficient isoflavone delivery vehicle capable of providing significant proportions of the total dose into the circulation in the active aglycone form for distribution to receptor-bearing tissues and subsequent pharmacological effects that determine possible health benefits and/or risks. PMID:20225898</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26070096','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26070096"><span id="translatedtitle">Method To Determine <span class="hlt">Protein</span> <span class="hlt">Concentration</span> in the <span class="hlt">Protein</span>-Nanoparticle Conjugates Aqueous Solution Using Circular Dichroism Spectroscopy.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Li, Shanghao; Peng, Zhili; Leblanc, Roger M</p> <p>2015-07-01</p> <p>Considerable efforts have been made to synthesize and characterize <span class="hlt">protein</span>-nanoparticle conjugates (<span class="hlt">protein</span>-NPs) for their promising applications in bionanotechnology. However, <span class="hlt">protein</span> <span class="hlt">concentration</span> determination in the <span class="hlt">protein</span>-NPs has so far not been reported. In this Letter, we present a simple and nondestructive approach to quantify the <span class="hlt">protein</span> <span class="hlt">concentration</span> in the <span class="hlt">protein</span>-NPs aqueous solution using circular dichroism (CD) spectroscopy. Carbon dots (∼4 nm), gold nanoparticles (∼10 nm), and polyethylene glycol (PEG, molecular weight ∼3000) were either physically mixed or covalently conjugated (not in the case of gold nanoparticles) with <span class="hlt">proteins</span> (human transferrin, human serum albumin, and ovalbumin). We were able to quantify the <span class="hlt">protein</span> <span class="hlt">concentration</span> in the <span class="hlt">protein</span>-nanoparticle conjugates using a calibration curve from the CD spectra. PMID:26070096</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2012JASMS..23.1522S','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2012JASMS..23.1522S"><span id="translatedtitle"><span class="hlt">Absolute</span> Quantification of Prion <span class="hlt">Protein</span> (90-231) Using Stable Isotope-Labeled Chymotryptic Peptide Standards in a LC-MRM AQUA Workflow</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Sturm, Robert; Sheynkman, Gloria; Booth, Clarissa; Smith, Lloyd M.; Pedersen, Joel A.; Li, Lingjun</p> <p>2012-09-01</p> <p>Substantial evidence indicates that the disease-associated conformer of the prion <span class="hlt">protein</span> (PrPTSE) constitutes the etiologic agent in prion diseases. These diseases affect multiple mammalian species. PrPTSE has the ability to convert the conformation of the normal prion <span class="hlt">protein</span> (PrPC) into a β-sheet rich form resistant to proteinase K digestion. Common immunological techniques lack the sensitivity to detect PrPTSE at subfemtomole levels, whereas animal bioassays, cell culture, and in vitro conversion assays offer higher sensitivity but lack the high-throughput the immunological assays offer. Mass spectrometry is an attractive alternative to the above assays as it offers high-throughput, direct measurement of a <span class="hlt">protein</span>'s signature peptide, often with subfemtomole sensitivities. Although a liquid chromatography-multiple reaction monitoring (LC-MRM) method has been reported for PrPTSE, the chemical composition and lack of amino acid sequence conservation of the signature peptide may compromise its accuracy and make it difficult to apply to multiple species. Here, we demonstrate that an alternative protease (chymotrypsin) can produce signature peptides suitable for a LC-MRM <span class="hlt">absolute</span> quantification (AQUA) experiment. The new method offers several advantages, including: (1) a chymotryptic signature peptide lacking chemically active residues (Cys, Met) that can confound assay accuracy; (2) low attomole limits of detection and quantitation (LOD and LOQ); and (3) a signature peptide retaining the same amino acid sequence across most mammals naturally susceptible to prion infection as well as important laboratory models. To the authors' knowledge, this is the first report on the use of a non-tryptic peptide in a LC-MRM AQUA workflow.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1216999','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1216999"><span id="translatedtitle">Effect of channelling on the <span class="hlt">concentration</span> of bulk-phase intermediates as cytosolic <span class="hlt">proteins</span> become more <span class="hlt">concentrated</span>.</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Kholodenko, B N; Westerhoff, H V; Cascante, M</p> <p>1996-01-01</p> <p>This paper shows that metabolic channelling can provide a mechanism for decreasing the <span class="hlt">concentration</span> of metabolites in the cytoplasm when cytosolic <span class="hlt">proteins</span> become more <span class="hlt">concentrated</span>. A dynamic complex catalysing the direct transfer of an intermediate is compared with the analogous pathway lacking a channel (an "ideal" pathway). In an ideal pathway a proportional increase in <span class="hlt">protein</span> content does not result in a change in the steady-state <span class="hlt">concentration</span> of the bulk-phase intermediate, whereas in a channelling pathway the bulk-phase intermediate either decreases or increases depending on the elemental rate constants within the enzyme mechanisms. When the <span class="hlt">concentration</span> of the enzymes are equal, the pool size decreases with increasing <span class="hlt">protein</span> <span class="hlt">concentration</span> if the elemental step depleting the bulk-phase intermediate exerts more control on its <span class="hlt">concentration</span> than the step supplying the intermediate. Results are illustrated numerically, and a simplified dynamic channel is analysed in which the <span class="hlt">concentration</span> of the enzyme-enzyme forms. For such a "hit-and-run" channel it is shown that, when the product-releasing step of the enzyme located upstream is close to equilibrium, the pool size decreases as the <span class="hlt">concentrations</span> of the enzymes increase in proportion, regardless of the rate, equilibrium constants and <span class="hlt">concentration</span> ratios of the two sequential enzymes. PMID:8611176</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://medlineplus.gov/ency/article/003649.htm','NIH-MEDLINEPLUS'); return false;" href="https://medlineplus.gov/ency/article/003649.htm"><span id="translatedtitle">Eosinophil count - <span class="hlt">absolute</span></span></a></p> <p><a target="_blank" href="http://medlineplus.gov/">MedlinePlus</a></p> <p></p> <p></p> <p>Eosinophils; <span class="hlt">Absolute</span> eosinophil count ... the white blood cell count to give the <span class="hlt">absolute</span> eosinophil count. ... than 500 cells per microliter (cells/mcL). Normal value ranges may vary slightly among different laboratories. Talk ...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=328894','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=328894"><span id="translatedtitle">Developing low cost feed grade soybean <span class="hlt">protein</span> <span class="hlt">concentrates</span> for aquaculture</span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>One emerging area in the global soy industry, particularly the U.S. soybean industry, has been developing soy-based feeds as an alternative <span class="hlt">protein</span> source to meet the growing needs of aquaculture in China and elsewhere. Traditionally, fishmeal is a key <span class="hlt">protein</span> ingredient in fish diets, but its sup...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27581485','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27581485"><span id="translatedtitle">Transient <span class="hlt">absolute</span> robustness in stochastic biochemical networks.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Enciso, German A</p> <p>2016-08-01</p> <p><span class="hlt">Absolute</span> robustness allows biochemical networks to sustain a consistent steady-state output in the face of <span class="hlt">protein</span> <span class="hlt">concentration</span> variability from cell to cell. This property is structural and can be determined from the topology of the network alone regardless of rate parameters. An important question regarding these systems is the effect of discrete biochemical noise in the dynamical behaviour. In this paper, a variable freezing technique is developed to show that under mild hypotheses the corresponding stochastic system has a transiently robust behaviour. Specifically, after finite time the distribution of the output approximates a Poisson distribution, centred around the deterministic mean. The approximation becomes increasingly accurate, and it holds for increasingly long finite times, as the total <span class="hlt">protein</span> <span class="hlt">concentrations</span> grow to infinity. In particular, the stochastic system retains a transient, <span class="hlt">absolutely</span> robust behaviour corresponding to the deterministic case. This result contrasts with the long-term dynamics of the stochastic system, which eventually must undergo an extinction event that eliminates robustness and is completely different from the deterministic dynamics. The transiently robust behaviour may be sufficient to carry out many forms of robust signal transduction and cellular decision-making in cellular organisms. PMID:27581485</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/biblio/22415704','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/biblio/22415704"><span id="translatedtitle">Accurate and <span class="hlt">absolute</span> diffusion measurements of Rhodamine 6G in low-<span class="hlt">concentration</span> aqueous solutions by the PGSE-WATERGATE sequence</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>Majer, G.; Zick, K.</p> <p>2015-04-28</p> <p>A pulsed field gradient spin-echo nuclear magnetic resonance (NMR) sequence with solvent suppression (PGSE-WATERGATE) was applied to accurately measure the diffusion coefficients of Rhodamine 6G (Rh6G) in low-<span class="hlt">concentration</span> aqueous solutions. Three samples with Rh6G <span class="hlt">concentrations</span> of C{sub Rh6G} = 1, 4.5, and 25 μM were investigated. The precise determination of the diffusion coefficients in this low-<span class="hlt">concentration</span> range was made possible by using a cryogenically cooled NMR probe and by the effective solvent suppression of the PGSE-WATERGATE sequence. The present results bridge the gap between diffusion data measured by fluorescence correlation spectroscopy in the single molecule limit and diffusivities obtained by pulsed field gradient NMR (PFG-NMR) without solvent suppression at higher <span class="hlt">concentrations</span>. To further extend the <span class="hlt">concentration</span> range, the diffusion coefficient of Rh6G was also measured on a sample with C{sub Rh6G} = 410 μM by PFG-NMR. The overall <span class="hlt">concentration</span> dependence of the Rh6G diffusion at 25 °C is discussed in terms of dimerization of the Rh6G molecules. The <span class="hlt">concentration</span>-dependent monomer/dimer proportion is deduced from the diffusion data.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/23968486','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/23968486"><span id="translatedtitle">Bioaccumulation of perfluoroalkyl substances by Daphnia magna in water with different types and <span class="hlt">concentrations</span> of <span class="hlt">protein</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Xia, Xinghui; Rabearisoa, Andry H; Jiang, Xiaoman; Dai, Zhineng</p> <p>2013-10-01</p> <p>Perfluoroalkyl substances (PFASs) are sometimes regarded as proteinophilic compounds, however, there is no research report about the effect of environmental <span class="hlt">protein</span> on the bioaccumulation of PFASs in waters. In the present study we investigated influences of <span class="hlt">protein</span> on the bioaccumulation of six kinds of PFASs by Daphnia magna in water; it included perfluorooctane sulfonate, perfluorooctanoic acid, perfluorononanoic acid, perfluorodecanoic acid, perfluoroundecanoic acid, and perfluorododecanoic acid. Two types of <span class="hlt">protein</span> including bovine albumin from animal and soy peptone from plant were compared and the effects of <span class="hlt">protein</span> <span class="hlt">concentration</span> were investigated. Both types of <span class="hlt">protein</span> at high <span class="hlt">concentrations</span> (10 and 20 mg L(-1)) suppressed the bioaccumulation of PFASs. When <span class="hlt">protein</span> <span class="hlt">concentration</span> increased from 0 to 20 mg L(-1), the decreasing ratios of the PFAS body burden (35.3-52.9%) in Daphnia magna induced by bovine albumin were significantly higher than those (22.0-36.6%) by soy peptone. The dialysis bag experiment results showed that the binding of PFASs to <span class="hlt">protein</span> followed the Freundlich isotherm, suggesting it is not a linear partitioning process but an adsorption-like process. The partition coefficients of PFASs between bovine albumin and water were higher compared to soy peptone; this resulted in higher reducing rates of freely dissolved <span class="hlt">concentrations</span> of PFASs with increasing bovine albumin <span class="hlt">concentration</span>, leading to a stronger suppression of PFAS bioaccumulation. However, the presence of both types of <span class="hlt">protein</span> with a low <span class="hlt">concentration</span> (1 mg L(-1)) enhanced the bioaccumulation of PFASs. Furthermore, the water-based bioaccumulation factor based on the freely dissolved <span class="hlt">concentrations</span> of PFASs even increased with and the depuration rate constants of PFASs from Daphnia magna decreased with <span class="hlt">protein</span> <span class="hlt">concentration</span>, suggesting that <span class="hlt">protein</span> would not only reduce the bioavailable <span class="hlt">concentrations</span> and uptake rates of PFASs but also lower the elimination rates of PFASs in</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/3625919','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/3625919"><span id="translatedtitle">Urea <span class="hlt">concentration</span> in collared peccary milk as an indicator of <span class="hlt">protein</span> nutritional status.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Lochmiller, R L; Hellgren, E C; Grant, W E; Varner, L W</p> <p>1987-07-01</p> <p>Milk urea nitrogen (UN) <span class="hlt">concentration</span> was examined as a possible index to <span class="hlt">protein</span>-energy intake in female collared peccaries (Tayassu tajacu). Captive adults were bred and assigned to one of four experimental diets through gestation and lactation. Females fed a high <span class="hlt">protein</span> diet produced milk with UN <span class="hlt">concentrations</span> exceeding those of low-<span class="hlt">protein</span>-fed females. A low energy intake tended to elevate UN <span class="hlt">concentrations</span> in milk.</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_4");'>4</a></li> <li><a href="#" onclick='return showDiv("page_5");'>5</a></li> <li class="active"><span>6</span></li> <li><a href="#" onclick='return showDiv("page_7");'>7</a></li> <li><a href="#" onclick='return showDiv("page_8");'>8</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_6 --> <div id="page_7" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_5");'>5</a></li> <li><a href="#" onclick='return showDiv("page_6");'>6</a></li> <li class="active"><span>7</span></li> <li><a href="#" onclick='return showDiv("page_8");'>8</a></li> <li><a href="#" onclick='return showDiv("page_9");'>9</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="121"> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2010AMTD....3.3675S','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2010AMTD....3.3675S"><span id="translatedtitle"><span class="hlt">Absolute</span> accuracy and sensitivity analysis of OP-FTIR retrievals of CO2, CH4 and CO over <span class="hlt">concentrations</span> representative of ''clean air'' and ''polluted plumes''</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Smith, T. E. L.; Wooster, M. J.; Tattaris, M.; Griffith, D. W. T.</p> <p>2010-08-01</p> <p>When compared to established point-sampling methods, Open-Path Fourier Transform Infrared (OP-FTIR) spectroscopy can provide path-integrated <span class="hlt">concentrations</span> of multiple gases simultaneously, in situ and near-continuously. <span class="hlt">Concentrations</span> can be retrieved from the measured IR spectra using a forward model coupled to a non-linear least squares fitting procedure, without requiring ''background'' spectral measurements unaffected by the gases of interest. However, few studies have investigated the accuracy of such retrievals for CO2, CH4 and CO, particularly across a broad <span class="hlt">concentration</span> range covering ambient to highly polluted air (e.g. from biomass burning or industrial plumes). Here we perform such an assessment using data collected by a field-portable FTIR spectrometer. The FTIR was positioned to view a fixed IR source placed at the other end of an IR-transparent cell filled with the gases of interest, whose target <span class="hlt">concentrations</span> were varied by up to two orders of magnitude. Retrievals made using the forward model are complicated by absorption line pressure broadening, the effects of temperature on absorption band shape and by convolution of the gas absorption lines and the instrument line shape (ILS). Despite this, with optimal forward model parameterisation (i.e. the wavenumber range used in the retrieval, gas temperature, pressure and ILS), <span class="hlt">concentration</span> retrievals for all gases were able to be made to within 5% of the true value. Sensitivity to the aforementioned model inputs was also investigated. CO retrievals were shown to be most sensitive to the ILS (a function of the assumed instrument FOV), which is due to the narrow nature of CO absorption lines and their consequent sensitivity to convolution with the ILS. Conversely, CO2 retrievals were most sensitive to assumed atmospheric parameters, particularly temperature. The analysis suggests that trace gas <span class="hlt">concentration</span> retrieval errors can remain well below 10%, even with the uncertainties in atmospheric pressure</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.gpo.gov/fdsys/pkg/CFR-2010-title21-vol3/pdf/CFR-2010-title21-vol3-sec172-385.pdf','CFR'); return false;" href="https://www.gpo.gov/fdsys/pkg/CFR-2010-title21-vol3/pdf/CFR-2010-title21-vol3-sec172-385.pdf"><span id="translatedtitle">21 CFR 172.385 - Whole fish <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="http://www.gpo.gov/fdsys/browse/collectionCfr.action?selectedYearFrom=2010&page.go=Go">Code of Federal Regulations, 2010 CFR</a></p> <p></p> <p>2010-04-01</p> <p>... supplement in manufactured food, the total fluoride content (expressed as F) of the finished food shall not... contents. It is prepared by solvent extraction of fat and moisture with isopropyl alcohol or with ethylene... additive meets the following specifications: (1) <span class="hlt">Protein</span> content (N × 6.25) shall not be less than...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/4003547','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/4003547"><span id="translatedtitle">Lymph flow, lymph <span class="hlt">protein</span> <span class="hlt">concentration</span>, and <span class="hlt">protein</span> output from rat small intestine.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Lee, J S</p> <p>1985-06-01</p> <p>Lymph flow (JL), lymph <span class="hlt">protein</span> <span class="hlt">concentration</span> (CL), and <span class="hlt">protein</span> output (JP) from the main intestinal lymph duct were determined. The basal JL from the mesenteric pedicle alone was the same as that from the mesenteric pedicle attached with a segment of the nonabsorbing intestine, indicating that the basal JL does not originate from the intestine but is totally from the region of the mesenteric pedicle. The basal CL was 3.5-3.8 g/100 ml. When the intestine was absorbing water, JL increased and CL decreased, but JP increased above the basal JP in the initial 20 min of water absorption and then decreased progressively with time. Furthermore, it was estimated that CL in the "excess lymph" (formed during water absorption) was 1.4 +/- 0.2 g/100 ml in the initial 10 min of water absorption and was zero or nearly so in the later periods. From this and other evidence, it is concluded that under various conditions without net water absorption rat small intestine does not produce lymph and that during water absorption there is no significant increase in capillary permeability or capillary filtration. Therefore, the excess lymph could be mostly derived from the fluid absorbed from the lumen of the intestine.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2011AMT.....4...97S','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2011AMT.....4...97S"><span id="translatedtitle"><span class="hlt">Absolute</span> accuracy and sensitivity analysis of OP-FTIR retrievals of CO2, CH4 and CO over <span class="hlt">concentrations</span> representative of "clean air" and "polluted plumes"</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Smith, T. E. L.; Wooster, M. J.; Tattaris, M.; Griffith, D. W. T.</p> <p>2011-01-01</p> <p>When compared to established point-sampling methods, Open-Path Fourier Transform Infrared (OP-FTIR) spectroscopy can provide path-integrated <span class="hlt">concentrations</span> of multiple gases simultaneously, in situ and near-continuously. The trace gas pathlength amounts can be retrieved from the measured IR spectra using a forward model coupled to a non-linear least squares fitting procedure, without requiring "background" spectral measurements unaffected by the gases of interest. However, few studies have investigated the accuracy of such retrievals for CO2, CH4 and CO, particularly across broad <span class="hlt">concentration</span> ranges covering those characteristic of ambient to highly polluted air (e.g. from biomass burning or industrial plumes). Here we perform such an assessment using data collected by a field-portable FTIR spectrometer. The FTIR was positioned to view a fixed IR source placed at the other end of an IR-transparent cell filled with the gases of interest, whose target <span class="hlt">concentrations</span> were varied by more than two orders of magnitude. Retrievals made using the model are complicated by absorption line pressure broadening, the effects of temperature on absorption band shape, and by convolution of the gas absorption lines and the instrument line shape (ILS). Despite this, with careful model parameterisation (i.e. the optimum wavenumber range, ILS, and assumed gas temperature and pressure for the retrieval), <span class="hlt">concentrations</span> for all target gases were able to be retrieved to within 5%. Sensitivity to the aforementioned model inputs was also investigated. CO retrievals were shown to be most sensitive to the ILS (a function of the assumed instrument field-of-view), which is due to the narrow nature of CO absorption lines and their consequent sensitivity to convolution with the ILS. Conversely, CO2 retrievals were most sensitive to assumed atmospheric parameters, particularly gas temperature. Our findings provide confidence that FTIR-derived trace gas retrievals of CO2, CH4 and CO based on</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/24329978','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/24329978"><span id="translatedtitle">The effect of feed solids <span class="hlt">concentration</span> and inlet temperature on the flavor of spray dried whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Park, Curtis W; Bastian, Eric; Farkas, Brian; Drake, MaryAnne</p> <p>2014-01-01</p> <p>Previous research has demonstrated that unit operations in whey <span class="hlt">protein</span> manufacture promote off-flavor production in whey <span class="hlt">protein</span>. The objective of this study was to determine the effects of feed solids <span class="hlt">concentration</span> in liquid retentate and spray drier inlet temperature on the flavor of dried whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC). Cheddar cheese whey was manufactured, fat-separated, pasteurized, bleached (250 ppm hydrogen peroxide), and ultrafiltered (UF) to obtain WPC80 retentate (25% solids, wt/wt). The liquid retentate was then diluted with deionized water to the following solids <span class="hlt">concentrations</span>: 25%, 18%, and 10%. Each of the treatments was then spray dried at the following temperatures: 180 °C, 200 °C, and 220 °C. The experiment was replicated 3 times. Flavor of the WPC80 was evaluated by sensory and instrumental analyses. Particle size and surface free fat were also analyzed. Both main effects (solids <span class="hlt">concentration</span> and inlet temperature) and interactions were investigated. WPC80 spray dried at 10% feed solids <span class="hlt">concentration</span> had increased surface free fat, increased intensities of overall aroma, cabbage and cardboard flavors and increased <span class="hlt">concentrations</span> of pentanal, hexanal, heptanal, decanal, (E)2-decenal, DMTS, DMDS, and 2,4-decadienal (P < 0.05) compared to WPC80 spray dried at 25% feed solids. Product spray dried at lower inlet temperature also had increased surface free fat and increased intensity of cardboard flavor and increased <span class="hlt">concentrations</span> of pentanal, (Z)4-heptenal, nonanal, decanal, 2,4-nonadienal, 2,4-decadienal, and 2- and 3-methyl butanal (P < 0.05) compared to product spray dried at higher inlet temperature. Particle size was higher for powders from increased feed solids <span class="hlt">concentration</span> and increased inlet temperature (P < 0.05). An increase in feed solids <span class="hlt">concentration</span> in the liquid retentate and inlet temperature within the parameters evaluated decreased off-flavor intensity in the resulting WPC80. PMID:24329978</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/24329978','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/24329978"><span id="translatedtitle">The effect of feed solids <span class="hlt">concentration</span> and inlet temperature on the flavor of spray dried whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Park, Curtis W; Bastian, Eric; Farkas, Brian; Drake, MaryAnne</p> <p>2014-01-01</p> <p>Previous research has demonstrated that unit operations in whey <span class="hlt">protein</span> manufacture promote off-flavor production in whey <span class="hlt">protein</span>. The objective of this study was to determine the effects of feed solids <span class="hlt">concentration</span> in liquid retentate and spray drier inlet temperature on the flavor of dried whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC). Cheddar cheese whey was manufactured, fat-separated, pasteurized, bleached (250 ppm hydrogen peroxide), and ultrafiltered (UF) to obtain WPC80 retentate (25% solids, wt/wt). The liquid retentate was then diluted with deionized water to the following solids <span class="hlt">concentrations</span>: 25%, 18%, and 10%. Each of the treatments was then spray dried at the following temperatures: 180 °C, 200 °C, and 220 °C. The experiment was replicated 3 times. Flavor of the WPC80 was evaluated by sensory and instrumental analyses. Particle size and surface free fat were also analyzed. Both main effects (solids <span class="hlt">concentration</span> and inlet temperature) and interactions were investigated. WPC80 spray dried at 10% feed solids <span class="hlt">concentration</span> had increased surface free fat, increased intensities of overall aroma, cabbage and cardboard flavors and increased <span class="hlt">concentrations</span> of pentanal, hexanal, heptanal, decanal, (E)2-decenal, DMTS, DMDS, and 2,4-decadienal (P < 0.05) compared to WPC80 spray dried at 25% feed solids. Product spray dried at lower inlet temperature also had increased surface free fat and increased intensity of cardboard flavor and increased <span class="hlt">concentrations</span> of pentanal, (Z)4-heptenal, nonanal, decanal, 2,4-nonadienal, 2,4-decadienal, and 2- and 3-methyl butanal (P < 0.05) compared to product spray dried at higher inlet temperature. Particle size was higher for powders from increased feed solids <span class="hlt">concentration</span> and increased inlet temperature (P < 0.05). An increase in feed solids <span class="hlt">concentration</span> in the liquid retentate and inlet temperature within the parameters evaluated decreased off-flavor intensity in the resulting WPC80.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27546789','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27546789"><span id="translatedtitle">RNA Remodeling Activity of DEAD Box <span class="hlt">Proteins</span> Tuned by <span class="hlt">Protein</span> <span class="hlt">Concentration</span>, RNA Length, and ATP.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Kim, Younghoon; Myong, Sua</p> <p>2016-09-01</p> <p>DEAD box RNA helicases play central roles in RNP biogenesis. We reported earlier that LAF-1, a DEAD box RNA helicase in C. elegans, dynamically interacts with RNA and that the interaction likely contributes to the fluidity of RNP droplets. Here we investigate the molecular basis of the interaction of RNA with LAF-1 and its human homolog, DDX3X. We show that both LAF-1 and DDX3X, at low <span class="hlt">concentrations</span>, are monomers that induce tight compaction of single-stranded RNA. At high <span class="hlt">concentrations</span>, the <span class="hlt">proteins</span> are multimeric and dynamically interact with RNA in an RNA length-dependent manner. The dynamic LAF-1-RNA interaction stimulates RNA annealing activity. ATP adversely affects the RNA remodeling ability of LAF-1 by suppressing the affinity, dynamics, and annealing activity of LAF-1, suggesting that ATP may promote disassembly of the RNP complex. Based on our results, we postulate a plausible molecular mechanism underlying the dynamic equilibrium of the LAF-1 RNP complex. PMID:27546789</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/2343735','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/2343735"><span id="translatedtitle"><span class="hlt">Protein</span> binding of prilocaine in human plasma: influence of <span class="hlt">concentration</span>, pH and temperature.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Bachmann, B; Biscoping, J; Sinning, E; Hempelmann, G</p> <p>1990-05-01</p> <p><span class="hlt">Protein</span> binding of prilocaine was investigated in vitro under various conditions of changing pH, temperature and total plasma <span class="hlt">concentration</span> by means of HPLC with UV-detection and ultrafiltration. Whereas changes in temperature (25 degrees C-40 degrees C) and pH (pH 5-pH 10) influenced <span class="hlt">protein</span> binding markedly, rising plasma <span class="hlt">concentrations</span> up to 16 micrograms/ml did not affect plasma <span class="hlt">protein</span> binding significantly. This may be a possible explanation for clinical evidence of low toxicity associated with the use of prilocaine. Discussions concerning <span class="hlt">protein</span> binding of local anaesthetics should always be based on defined ambient conditions (pH, temperature, <span class="hlt">concentration</span>).</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/servlets/purl/1042637','DOE-PATENT-XML'); return false;" href="http://www.osti.gov/scitech/servlets/purl/1042637"><span id="translatedtitle"><span class="hlt">Absolute</span> nuclear material assay</span></a></p> <p><a target="_blank" href="http://www.osti.gov/doepatents">DOEpatents</a></p> <p>Prasad, Manoj K.; Snyderman, Neal J.; Rowland, Mark S.</p> <p>2012-05-15</p> <p>A method of <span class="hlt">absolute</span> nuclear material assay of an unknown source comprising counting neutrons from the unknown source and providing an <span class="hlt">absolute</span> nuclear material assay utilizing a model to optimally compare to the measured count distributions. In one embodiment, the step of providing an <span class="hlt">absolute</span> nuclear material assay comprises utilizing a random sampling of analytically computed fission chain distributions to generate a continuous time-evolving sequence of event-counts by spreading the fission chain distribution in time.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/servlets/purl/993087','DOE-PATENT-XML'); return false;" href="http://www.osti.gov/scitech/servlets/purl/993087"><span id="translatedtitle"><span class="hlt">Absolute</span> nuclear material assay</span></a></p> <p><a target="_blank" href="http://www.osti.gov/doepatents">DOEpatents</a></p> <p>Prasad, Manoj K.; Snyderman, Neal J.; Rowland, Mark S.</p> <p>2010-07-13</p> <p>A method of <span class="hlt">absolute</span> nuclear material assay of an unknown source comprising counting neutrons from the unknown source and providing an <span class="hlt">absolute</span> nuclear material assay utilizing a model to optimally compare to the measured count distributions. In one embodiment, the step of providing an <span class="hlt">absolute</span> nuclear material assay comprises utilizing a random sampling of analytically computed fission chain distributions to generate a continuous time-evolving sequence of event-counts by spreading the fission chain distribution in time.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/11745172','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/11745172"><span id="translatedtitle"><span class="hlt">Protein</span> modification during anti-viral heat-treatment bioprocessing of factor VIII <span class="hlt">concentrates</span>, factor IX <span class="hlt">concentrates</span>, and model <span class="hlt">proteins</span> in the presence of sucrose.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Smales, C Mark; Pepper, Duncan S; James, David C</p> <p>2002-01-01</p> <p>To ensure the optimal safety of plasma derived and new generation recombinant <span class="hlt">proteins</span>, heat treatment is customarily applied in the manufacturing of such biopharmaceuticals as a means of viral inactivation. In subjecting <span class="hlt">proteins</span> to anti-viral heat-treatment it is necessary to use high <span class="hlt">concentrations</span> of thermostabilizing excipients to prevent <span class="hlt">protein</span> damage, and it is therefore imperative that the correct balance between bioprocessing conditions, maintenance of <span class="hlt">protein</span> integrity and virus kill is found. In this study we have utilized model <span class="hlt">proteins</span> (lysozyme, fetuin, and human serum albumin) and plasma-derived therapeutic <span class="hlt">proteins</span> (factor VIII and factor IX) to investigate the <span class="hlt">protein</span> modifications that occur during anti-viral heat treatment. Specifically, we investigated the relationship between bioprocessing conditions and the type and extent of <span class="hlt">protein</span> modification under a variety of industrially relevant wet and lyophilized heat treatments using sucrose as a thermostabilizing agent. Heat treatment led to the formation of disulfide crosslinks and aggregates in <span class="hlt">proteins</span> containing free cysteine residues. Terminal oligosaccharide sialic acid residues were hydrolyzed from the glycan moieties of glycoproteins during anti-viral heat treatment. Heat treatment promoted sucrose hydrolysis to yield glucose and fructose, leading, in turn, to the glycation of lysine amino groups in those <span class="hlt">proteins</span> containing di-lysine motifs. During extended hear treatments, 1,2-dicarbonyl type advanced glycation end-products were also formed. Glycation-type modifications were more prevalent in wet heat-treated <span class="hlt">protein</span> formulations.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=212459','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=212459"><span id="translatedtitle">P1 plasmid replication: measurement of initiator <span class="hlt">protein</span> <span class="hlt">concentration</span> in vivo.</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Swack, J A; Pal, S K; Mason, R J; Abeles, A L; Chattoraj, D K</p> <p>1987-01-01</p> <p>To study the functions of the mini-P1 replication initiation <span class="hlt">protein</span> RepA quantitatively, we have developed a method to measure RepA <span class="hlt">concentration</span> by using immunoblotting. In vivo, there are about 20 RepA dimers per unit-copy plasmid DNA. RepA was deduced to be a dimer from gel filtration of the purified <span class="hlt">protein</span>. Since there are 14 binding sites of the <span class="hlt">protein</span> per replicon, the physiological <span class="hlt">concentration</span> of the <span class="hlt">protein</span> appears to be sufficiently low to be a rate-limiting factor for replication. Autoregulation is apparently responsible for the low <span class="hlt">protein</span> level; at the physiological <span class="hlt">concentration</span> of the <span class="hlt">protein</span>, the repA promoter retains only 0.1% of its full activity as determined by gene fusions to lacZ. When the <span class="hlt">concentration</span> is further decreased by a factor of 3 or increased by a factor of 40, replication is no longer detectable. Images PMID:3611028</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27121643','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27121643"><span id="translatedtitle">Quantifying Nanomolar <span class="hlt">Protein</span> <span class="hlt">Concentrations</span> Using Designed DNA Carriers and Solid-State Nanopores.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Kong, Jinglin; Bell, Nicholas A W; Keyser, Ulrich F</p> <p>2016-06-01</p> <p>Designed "DNA carriers" have been proposed as a new method for nanopore based specific <span class="hlt">protein</span> detection. In this system, target <span class="hlt">protein</span> molecules bind to a long DNA strand at a defined position creating a second level transient current drop against the background DNA translocation. Here, we demonstrate the ability of this system to quantify <span class="hlt">protein</span> <span class="hlt">concentrations</span> in the nanomolar range. After incubation with target <span class="hlt">protein</span> at different <span class="hlt">concentrations</span>, the fraction of DNA translocations showing a secondary current spike allows for the quantification of the corresponding <span class="hlt">protein</span> <span class="hlt">concentration</span>. For our proof-of-principle experiments we use two standard binding systems, biotin-streptavidin and digoxigenin-antidigoxigenin, that allow for measurements of the <span class="hlt">concentration</span> down to the low nanomolar range. The results demonstrate the potential for a novel quantitative and specific <span class="hlt">protein</span> detection scheme using the DNA carrier method.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26617031','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26617031"><span id="translatedtitle">Effects of enzymatic dephosphorylation on infant in vitro gastrointestinal digestibility of milk <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Liu, Dasong; Wang, Yuanyuan; Yu, Yun; Hu, Jinhua; Lu, Naiyan; Regenstein, Joe M; Wang, Miao; Zhou, Peng</p> <p>2016-04-15</p> <p>This study investigated the effects of dephosphorylation extent on infant in vitro gastric clotting property and gastrointestinal digestibility of milk <span class="hlt">protein</span> <span class="hlt">concentrate</span>. Dephosphorylation was affected by phosphatase type and incubation pH. A series of milk <span class="hlt">protein</span> <span class="hlt">concentrate</span> with 0-69% dephosphorylation were obtained by incubation with calf intestinal alkaline phosphatase at pH 6.5 for 0-420 min. Both β- and αs1-caseins in the modified milk <span class="hlt">protein</span> <span class="hlt">concentrate</span> showed multiply dephosphorylated isoforms with different numbers of phosphate groups depending on the extent of dephosphorylation. With increased dephosphorylation of milk <span class="hlt">protein</span> <span class="hlt">concentrate</span>, the gastric clotting extent decreased and the gastrointestinal digestibility increased under infant in vitro conditions. These results suggested the potential of developing a dephosphorylated milk <span class="hlt">protein</span> <span class="hlt">concentrate</span>, with improved gastric clotting property and gastrointestinal digestibility, to simulate the multiply phosphorylated patterns of human casein and hence to further the humanization of infant formula on a molecular level.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=318601','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=318601"><span id="translatedtitle">Physical and chemical changes in whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> stored at elevated temperature and humidity</span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>The chemistry of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) under adverse storage conditions was monitored to provide information on shelf life in hot, humid areas. WPC34 (34.9 g <span class="hlt">protein</span>/100 g) and WPC80 (76.8 g <span class="hlt">protein</span>/100 g) were stored for up to 18 mo under ambient conditions and at elevated temperature and...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/24819334','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/24819334"><span id="translatedtitle">Influence of sorbitol on <span class="hlt">protein</span> crowding in solution and freeze-<span class="hlt">concentrated</span> phases.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Khodadadi, S; Clark, N J; McAuley, A; Cristiglio, V; Curtis, J E; Shalaev, E Y; Krueger, S</p> <p>2014-06-21</p> <p>Small-angle neutron scattering was employed to study <span class="hlt">protein</span> crowding under freezing conditions that mimic those used in pharmaceutical processing. The results demonstrate that, although there is an increase in heterogeneity as the temperature is reduced, sorbitol reduces <span class="hlt">protein</span> crowding in both solution and freeze-<span class="hlt">concentrated</span> phases, thus protecting the <span class="hlt">protein</span> from forming oligomers or irreversible aggregates.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3787774','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3787774"><span id="translatedtitle">Molecular dynamics simulations of membrane <span class="hlt">proteins</span> under asymmetric ionic <span class="hlt">concentrations</span></span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Khalili-Araghi, Fatemeh; Ziervogel, Brigitte; Gumbart, James C.</p> <p>2013-01-01</p> <p>A computational method is developed to allow molecular dynamics simulations of biomembrane systems under realistic ionic gradients and asymmetric salt <span class="hlt">concentrations</span> while maintaining the conventional periodic boundary conditions required to minimize finite-size effects in an all-atom explicit solvent representation. The method, which consists of introducing a nonperiodic energy step acting on the ionic species at the edge of the simulation cell, is first tested with illustrative applications to a simple membrane slab model and a phospholipid membrane bilayer. The nonperiodic energy-step method is then used to calculate the reversal potential of the bacterial porin OmpF, a large cation-specific β-barrel channel, by simulating the I-V curve under an asymmetric 10:1 KCl <span class="hlt">concentration</span> gradient. The calculated reversal potential of 28.6 mV is found to be in excellent agreement with the values of 26–27 mV measured from lipid bilayer experiments, thereby demonstrating that the method allows realistic simulations of nonequilibrium membrane transport with quantitative accuracy. As a final example, the pore domain of Kv1.2, a highly selective voltage-activated K+ channel, is simulated in a lipid bilayer under conditions that recreate, for the first time, the physiological K+ and Na+ <span class="hlt">concentration</span> gradients and the electrostatic potential difference of living cells. PMID:24081985</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/7826189','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/7826189"><span id="translatedtitle">Effect of succinylation of oil palm <span class="hlt">protein</span> <span class="hlt">concentrates</span> on the functional properties.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Pacheco de Delahaye, E</p> <p>1993-06-01</p> <p>Defatted kernel flour of oil palm, grounded to 60 mesh, was taken as raw material to produce <span class="hlt">protein</span> <span class="hlt">concentrates</span> (70.8%) <span class="hlt">protein</span>) which were succinylated at different levels (0.05; 0.2 and 0.6). The extent of acylation was measured as percentage of lysine modification reaching values from 18.4% to 48.6%. <span class="hlt">Protein</span> <span class="hlt">concentrate</span> functional properties were determined: Water solubility (pH 2-10); water absorption (320%); oil absorption (2.2 ml oil/g), emulsion activity and emulsion stability (28-46%). The functional properties were enhanced by succinylation if compared with the untreated <span class="hlt">protein</span> <span class="hlt">concentrate</span>, however, "in vitro" digestibility was not affected, by succinylation. In summary, the results of this study indicate that acylation using succinyl anhydride can improve the functional properties of oil palm <span class="hlt">protein</span> <span class="hlt">concentrate</span> over those without such treatment.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27207010','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27207010"><span id="translatedtitle">Soybean bio-refinery platform: enzymatic process for production of soy <span class="hlt">protein</span> <span class="hlt">concentrate</span>, soy <span class="hlt">protein</span> isolate and fermentable sugar syrup.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Loman, Abdullah Al; Islam, S M Mahfuzul; Li, Qian; Ju, Lu-Kwang</p> <p>2016-10-01</p> <p>Soybean carbohydrate is often found to limit the use of <span class="hlt">protein</span> in soy flour as food and animal feed due to its indigestibility to monogastric animal. In the current study, an enzymatic process was developed to produce not only soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> and soy <span class="hlt">protein</span> isolate without indigestible carbohydrate but also soluble reducing sugar as potential fermentation feedstock. For increasing <span class="hlt">protein</span> content in the product and maximizing <span class="hlt">protein</span> recovery, the process was optimized to include the following steps: hydrolysis of soy flour using an Aspergillus niger enzyme system; separation of the solid and liquid by centrifugation (10 min at 7500×g); an optional step of washing to remove entrapped hydrolysate from the <span class="hlt">protein</span>-rich wet solid stream by ethanol (at an ethanol-to-wet-solid ratio (v/w) of 10, resulting in a liquid phase of approximately 60 % ethanol); and a final precipitation of residual <span class="hlt">protein</span> from the sugar-rich liquid stream by heat treatment (30 min at 95 °C). Starting from 100 g soy flour, this process would produce approximately 54 g soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> with 70 % <span class="hlt">protein</span> (or, including the optional solid wash, 43 g with 80 % <span class="hlt">protein</span>), 9 g soy <span class="hlt">protein</span> isolate with 89 % <span class="hlt">protein</span>, and 280 ml syrup of 60 g/l reducing sugar. The amino acid composition of the soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> produced was comparable to that of the starting soy flour. Enzymes produced by three fungal species, A. niger, Trichoderma reesei, and Aspergillus aculeatus, were also evaluated for effectiveness to use in this process. PMID:27207010</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27207010','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27207010"><span id="translatedtitle">Soybean bio-refinery platform: enzymatic process for production of soy <span class="hlt">protein</span> <span class="hlt">concentrate</span>, soy <span class="hlt">protein</span> isolate and fermentable sugar syrup.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Loman, Abdullah Al; Islam, S M Mahfuzul; Li, Qian; Ju, Lu-Kwang</p> <p>2016-10-01</p> <p>Soybean carbohydrate is often found to limit the use of <span class="hlt">protein</span> in soy flour as food and animal feed due to its indigestibility to monogastric animal. In the current study, an enzymatic process was developed to produce not only soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> and soy <span class="hlt">protein</span> isolate without indigestible carbohydrate but also soluble reducing sugar as potential fermentation feedstock. For increasing <span class="hlt">protein</span> content in the product and maximizing <span class="hlt">protein</span> recovery, the process was optimized to include the following steps: hydrolysis of soy flour using an Aspergillus niger enzyme system; separation of the solid and liquid by centrifugation (10 min at 7500×g); an optional step of washing to remove entrapped hydrolysate from the <span class="hlt">protein</span>-rich wet solid stream by ethanol (at an ethanol-to-wet-solid ratio (v/w) of 10, resulting in a liquid phase of approximately 60 % ethanol); and a final precipitation of residual <span class="hlt">protein</span> from the sugar-rich liquid stream by heat treatment (30 min at 95 °C). Starting from 100 g soy flour, this process would produce approximately 54 g soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> with 70 % <span class="hlt">protein</span> (or, including the optional solid wash, 43 g with 80 % <span class="hlt">protein</span>), 9 g soy <span class="hlt">protein</span> isolate with 89 % <span class="hlt">protein</span>, and 280 ml syrup of 60 g/l reducing sugar. The amino acid composition of the soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> produced was comparable to that of the starting soy flour. Enzymes produced by three fungal species, A. niger, Trichoderma reesei, and Aspergillus aculeatus, were also evaluated for effectiveness to use in this process.</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_5");'>5</a></li> <li><a href="#" onclick='return showDiv("page_6");'>6</a></li> <li class="active"><span>7</span></li> <li><a href="#" onclick='return showDiv("page_8");'>8</a></li> <li><a href="#" onclick='return showDiv("page_9");'>9</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_7 --> <div id="page_8" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_6");'>6</a></li> <li><a href="#" onclick='return showDiv("page_7");'>7</a></li> <li class="active"><span>8</span></li> <li><a href="#" onclick='return showDiv("page_9");'>9</a></li> <li><a href="#" onclick='return showDiv("page_10");'>10</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="141"> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/22408408','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/22408408"><span id="translatedtitle">Composition, structure and functional properties of <span class="hlt">protein</span> <span class="hlt">concentrates</span> and isolates produced from walnut (Juglans regia L.).</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Mao, Xiaoying; Hua, Yufei</p> <p>2012-01-01</p> <p>In this study, composition, structure and the functional properties of <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) and <span class="hlt">protein</span> isolate (WPI) produced from defatted walnut flour (DFWF) were investigated. The results showed that the composition and structure of walnut <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) and walnut <span class="hlt">protein</span> isolate (WPI) were significantly different. The molecular weight distribution of WPI was uniform and the <span class="hlt">protein</span> composition of DFWF and WPC was complex with the <span class="hlt">protein</span> aggregation. H(0) of WPC was significantly higher (p < 0.05) than those of DFWF and WPI, whilst WPI had a higher H(0) compared to DFWF. The secondary structure of WPI was similar to WPC. WPI showed big flaky plate like structures; whereas WPC appeared as a small flaky and more compact structure. The most functional properties of WPI were better than WPC. In comparing most functional properties of WPI and WPC with soybean <span class="hlt">protein</span> <span class="hlt">concentrate</span> and isolate, WPI and WPC showed higher fat absorption capacity (FAC). Emulsifying properties and foam properties of WPC and WPI in alkaline pH were comparable with that of soybean <span class="hlt">protein</span> <span class="hlt">concentrate</span> and isolate. Walnut <span class="hlt">protein</span> <span class="hlt">concentrates</span> and isolates can be considered as potential functional food ingredients.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27197958','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27197958"><span id="translatedtitle">Large-scale multiplex <span class="hlt">absolute</span> <span class="hlt">protein</span> quantification of drug-metabolizing enzymes and transporters in human intestine, liver, and kidney microsomes by SWATH-MS: Comparison with MRM/SRM and HR-MRM/PRM.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Nakamura, Kenji; Hirayama-Kurogi, Mio; Ito, Shingo; Kuno, Takuya; Yoneyama, Toshihiro; Obuchi, Wataru; Terasaki, Tetsuya; Ohtsuki, Sumio</p> <p>2016-08-01</p> <p>The purpose of the present study was to examine simultaneously the <span class="hlt">absolute</span> <span class="hlt">protein</span> amounts of 152 membrane and membrane-associated <span class="hlt">proteins</span>, including 30 metabolizing enzymes and 107 transporters, in pooled microsomal fractions of human liver, kidney, and intestine by means of SWATH-MS with stable isotope-labeled internal standard peptides, and to compare the results with those obtained by MRM/SRM and high resolution (HR)-MRM/PRM. The <span class="hlt">protein</span> expression levels of 27 metabolizing enzymes, 54 transporters, and six other membrane <span class="hlt">proteins</span> were quantitated by SWATH-MS; other targets were below the lower limits of quantitation. Most of the values determined by SWATH-MS differed by less than 50% from those obtained by MRM/SRM or HR-MRM/PRM. Various metabolizing enzymes were expressed in liver microsomes more abundantly than in other microsomes. Ten, 13, and eight transporters listed as important for drugs by International Transporter Consortium were quantified in liver, kidney, and intestinal microsomes, respectively. Our results indicate that SWATH-MS enables large-scale multiplex <span class="hlt">absolute</span> <span class="hlt">protein</span> quantification while retaining similar quantitative capability to MRM/SRM or HR-MRM/PRM. SWATH-MS is expected to be useful methodology in the context of drug development for elucidating the molecular mechanisms of drug absorption, metabolism, and excretion in the human body based on <span class="hlt">protein</span> profile information.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25485892','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25485892"><span id="translatedtitle">Whey <span class="hlt">protein</span> supplementation increases methionine intake but not homocysteine plasma <span class="hlt">concentration</span> in rats.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Deminice, Rafael; Comparotto, Hugo; Jordao, Alceu Afonso</p> <p>2015-01-01</p> <p>The purpose of this study was to examine the effects of whey <span class="hlt">protein</span> supplementation on homocysteine (Hcy) metabolism and liver oxidative stress in rats. Twenty-four rats were divided into 3 groups (n = 8) to receive one of the following diets for 4 weeks: control diet (C), whey <span class="hlt">protein</span>-composed diet (WP), and whey <span class="hlt">protein</span>-supplemented diet (WPS). The C and WP diets consisted of AIN-93 with 20% casein and 20% whey <span class="hlt">protein</span> as <span class="hlt">protein</span> source, respectively. WPS was AIN-93 (20% casein) supplemented by the addition of 20% (w/w) whey <span class="hlt">protein</span>. Four weeks of ingesting a WPS diet resulted in a significantly higher (P < 0.05) total <span class="hlt">protein</span> and methionine intakes. Although a significant increase (P < 0.05) in the hepatic S-adenosylmethionine and S-adenosylhomocysteine levels occurred in WPS group compared with C and WP, no significant change was observed in plasma Hcy <span class="hlt">concentration</span> between groups. Furthermore, the levels of lipid hydroperoxides and advanced oxidation <span class="hlt">protein</span> products, known liver oxidative stress markers, were increased in the WPS group compared with the C group. In addition, no change in glutathione liver <span class="hlt">concentration</span> was observed in any of the groups studied. In conclusion, whey <span class="hlt">protein</span> supplementation increases methionine intake substantially; however, it does not change plasma Hcy <span class="hlt">concentrations</span>. On the other hand, increased hepatic oxidative stress markers were observed in whey <span class="hlt">protein</span> supplemented rats were probably due to high <span class="hlt">protein</span> intake.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27322507','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27322507"><span id="translatedtitle">The evaluation of NT-proCNP, C-reactive <span class="hlt">protein</span> and serum amyloid A <span class="hlt">protein</span> <span class="hlt">concentration</span> in patients with multiple myeloma undergoing stem cell transplantation.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Tomasiuk, Ryszard; Gawroński, Krzysztof; Rzepecki, Piotr; Rabijewski, Michał; Cacko, Marek</p> <p>2016-08-01</p> <p>The importance of proinflamatory cytokines and acute phase <span class="hlt">proteins</span> in pathogenesis and progression of MM is well known. However, there are any studies evaluating the role of NT-proCN in management and treatment of MM. The aim of our study was to evaluate the <span class="hlt">concentration</span> of NT-proCNP and acute phase <span class="hlt">proteins</span> in patients with MM before and after stem cell transplantation. We involved 40 newly diagnosed MM patients in stage III according to the Durie-Salmon classification and treated with high dose of melphalan (200mg/m2) prior to ASCT. <span class="hlt">Concentration</span> of NT-proCNP, hs-CRP and SAA were measured before conditioning treatment and every 4days until the 24th day after stem cell infusion. We observed low NT-proCNP levels before conditioning treatment (0.121±0.04pmol/l), the higher in day on ASCT (0.28±0.14pmol/l). Further we showed significant gradual increase <span class="hlt">concentration</span> of NT-proCNP up to 12days after stem cells infusion (1.07±0.72pmol/l). The kinetics of hs-CRP and SAA levels were similar to NT-proCNP. We showed positive correlation between NT-proCNP levels and <span class="hlt">absolute</span> neutrophil and platelets count in patients after ASCT. NT-proCNP can be useful parameter to assess effectiveness of treatment and monitoring of hematopoetic recovery time in patients with MM after stem cell transplantations. PMID:27322507</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/25876988','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/25876988"><span id="translatedtitle"><span class="hlt">Concentrate</span> reduction and sequential roughage offer to dairy cows: effects on milk <span class="hlt">protein</span> yield, <span class="hlt">protein</span> efficiency and milk quality.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Leiber, Florian; Dorn, Katharina; Probst, Johanna K; Isensee, Anne; Ackermann, Nick; Kuhn, Anton; Spengler Neff, Anet</p> <p>2015-08-01</p> <p>An experiment was conducted during 6 weeks to evaluate effects of a reduced dietary level of <span class="hlt">protein</span>-rich <span class="hlt">concentrates</span> in a moderate dairy production system on cows' performance, <span class="hlt">protein</span> efficiency and milk quality including fatty acid profiles. Twenty-three lactating cows (Swiss Fleckvieh) were assigned either to a group receiving on average 2.4 kg/d individually fed <span class="hlt">concentrates</span> (Prot+, n = 12) or to a group receiving no individually fed <span class="hlt">concentrates</span> (Prot-, n = 11). All cows had ad-libitum access to a total mixed ration (TMR) mainly based on grass and maize silage, hay and little potatoes and soybean cake. In weeks 4-6 of the experiment, part of the hay was excluded from the TMR, and fed separately in the morning. Individual feed intake and milk yield were recorded during weeks 3 and 6 of the experiment; at the same time feed, faeces and milk samples were collected twice per week for analyses. Data were processed in linear mixed models. Omission of individual <span class="hlt">concentrates</span> in Prot- was fully compensated by higher roughage intake in terms of dry matter. Crude <span class="hlt">protein</span> (CP) and net energy intake was almost maintained. Despite a lower apparent CP digestibility in Prot-, the ratio of milk <span class="hlt">protein</span> to ingested CP was the same in both groups, indicating a higher ruminal utilisation of degraded CP in Prot-. This corresponded with lower milk urea <span class="hlt">concentrations</span> in Prot-. Milk quality was affected in terms of lower <span class="hlt">concentrations</span> of linoleic and conjugated linoleic acid in milk fat of Prot-. <span class="hlt">Concentrations</span> of odd- and branched-chain fatty acids in milk were increased in Prot-. Sequential offer of hay and TMR did not lead to considerable effects in intake, efficiency and milk quality. In conclusion, the results indicate that the efficiency of feed <span class="hlt">protein</span> utilisation for milk <span class="hlt">protein</span> is not impaired if <span class="hlt">concentrates</span> are reduced in a moderate- to low-input dairy production system. PMID:25876988</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/biblio/5553886','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/biblio/5553886"><span id="translatedtitle">Effect of membrane <span class="hlt">protein</span> <span class="hlt">concentration</span> on binding of /sup 3/H-imipramine in human platelets</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>Barkai, A.I.; Kowalik, S.; Baron, M.</p> <p>1985-02-01</p> <p>Binding of /sup 3/H-imipramine to platelet membranes has been implicated as a marker for depression. Comparing /sup 3/H-IMI binding between depressed patients and normal subjects we observed an increase in the dissociation constant Kd with increasing membrane <span class="hlt">protein</span>. This phenomenon was studied more rigorously in five normal subjects. Platelet membranes were prepared and adjusted to four <span class="hlt">concentrations</span> of <span class="hlt">protein</span> ranging from 100 to 800 micrograms/ml. The /sup 3/H-IMI binding parameters of maximum binding sites number (Bmax) and Kd were obtained by Scatchard analysis at each membrane <span class="hlt">concentration</span>. A positive linear relationship was found between K/sub d/ values and the <span class="hlt">concentration</span> of membrane <span class="hlt">protein</span> in the assay, but no change was observed in Bmax. The variability in Kd values reported in the literature may be accounted for in part by the different <span class="hlt">concentrations</span> of membrane <span class="hlt">protein</span> used in various studies.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26551210','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26551210"><span id="translatedtitle">The elution of certain <span class="hlt">protein</span> affinity tags with millimolar <span class="hlt">concentrations</span> of diclofenac.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Baliova, Martina; Juhasova, Anna; Jursky, Frantisek</p> <p>2015-12-01</p> <p>Diclofenac (2-[(2, 6-dichlorophenyl)amino] benzeneacetic acid) is a sparingly soluble, nonsteroidal anti-inflammatory drug therapeutically acting at low micromolar <span class="hlt">concentrations</span>. In pH range from 8 to 11, its aqueous solubility can be increased up to 200 times by the presence of counter ions such as sodium. Our <span class="hlt">protein</span> interaction studies revealed that a millimolar <span class="hlt">concentration</span> of sodium diclofenac is able to elute glutathione S-transferase (GST), cellulose binding <span class="hlt">protein</span> (CBD), and maltose binding <span class="hlt">protein</span> (MBP) but not histidine-tagged or PDZ-tagged <span class="hlt">proteins</span> from their affinity resins. The elution efficiency of diclofenac is comparable with the eluting agents normally used at similar <span class="hlt">concentrations</span>. Native gel electrophoresis of sodium diclofenac-treated <span class="hlt">proteins</span> showed that the interaction is non-covalent and non-denaturing. These results suggest that sodium diclofenac, in addition to its pharmaceutical applications, can also be exploited as a lead for the development of new proteomics reagents.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1082755','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1082755"><span id="translatedtitle">Coat <span class="hlt">Protein</span> Activation of Alfalfa Mosaic Virus Replication Is <span class="hlt">Concentration</span> Dependent</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Guogas, Laura M.; Laforest, Siana M.; Gehrke, Lee</p> <p>2005-01-01</p> <p>Alfalfa mosaic virus (AMV) and ilarvirus RNAs are infectious only in the presence of the viral coat <span class="hlt">protein</span>; therefore, an understanding of coat <span class="hlt">protein</span>'s function is important for defining viral replication mechanisms. Based on in vitro replication experiments, the conformational switch model states that AMV coat <span class="hlt">protein</span> blocks minus-strand RNA synthesis (R. C. Olsthoorn, S. Mertens, F. T. Brederode, and J. F. Bol, EMBO J. 18:4856-4864, 1999), while another report states that coat <span class="hlt">protein</span> present in an inoculum is required to permit minus-strand synthesis (L. Neeleman and J. F. Bol, Virology 254:324-333, 1999). Here, we report on experiments that address these contrasting results with a goal of defining coat protein′s function in the earliest stages of AMV replication. To detect coat-<span class="hlt">protein</span>-activated AMV RNA replication, we designed and characterized a subgenomic luciferase reporter construct. We demonstrate that activation of viral RNA replication by coat <span class="hlt">protein</span> is <span class="hlt">concentration</span> dependent; that is, replication was strongly stimulated at low coat <span class="hlt">protein</span> <span class="hlt">concentrations</span> but decreased progressively at higher <span class="hlt">concentrations</span>. Genomic RNA3 mutations preventing coat <span class="hlt">protein</span> mRNA translation or disrupting coat <span class="hlt">protein</span>'s RNA binding domain diminished replication. The data indicate that RNA binding and an ongoing supply of coat <span class="hlt">protein</span> are required to initiate replication on progeny genomic RNA transcripts. The data do not support the conformational switch model's claim that coat <span class="hlt">protein</span> inhibits the initial stages of viral RNA replication. Replication activation may correlate with low local coat <span class="hlt">protein</span> <span class="hlt">concentrations</span> and low coat <span class="hlt">protein</span> occupancy on the multiple binding sites present in the 3′ untranslated regions of the viral RNAs. PMID:15827190</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27558718','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27558718"><span id="translatedtitle">Molecular Effects of <span class="hlt">Concentrated</span> Solutes on <span class="hlt">Protein</span> Hydration, Dynamics, and Electrostatics.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Abriata, Luciano A; Spiga, Enrico; Peraro, Matteo Dal</p> <p>2016-08-23</p> <p>Most studies of <span class="hlt">protein</span> structure and function are performed in dilute conditions, but <span class="hlt">proteins</span> typically experience high solute <span class="hlt">concentrations</span> in their physiological scenarios and biotechnological applications. High solute <span class="hlt">concentrations</span> have well-known effects on coarse <span class="hlt">protein</span> traits like stability, diffusion, and shape, but likely also perturb other traits through finer effects pertinent at the residue and atomic levels. Here, NMR and molecular dynamics investigations on ubiquitin disclose variable interactions with <span class="hlt">concentrated</span> solutes that lead to localized perturbations of the <span class="hlt">protein</span>'s surface, hydration, electrostatics, and dynamics, all dependent on solute size and chemical properties. Most strikingly, small polar uncharged molecules are sticky on the <span class="hlt">protein</span> surface, whereas charged small molecules are not, but the latter still perturb the internal <span class="hlt">protein</span> electrostatics as they diffuse nearby. Meanwhile, interactions with macromolecular crowders are favored mainly through hydrophobic, but not through polar, surface patches. All the tested small solutes strongly slow down water exchange at the <span class="hlt">protein</span> surface, whereas macromolecular crowders do not exert such strong perturbation. Finally, molecular dynamics simulations predict that unspecific interactions slow down microsecond- to millisecond-timescale <span class="hlt">protein</span> dynamics despite having only mild effects on pico- to nanosecond fluctuations as corroborated by NMR. We discuss our results in the light of recent advances in understanding <span class="hlt">proteins</span> inside living cells, focusing on the physical chemistry of quinary structure and cellular organization, and we reinforce the idea that <span class="hlt">proteins</span> should be studied in native-like media to achieve a faithful description of their function. PMID:27558718</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3064784','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3064784"><span id="translatedtitle"><span class="hlt">Concentration</span>-dependent exchange accelerates turnover of <span class="hlt">proteins</span> bound to double-stranded DNA</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Graham, John S.; Johnson, Reid C.; Marko, John F.</p> <p>2011-01-01</p> <p>The multistep kinetics through which DNA-binding <span class="hlt">proteins</span> bind their targets are heavily studied, but relatively little attention has been paid to <span class="hlt">proteins</span> leaving the double helix. Using single-DNA stretching and fluorescence detection, we find that sequence-neutral DNA-binding <span class="hlt">proteins</span> Fis, HU and NHP6A readily exchange with themselves and with each other. In experiments focused on the Escherichia coli nucleoid-associated <span class="hlt">protein</span> Fis, only a small fraction of <span class="hlt">protein</span> bound to DNA spontaneously dissociates into <span class="hlt">protein</span>-free solution. However, if Fis is present in solution, we find that a <span class="hlt">concentration</span>-dependent exchange reaction occurs which turns over the bound <span class="hlt">protein</span>, with a rate of kexch = 6 × 104 M−1s−1. The bacterial DNA-binding <span class="hlt">protein</span> HU and the yeast HMGB <span class="hlt">protein</span> NHP6A display the same phenomenon of <span class="hlt">protein</span> in solution accelerating dissociation of previously bound labeled <span class="hlt">proteins</span> as exchange occurs. Thus, solvated <span class="hlt">proteins</span> can play a key role in facilitating removal and renewal of <span class="hlt">proteins</span> bound to the double helix, an effect that likely plays a major role in promoting the turnover of <span class="hlt">proteins</span> bound to DNA in vivo and, therefore, in controlling the dynamics of gene regulation. PMID:21097894</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25494777','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25494777"><span id="translatedtitle">Intermolecular interactions in highly <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions upon compression and the role of the solvent.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Grobelny, S; Erlkamp, M; Möller, J; Tolan, M; Winter, R</p> <p>2014-12-14</p> <p>The influence of high hydrostatic pressure on the structure and <span class="hlt">protein-protein</span> interaction potential of highly <span class="hlt">concentrated</span> lysozyme solutions up to about 370 mg ml(-1) was studied and analyzed using small-angle X-ray scattering in combination with a liquid-state theoretical approach. In the <span class="hlt">concentration</span> region below 200 mg ml(-1), the interaction parameters of lysozyme solutions are affected by pressure in a nonlinear way, which is probably due to significant changes in the structural properties of bulk water, i.e., due to a solvent-mediated effect. Conversely, for higher <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions, where hydration layers below ∼4 water molecules are reached, the interaction potential turns rather insensitive to compression. The onset of transient (dynamic) clustering is envisaged in this <span class="hlt">concentration</span> range. Our results also show that pressure suppresses <span class="hlt">protein</span> nucleation, aggregation and finally crystallization in supersaturated condensed <span class="hlt">protein</span> solutions. These findings are of importance for controlling and fine-tuning <span class="hlt">protein</span> crystallization. Moreover, these results are also important for understanding the high stability of highly <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions (as they occur intracellularly) in organisms thriving under hydrostatic pressure conditions such as in the deep sea, where pressures up to the kbar-level are reached.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/25494777','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/25494777"><span id="translatedtitle">Intermolecular interactions in highly <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions upon compression and the role of the solvent.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Grobelny, S; Erlkamp, M; Möller, J; Tolan, M; Winter, R</p> <p>2014-12-14</p> <p>The influence of high hydrostatic pressure on the structure and <span class="hlt">protein-protein</span> interaction potential of highly <span class="hlt">concentrated</span> lysozyme solutions up to about 370 mg ml(-1) was studied and analyzed using small-angle X-ray scattering in combination with a liquid-state theoretical approach. In the <span class="hlt">concentration</span> region below 200 mg ml(-1), the interaction parameters of lysozyme solutions are affected by pressure in a nonlinear way, which is probably due to significant changes in the structural properties of bulk water, i.e., due to a solvent-mediated effect. Conversely, for higher <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions, where hydration layers below ∼4 water molecules are reached, the interaction potential turns rather insensitive to compression. The onset of transient (dynamic) clustering is envisaged in this <span class="hlt">concentration</span> range. Our results also show that pressure suppresses <span class="hlt">protein</span> nucleation, aggregation and finally crystallization in supersaturated condensed <span class="hlt">protein</span> solutions. These findings are of importance for controlling and fine-tuning <span class="hlt">protein</span> crystallization. Moreover, these results are also important for understanding the high stability of highly <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions (as they occur intracellularly) in organisms thriving under hydrostatic pressure conditions such as in the deep sea, where pressures up to the kbar-level are reached. PMID:25494777</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/11540604','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/11540604"><span id="translatedtitle">Early leaf harvest reduces yield but not <span class="hlt">protein</span> <span class="hlt">concentration</span> of cowpea seeds.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Nielsen, S S; Osuala, C I; Brandt, W E</p> <p>1994-06-01</p> <p>Five greenhouse-grown cowpea [Vigna unguiculata (L.) Walp] cultivars were tested in a generalized random complete-block design to determine the effect of early leaf harvest on dry weight and <span class="hlt">protein</span> <span class="hlt">concentration</span> of plant parts at maturity. The most recent, fully expanded leaves on each branch from one group of plants were harvested at 5 and 7 weeks after planting. On the other groups of plants, no early leaf harvest was performed. Dry weight and <span class="hlt">protein</span> <span class="hlt">concentration</span> (dry weight basis) were determined for leaves, stems, and seeds at maturity and for leaves harvested early. Weight and <span class="hlt">protein</span> <span class="hlt">concentration</span> of seeds, leaves, and stems differed significantly between cultivars; <span class="hlt">protein</span> <span class="hlt">concentration</span> of leaves harvested at 5 or 7 weeks did not. Dry weight of leaves harvested at 5 vs. 7 weeks did not differ significantly, but leaf <span class="hlt">protein</span> <span class="hlt">concentration</span> was significantly higher at 5 weeks compared to 7 weeks. Across all cultivars, early leaf harvest had no significant effect on leaf or stem weight per plant at maturity. However, there was a significant decrease in seed weight when leaves were harvested early. Results suggest that even limited leaf harvest at 5 and 7 weeks has detrimental effects on yield, but not on <span class="hlt">protein</span> <span class="hlt">concentration</span>, of cowpea seeds harvested at maturity.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/23586876','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/23586876"><span id="translatedtitle"><span class="hlt">Absolute</span> biological needs.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>McLeod, Stephen</p> <p>2014-07-01</p> <p><span class="hlt">Absolute</span> needs (as against instrumental needs) are independent of the ends, goals and purposes of personal agents. Against the view that the only needs are instrumental needs, David Wiggins and Garrett Thomson have defended <span class="hlt">absolute</span> needs on the grounds that the verb 'need' has instrumental and <span class="hlt">absolute</span> senses. While remaining neutral about it, this article does not adopt that approach. Instead, it suggests that there are <span class="hlt">absolute</span> biological needs. The <span class="hlt">absolute</span> nature of these needs is defended by appeal to: their objectivity (as against mind-dependence); the universality of the phenomenon of needing across the plant and animal kingdoms; the impossibility that biological needs depend wholly upon the exercise of the abilities characteristic of personal agency; the contention that the possession of biological needs is prior to the possession of the abilities characteristic of personal agency. Finally, three philosophical usages of 'normative' are distinguished. On two of these, to describe a phenomenon or claim as 'normative' is to describe it as value-dependent. A description of a phenomenon or claim as 'normative' in the third sense does not entail such value-dependency, though it leaves open the possibility that value depends upon the phenomenon or upon the truth of the claim. It is argued that while survival needs (or claims about them) may well be normative in this third sense, they are normative in neither of the first two. Thus, the idea of <span class="hlt">absolute</span> need is not inherently normative in either of the first two senses. PMID:23586876</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/23586876','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/23586876"><span id="translatedtitle"><span class="hlt">Absolute</span> biological needs.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>McLeod, Stephen</p> <p>2014-07-01</p> <p><span class="hlt">Absolute</span> needs (as against instrumental needs) are independent of the ends, goals and purposes of personal agents. Against the view that the only needs are instrumental needs, David Wiggins and Garrett Thomson have defended <span class="hlt">absolute</span> needs on the grounds that the verb 'need' has instrumental and <span class="hlt">absolute</span> senses. While remaining neutral about it, this article does not adopt that approach. Instead, it suggests that there are <span class="hlt">absolute</span> biological needs. The <span class="hlt">absolute</span> nature of these needs is defended by appeal to: their objectivity (as against mind-dependence); the universality of the phenomenon of needing across the plant and animal kingdoms; the impossibility that biological needs depend wholly upon the exercise of the abilities characteristic of personal agency; the contention that the possession of biological needs is prior to the possession of the abilities characteristic of personal agency. Finally, three philosophical usages of 'normative' are distinguished. On two of these, to describe a phenomenon or claim as 'normative' is to describe it as value-dependent. A description of a phenomenon or claim as 'normative' in the third sense does not entail such value-dependency, though it leaves open the possibility that value depends upon the phenomenon or upon the truth of the claim. It is argued that while survival needs (or claims about them) may well be normative in this third sense, they are normative in neither of the first two. Thus, the idea of <span class="hlt">absolute</span> need is not inherently normative in either of the first two senses.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=295952','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=295952"><span id="translatedtitle">Optical-mechanical system for on-combine segregation of wheat by grain <span class="hlt">protein</span> <span class="hlt">concentration</span></span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>Grain segregation by grain <span class="hlt">protein</span> <span class="hlt">concentration</span> (GPC) may help growers maximize revenues in markets that offer <span class="hlt">protein</span> premiums. Our objective was to develop an on-combine system for automatically segregating wheat (Triticum aestivum L.) by GPC during harvest. A multispectral optical sensor scans...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/24426032','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/24426032"><span id="translatedtitle">Chemical composition, functional and pasting properties of cassava starch and soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> blends.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Chinma, Chiemela Enyinnaya; Ariahu, Charles Chukwuma; Abu, Joseph Oneh</p> <p>2013-12-01</p> <p>The chemical, functional and pasting properties of cassava starch and soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> blends intended for biofilm processing were studied. Cassava starch and soy <span class="hlt">protein</span> <span class="hlt">concentrates</span> were prepared and mixed at different proportions (100: 0%; 90 : 10%; 80 : 20%; 70 : 30%; 60;40% and 50: 50%). Addition of varying levels of soy <span class="hlt">protein</span> <span class="hlt">concentrates</span> to cassava starch led to increases in moisture (from 7.10 to 9.17%), <span class="hlt">protein</span> ( from 0.32 to 79.03%), ash (from 0.45 to 2.67%) and fat (from 0.17 to 0.98%) contents while crude fiber, carbohydrate and amylose contents decreased from ( 1.19 to 0.38%, 90.77 to 57.01% and 29.45 to 23.04%) respectively . Water absorption capacity and swelling power of cassava starch were improved as a result of soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> addition while syneresis and solubility value of composite blends were lower than 100% cassava starch. In general, cassava-soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> blends formed firmer gels than cassava starch alone. There were significant (p ≤ 0.05) increases in peak viscosity (from 160.12 to 268.32RVU), final viscosity (from 140.41 to 211.08RVU) and pasting temperature (from 71.00 to 72.32 °C ) of cassava starch due to addition of soy <span class="hlt">protein</span> <span class="hlt">concentrate</span>. These results suggest that the addition of soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> to cassava starch affected the studied functional properties of cassava starch as evidenced by changes such as reduced syneresis, and solubility that are desirable when considering this biopolymer as an edible biofilm.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/24426032','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/24426032"><span id="translatedtitle">Chemical composition, functional and pasting properties of cassava starch and soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> blends.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Chinma, Chiemela Enyinnaya; Ariahu, Charles Chukwuma; Abu, Joseph Oneh</p> <p>2013-12-01</p> <p>The chemical, functional and pasting properties of cassava starch and soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> blends intended for biofilm processing were studied. Cassava starch and soy <span class="hlt">protein</span> <span class="hlt">concentrates</span> were prepared and mixed at different proportions (100: 0%; 90 : 10%; 80 : 20%; 70 : 30%; 60;40% and 50: 50%). Addition of varying levels of soy <span class="hlt">protein</span> <span class="hlt">concentrates</span> to cassava starch led to increases in moisture (from 7.10 to 9.17%), <span class="hlt">protein</span> ( from 0.32 to 79.03%), ash (from 0.45 to 2.67%) and fat (from 0.17 to 0.98%) contents while crude fiber, carbohydrate and amylose contents decreased from ( 1.19 to 0.38%, 90.77 to 57.01% and 29.45 to 23.04%) respectively . Water absorption capacity and swelling power of cassava starch were improved as a result of soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> addition while syneresis and solubility value of composite blends were lower than 100% cassava starch. In general, cassava-soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> blends formed firmer gels than cassava starch alone. There were significant (p ≤ 0.05) increases in peak viscosity (from 160.12 to 268.32RVU), final viscosity (from 140.41 to 211.08RVU) and pasting temperature (from 71.00 to 72.32 °C ) of cassava starch due to addition of soy <span class="hlt">protein</span> <span class="hlt">concentrate</span>. These results suggest that the addition of soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> to cassava starch affected the studied functional properties of cassava starch as evidenced by changes such as reduced syneresis, and solubility that are desirable when considering this biopolymer as an edible biofilm. PMID:24426032</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26142868','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26142868"><span id="translatedtitle">The composition and functional properties of whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> produced from buttermilk are comparable with those of whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> produced from skimmed milk.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Svanborg, Sigrid; Johansen, Anne-Grethe; Abrahamsen, Roger K; Skeie, Siv B</p> <p>2015-09-01</p> <p>The demand for whey <span class="hlt">protein</span> is increasing in the food industry. Traditionally, whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> (WPC) and isolates are produced from cheese whey. At present, microfiltration (MF) enables the utilization of whey from skim milk (SM) through milk <span class="hlt">protein</span> fractionation. This study demonstrates that buttermilk (BM) can be a potential source for the production of a WPC with a comparable composition and functional properties to a WPC obtained by MF of SM. Through the production of WPC powder and a casein- and phospholipid (PL)-rich fraction by the MF of BM, sweet BM may be used in a more optimal and economical way. Sweet cream BM from industrial churning was skimmed before MF with 0.2-µm ceramic membranes at 55 to 58°C. The fractionations of BM and SM were performed under the same conditions using the same process, and the whey <span class="hlt">protein</span> fractions from BM and SM were <span class="hlt">concentrated</span> by ultrafiltration and diafiltration. The ultrafiltration and diafiltration was performed at 50°C using pasteurized tap water and a membrane with a 20-kDa cut-off to retain as little lactose as possible in the final WPC powders. The ultrafiltrates were subsequently spray dried, and their functional properties and chemical compositions were compared. The amounts of whey <span class="hlt">protein</span> and PL in the WPC powder from BM (BMWPC) were comparable to the amounts found in the WPC from SM (SMWPC); however, the composition of the PL classes differed. The BMWPC contained less total <span class="hlt">protein</span>, casein, and lactose compared with SMWPC, as well as higher contents of fat and citric acid. No difference in <span class="hlt">protein</span> solubility was observed at pH values of 4.6 and 7.0, and the overrun was the same for BMWPC and SMWPC; however, the BMWPC made less stable foam than SMWPC.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2015csw..confa1020N','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2015csw..confa1020N"><span id="translatedtitle">Molecular Dynamics Simulations to Clarify the <span class="hlt">Concentration</span> Dependency of <span class="hlt">Protein</span> Aggregation</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Nishikawa, Naohiro; Sakae, Yoshitake; Okamoto, Yuko</p> <p></p> <p>We examined the <span class="hlt">concentration</span> dependency of amyloid <span class="hlt">protein</span> aggregation by using several molecular dynamics simulations, which were performed with different <span class="hlt">concentrations</span> for each system. For these simulations, we used a fragment of amyloid-β, which is believed to be the cause of Alzheimer's disease, as our simulation system. We found that high <span class="hlt">concentration</span> of amyloid peptides promotes the formation of β-structures which is the origin of amyloid fibrils.</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_6");'>6</a></li> <li><a href="#" onclick='return showDiv("page_7");'>7</a></li> <li class="active"><span>8</span></li> <li><a href="#" onclick='return showDiv("page_9");'>9</a></li> <li><a href="#" onclick='return showDiv("page_10");'>10</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_8 --> <div id="page_9" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_7");'>7</a></li> <li><a href="#" onclick='return showDiv("page_8");'>8</a></li> <li class="active"><span>9</span></li> <li><a href="#" onclick='return showDiv("page_10");'>10</a></li> <li><a href="#" onclick='return showDiv("page_11");'>11</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="161"> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25720159','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25720159"><span id="translatedtitle">[Short gel method for pretreatment of <span class="hlt">protein</span> samples with high <span class="hlt">concentration</span> of detergent].</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Ma, Shouzhi; Zhang, Tao; Zhai, Linhui; Sun, Yulin; Xu, Ping; Zhao, Xiaohang</p> <p>2014-09-01</p> <p>In proteomic research, to improve <span class="hlt">protein</span> solubility of membrane <span class="hlt">proteins</span> and nuclear <span class="hlt">proteins</span>, buffers containing high <span class="hlt">concentration</span> of detergent, such as 4% SDS, were widely used. However, high <span class="hlt">concentration</span> of detergent might severely interfere with the downstream proteomic analysis, including <span class="hlt">protein</span> quantitation and trypsin digestion. To improve the proteomic compatibility of buffers with high <span class="hlt">concentration</span> of detergent, we used short gel method to pretreat buffers containing detergent. <span class="hlt">Protein</span> samples were first separated by a short (2-2.5 mm) SDS-PAGE electrophoresis, and <span class="hlt">proteins</span> were quantitated by comparing with bovine serum albumin standards via optical density analysis. The gel was then cut and peptides were recovered using in-gel digestion. The quantitative linearity range of this method was 1 to 8 μg. The quantitation was accurate and reproducible. After short gel analysis, recovered peptides generated high mass spectrometry signals. In conclusion, short gel method eliminated the interference of high <span class="hlt">concentration</span> detergent in the proteomics analysis, and it was suitable for <span class="hlt">protein</span> samples' pretreatment, and was worth to apply in proteomic research.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25829594','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25829594"><span id="translatedtitle">Influence of watermelon seed <span class="hlt">protein</span> <span class="hlt">concentrates</span> on dough handling, textural and sensory properties of cookies.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Wani, Ali Abas; Sogi, D S; Singh, Preeti; Khatkar, B S</p> <p>2015-04-01</p> <p>Fruit processing wastes contain numerous by products of potential use in food & allied industry. Watermelon seeds represent a major by-product of the processing waste and contain high amount of nutritional <span class="hlt">proteins</span>. <span class="hlt">Protein</span> rich cereal based products are in demand due to their health promoting benefits. With this aim, wheat flour was fortified with watermelon seed <span class="hlt">protein</span> <span class="hlt">concentrates</span> (2.5 %, 5 %, 7.5 % and 10 % levels) to prepare cookies with desirable physical, nutritional, and textural and sensory properties. Substitution levels of 5 % and 10 % significantly (p ≤ 0.05) increased the dough stability and mixing tolerance index, however pasting properties and dough extensibility decreased considerably above 5 % substitution levels. Cookie fracture force (kg) increased significantly (p ≤ 0.05) above 5 % fortification levels. Cookie spread factor (W/T) increased from 2.5 % to 7.5 % fortification levels, further increase showed negative impact. Sensory scores of the cookies showed that <span class="hlt">protein</span> <span class="hlt">concentrate</span> may be added up to 7.5 % fortification levels. This study revealed that watermelon <span class="hlt">protein</span> <span class="hlt">concentrates</span> can be fortified with <span class="hlt">protein</span> <span class="hlt">concentrates</span> upto 5-7.5 % levels in cookies to improve their <span class="hlt">protein</span> quality.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2014APS..MARJ16001S','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2014APS..MARJ16001S"><span id="translatedtitle">Arrest scenarios in <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions - from hard sphere glasses to arrested spinodal decomposition</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Stradner, Anna; Bucciarelli, Saskia; Casal, Lucia; Foffi, Giuseppe; Thurston, George; Farago, Bela; Schurtenberger, Peter</p> <p>2014-03-01</p> <p>The occurrence of an arrest transition in <span class="hlt">concentrated</span> colloid suspensions and its dependence on the interaction potential is a hot topic in soft matter. Such arrest transitions can also occur in <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions, as they exist e.g. in biological cells or are increasingly used in pharmaceutical formulations. Here we demonstrate the applicability of concepts from colloid science to understand the dynamics of <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions. In this presentation we report a combination of 3D light scattering, small-angle X-ray scattering and neutron spin echo measurements to study the structural properties as well as the collective and self diffusion of <span class="hlt">proteins</span> in highly <span class="hlt">concentrated</span> solutions on the relevant length and time scales. We demonstrate that various arrest scenarios indeed exist for different globular <span class="hlt">proteins</span>. The <span class="hlt">proteins</span> chosen are different bovine lens crystallins. We report examples of hard and attractive glass transitions and arrested spinodal decomposition directly linked to the effective pair potentials determined in static scattering experiments for the different <span class="hlt">proteins</span>. We discuss these different arrest scenarios in view of possible applications of dense <span class="hlt">protein</span> solutions as well as in view of their possible relevance for living systems.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=2011JPhCS.276a2144S&link_type=ABSTRACT','NASAADS'); return false;" href="http://adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=2011JPhCS.276a2144S&link_type=ABSTRACT"><span id="translatedtitle">A Rapid Method for Determining the <span class="hlt">Concentration</span> of Recombinant <span class="hlt">Protein</span> Secreted from Pichia pastoris</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Sun, L. W.; Zhao, Y.; Niu, L. P.; Jiang, R.; Song, Y.; Feng, H.; feng, K.; Qi, C.</p> <p>2011-02-01</p> <p>Pichia secretive expression system is one of powerful eukaryotic expression systems in genetic engineering, which is especially suitable for industrial utilization. Because of the low <span class="hlt">concentration</span> of the target <span class="hlt">protein</span> in initial experiment, the methods and conditions for expression of the target <span class="hlt">protein</span> should be optimized according to the <span class="hlt">protein</span> yield repetitively. It is necessary to set up a rapid, simple and convenient analysis method for <span class="hlt">protein</span> expression levels instead of the generally used method such as ultrafiltration, purification, dialysis, lyophilization and so on. In this paper, acetone precipitation method was chosen to <span class="hlt">concentrate</span> the recombinant <span class="hlt">protein</span> firstly after comparing with four different <span class="hlt">protein</span> precipitation methods systematically, and then the <span class="hlt">protein</span> was analyzed by SDS-Polyacrylamide Gel Electrophoresis. The recombinant <span class="hlt">protein</span> was determined with the feature of <span class="hlt">protein</span> band by the Automated Image Capture and 1-D Analysis Software directly. With this method, the optimized expression conditions of basic fibroblast growth factor secreted from pichia were obtained, which is as the same as using traditional methods. Hence, a convenient tool to determine the optimized conditions for the expression of recombinant <span class="hlt">proteins</span> in Pichia was established.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/9382685','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/9382685"><span id="translatedtitle">[Comparative study of the composition and nutritional value of the seeds and <span class="hlt">protein</span> <span class="hlt">concentrations</span> in legumes].</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Cantoral, R; Fernández-Quintela, A; Martínez, J A; Macarulla, M T</p> <p>1995-09-01</p> <p>The nutritional properties of three legumes: pea (Pisum sativum), faba bean (Vicia faba) and soya (Glycine max) have been characterized. From these seeds, <span class="hlt">protein</span> <span class="hlt">concentrates</span> were elaborated by wet processing and two different procedures of drying were followed (freeze-drying and alcohol washing). The composition and content of several antinutritional factors (phytates, tannins, trypsin inhibitors and lectins) were assessed in all of them. Also some functional properties regarding their potential use in food technology were evaluated, such as <span class="hlt">protein</span> solubility at different pH, as well as water and oil absorption capacities. All the obtained <span class="hlt">concentrates</span> showed high <span class="hlt">protein</span> contents, nevertheless <span class="hlt">protein</span> extraction efficiency was smaller in alcohol-washed <span class="hlt">concentrates</span> than in the lyophilized ones. In the other hand, the <span class="hlt">concentrates</span> obtained from pea and faba bean showed higher yields than those obtained from soya. The content of antinutritional factors were markedly reduced after the <span class="hlt">concentration</span> process. Furthermore, the functional properties of pea and faba bean <span class="hlt">protein</span> <span class="hlt">concentrates</span> point out their suitability for food preparation as previously reported for soya. PMID:9382685</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3391308','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3391308"><span id="translatedtitle">Microfluidic three-dimensional hydrodynamic flow focusing for the rapid <span class="hlt">protein</span> <span class="hlt">concentration</span> analysis</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Hong, Sungmin; Tsou, Pei-Hsiang; Chou, Chao-Kai; Yamaguchi, Hirohito; Su, Chin B.; Hung, Mien-Chie; Kameoka, Jun</p> <p>2012-01-01</p> <p>A simple microfluidic 3D hydrodynamic flow focusing device has been developed and demonstrated quantitative determinations of quantum dot 525 with antibody (QD525-antibody) and hemagglutinin epitope tagged MAX (HA-MAX) <span class="hlt">protein</span> <span class="hlt">concentrations</span>. This device had a step depth cross junction structure at a hydrodynamic flow focusing point at which the analyte stream was flowed into a main detection channel and pinched not only horizontally but also vertically by two sheath streams. As a result, a triangular cross-sectional flow profile of the analyte stream was formed and the laser was focused on the top of the triangular shaped analyte stream. Since the detection volume was smaller than the radius of laser spot, a photon burst histogram showed Gaussian distribution, which was necessary for the quantitative analysis of <span class="hlt">protein</span> <span class="hlt">concentration</span>. By using this approach, a linear <span class="hlt">concentration</span> curve of QD525-antibody down to 10 pM was demonstrated. In addition, the <span class="hlt">concentration</span> of HA-MAX <span class="hlt">protein</span> in HEK293 cell lysate was determined as 0.283 ± 0.015 nM. This approach requires for only 1 min determining <span class="hlt">protein</span> <span class="hlt">concentration</span>. As the best of our knowledge, this is the first time to determinate <span class="hlt">protein</span> <span class="hlt">concentration</span> by using single molecule detection techniques. PMID:23785388</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2012APS..MARA40003T','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2012APS..MARA40003T"><span id="translatedtitle"><span class="hlt">Concentrated</span> dispersions of equilibrium <span class="hlt">protein</span> nanoclusters that reversibly dissociate into active monomers</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Truskett, Thomas M.; Johnston, Keith; Maynard, Jennifer; Borwankar, Ameya; Miller, Maria; Wilson, Brian; Dinin, Aileen; Khan, Tarik; Kaczorowski, Kevin</p> <p>2012-02-01</p> <p>Stabilizing <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions is of wide interest in drug delivery. However, a major challenge is how to reliably formulate <span class="hlt">concentrated</span>, low viscosity (i.e., syringeable) solutions of biologically active <span class="hlt">proteins</span>. Unfortunately, <span class="hlt">proteins</span> typically undergo irreversible aggregation at intermediate <span class="hlt">concentrations</span> of 100-200 mg/ml. In this talk, I describe how they can effectively avoid these intermediate <span class="hlt">concentrations</span> by reversibly assembling into nanoclusters. Nanocluster assembly is achieved by balancing short-ranged, cosolute-induced attractions with weak, longer-ranger electrostatic repulsions near the isoelectric point. Theory predicts that native <span class="hlt">proteins</span> are stabilized by a self-crowding mechanism within the <span class="hlt">concentrated</span> environment of the nanoclusters, while weak cluster-cluster interactions can result in colloidally-stable dispersions with moderate viscosities. I present experimental results where this strategy is used to create <span class="hlt">concentrated</span> antibody dispersions (up to 260 mg/ml) comprising nanoclusters of <span class="hlt">proteins</span> [monoclonal antibody 1B7, polyclonal sheep Immunoglobin G and bovine serum albumin], which upon dilution in vitro or administration in vivo, are conformationally stable and retain activity.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/19643046','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/19643046"><span id="translatedtitle">Effects of <span class="hlt">protein</span> <span class="hlt">concentration</span> and detergent on endotoxin reduction by ultrafiltration.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Jang, Hyun; Kim, Hyo-Seung; Moon, Seung-Cheol; Lee, Young-Rae; Yu, Kang-Yeoul; Lee, Byeong-Kil; Youn, Hyun Zo; Jeong, Young-Ju; Kim, Byeong-Soo; Lee, Sung-Ho; Kim, Jong-Suk</p> <p>2009-07-31</p> <p>Lipopolysaccharide (LPS), found in the outer membrane of Gram negative bacteria, only exerts its toxic effects when in free form. LPS has three major parts, lipid A, the toxic component, along with a core polysaccharide and O-specific polysaccharide. LPS monomers are known to have molecular masses between 10 to 30 kDa. Under physiological conditions, LPS exists in equilibrium between monomer and vesicle forms. LPS removal by 100 kDa ultrafiltration was more efficient (99.6% of LPS removed) with a low <span class="hlt">concentration</span> of <span class="hlt">protein</span> (2.0 mg/ml) compared to a high <span class="hlt">concentration</span> (20.1 mg/ml). In the presence of different detergents (0.5% Tween 20, 1.0% taurodeoxycholate and 1.0% Triton X-100), LPS removal was more efficient at low <span class="hlt">protein</span> <span class="hlt">concentrations</span> (2.0 mg/ml) compared to high <span class="hlt">protein</span> <span class="hlt">concentrations</span> (20.1 mg/ml).</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26241463','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26241463"><span id="translatedtitle">Relationship between oxygen <span class="hlt">concentration</span>, shear force and <span class="hlt">protein</span> oxidation in modified atmosphere packaged pork.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Bao, Yulong; Ertbjerg, Per</p> <p>2015-12-01</p> <p>Pork loins were stored at 5°C for 14 days to investigate the effect of oxygen <span class="hlt">concentration</span> in modified atmosphere packaging (MAP) on shear force and oxidation of lipids and <span class="hlt">proteins</span>. The modified atmosphere contained 0 to 80% O2, 20% CO2, and balanced with N2. The results showed that shear force and thiobarbituric acid-reactive substances (TBARS) values increased with increasing oxygen <span class="hlt">concentration</span>. <span class="hlt">Protein</span> oxidation when measured as loss of free thiol groups, was greater in meat packaged under oxygen (20-80%). Myosin heavy chain (MHC) cross-linking, another marker of <span class="hlt">protein</span> oxidation, was greater in MAP with 80% oxygen than 0% and 20% oxygen. Desmin degradation was not affected by the presence of oxygen, suggesting that the mechanism of oxygen-induced toughening of meat is through <span class="hlt">protein</span> oxidation leading to cross-linking of structural <span class="hlt">proteins</span> rather than through inactivation of proteolytic enzymes leading to reduced proteolysis.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26241463','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26241463"><span id="translatedtitle">Relationship between oxygen <span class="hlt">concentration</span>, shear force and <span class="hlt">protein</span> oxidation in modified atmosphere packaged pork.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Bao, Yulong; Ertbjerg, Per</p> <p>2015-12-01</p> <p>Pork loins were stored at 5°C for 14 days to investigate the effect of oxygen <span class="hlt">concentration</span> in modified atmosphere packaging (MAP) on shear force and oxidation of lipids and <span class="hlt">proteins</span>. The modified atmosphere contained 0 to 80% O2, 20% CO2, and balanced with N2. The results showed that shear force and thiobarbituric acid-reactive substances (TBARS) values increased with increasing oxygen <span class="hlt">concentration</span>. <span class="hlt">Protein</span> oxidation when measured as loss of free thiol groups, was greater in meat packaged under oxygen (20-80%). Myosin heavy chain (MHC) cross-linking, another marker of <span class="hlt">protein</span> oxidation, was greater in MAP with 80% oxygen than 0% and 20% oxygen. Desmin degradation was not affected by the presence of oxygen, suggesting that the mechanism of oxygen-induced toughening of meat is through <span class="hlt">protein</span> oxidation leading to cross-linking of structural <span class="hlt">proteins</span> rather than through inactivation of proteolytic enzymes leading to reduced proteolysis. PMID:26241463</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26284891','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26284891"><span id="translatedtitle">Aggregate structure, morphology and the effect of aggregation mechanisms on viscosity at elevated <span class="hlt">protein</span> <span class="hlt">concentrations</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Barnett, Gregory V; Qi, Wei; Amin, Samiul; Neil Lewis, E; Roberts, Christopher J</p> <p>2015-12-01</p> <p>Non-native aggregation is a common issue in a number of degenerative diseases and during manufacturing of <span class="hlt">protein</span>-based therapeutics. There is a growing interest to monitor <span class="hlt">protein</span> stability at intermediate to high <span class="hlt">protein</span> <span class="hlt">concentrations</span>, which are required for therapeutic dosing of subcutaneous injections. An understanding of the impact of <span class="hlt">protein</span> structural changes and interactions on the <span class="hlt">protein</span> aggregation mechanisms and resulting aggregate size and morphology may lead to improved strategies to reduce aggregation and solution viscosity. This report investigates non-native aggregation of a model <span class="hlt">protein</span>, α-chymotrypsinogen, under accelerated conditions at elevated <span class="hlt">protein</span> <span class="hlt">concentrations</span>. Far-UV circular dichroism and Raman scattering show structural changes during aggregation. Size exclusion chromatography and laser light scattering are used to monitor the progression of aggregate growth and monomer loss. Monomer loss is concomitant with increased β-sheet structures as monomers are added to aggregates, which illustrate a transition from a native monomeric state to an aggregate state. Aggregates grow predominantly through monomer-addition, resulting in a semi-flexible polymer morphology. Analysis of aggregation growth kinetics shows that pH strongly affects the characteristic timescales for nucleation (τn) and growth (τg), while the initial <span class="hlt">protein</span> <span class="hlt">concentration</span> has only minor effects on τn or τg. Low-shear viscosity measurements follow a common scaling relationship between average aggregate molecular weight (Mw(agg)) and <span class="hlt">concentration</span> (σ), which is consistent with semi-dilute polymer-solution theory. The results establish a link between aggregate growth mechanisms, which couple Mw(agg) and σ, to increases in solution viscosity even at these intermediate <span class="hlt">protein</span> <span class="hlt">concentrations</span> (less than 3w/v %).</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2016NatSR...625827G','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2016NatSR...625827G"><span id="translatedtitle">Photonic reagents for <span class="hlt">concentration</span> measurement of flu-orescent <span class="hlt">proteins</span> with overlapping spectra</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Goun, Alexei; Bondar, Denys I.; Er, Ali O.; Quine, Zachary; Rabitz, Herschel A.</p> <p>2016-05-01</p> <p>By exploiting photonic reagents (i.e., coherent control by shaped laser pulses), we employ Optimal Dynamic Discrimination (ODD) as a novel means for quantitatively characterizing mixtures of fluorescent <span class="hlt">proteins</span> with a large spectral overlap. To illustrate ODD, we simultaneously measured <span class="hlt">concentrations</span> of in vitro mixtures of Enhanced Blue Fluorescent <span class="hlt">Protein</span> (EBFP) and Enhanced Cyan Fluorescent <span class="hlt">Protein</span> (ECFP). Building on this foundational study, the ultimate goal is to exploit the capabilities of ODD for parallel monitoring of genetic and <span class="hlt">protein</span> circuits by suppressing the spectral cross-talk among multiple fluorescent reporters.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4867436','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4867436"><span id="translatedtitle">Photonic reagents for <span class="hlt">concentration</span> measurement of flu-orescent <span class="hlt">proteins</span> with overlapping spectra</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Goun, Alexei; Bondar, Denys I.; Er, Ali O.; Quine, Zachary; Rabitz, Herschel A.</p> <p>2016-01-01</p> <p>By exploiting photonic reagents (i.e., coherent control by shaped laser pulses), we employ Optimal Dynamic Discrimination (ODD) as a novel means for quantitatively characterizing mixtures of fluorescent <span class="hlt">proteins</span> with a large spectral overlap. To illustrate ODD, we simultaneously measured <span class="hlt">concentrations</span> of in vitro mixtures of Enhanced Blue Fluorescent <span class="hlt">Protein</span> (EBFP) and Enhanced Cyan Fluorescent <span class="hlt">Protein</span> (ECFP). Building on this foundational study, the ultimate goal is to exploit the capabilities of ODD for parallel monitoring of genetic and <span class="hlt">protein</span> circuits by suppressing the spectral cross-talk among multiple fluorescent reporters. PMID:27181496</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/2930407','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/2930407"><span id="translatedtitle">Determination of chicken and turkey plasma and serum <span class="hlt">protein</span> <span class="hlt">concentrations</span> by refractometry and the biuret method.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Andreasen, C B; Latimer, K S; Kircher, I M; Brown, J</p> <p>1989-01-01</p> <p>Plasma and serum <span class="hlt">protein</span> <span class="hlt">concentrations</span> were determined in chickens and turkeys by refractometry (with human and veterinary refractometers) and by the biuret method. Chicken and turkey serum <span class="hlt">protein</span> values were significantly lower than respective plasma <span class="hlt">protein</span> values according to both methods. Refractometer readings for both plasma and serum correlated closely with the results of the biuret test (r2 = 0.72 to 0.97). These findings indicate that plasma and serum <span class="hlt">protein</span> values may be determined accurately in chickens and turkeys with a handheld refractometer.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/biblio/1231575-absolute-path-command','SCIGOV-ESTSC'); return false;" href="http://www.osti.gov/scitech/biblio/1231575-absolute-path-command"><span id="translatedtitle">The <span class="hlt">absolute</span> path command</span></a></p> <p><a target="_blank" href=""></a></p> <p></p> <p>2012-05-11</p> <p>The ap command traveres all symlinks in a given file, directory, or executable name to identify the final <span class="hlt">absolute</span> path. It can print just the final path, each intermediate link along with the symlink chan, and the permissions and ownership of each directory component in the final path. It has functionality similar to "which", except that it shows the final path instead of the first path. It is also similar to "pwd", but it canmore » provide the <span class="hlt">absolute</span> path to a relative directory from the current working directory.« less</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/biblio/1231575','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/biblio/1231575"><span id="translatedtitle">The <span class="hlt">absolute</span> path command</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>Moody, A.</p> <p>2012-05-11</p> <p>The ap command traveres all symlinks in a given file, directory, or executable name to identify the final <span class="hlt">absolute</span> path. It can print just the final path, each intermediate link along with the symlink chan, and the permissions and ownership of each directory component in the final path. It has functionality similar to "which", except that it shows the final path instead of the first path. It is also similar to "pwd", but it can provide the <span class="hlt">absolute</span> path to a relative directory from the current working directory.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/10822058','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/10822058"><span id="translatedtitle">Activation of G <span class="hlt">protein</span> by opioid receptors: role of receptor number and G-<span class="hlt">protein</span> <span class="hlt">concentration</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Remmers, A E; Clark, M J; Alt, A; Medzihradsky, F; Woods, J H; Traynor, J R</p> <p>2000-05-19</p> <p>The collision-coupling model for receptor-G-<span class="hlt">protein</span> interaction predicts that the rate of G-<span class="hlt">protein</span> activation is dependent on receptor density, but not G-<span class="hlt">protein</span> levels. C6 cells expressing mu- or delta-opioid receptors, or SH-SY5Y cells, were treated with beta-funaltrexamine (mu) or naltrindole-5'-isothiocyanate (delta) to decrease receptor number. The time course of full or partial agonist-stimulated ¿35SGTPgammaS binding did not vary in C6 cell membranes containing <1-25 pmol/mg mu-opioid receptor, or 1. 4-4.3 pmol/mg delta-opioid receptor, or in SHSY5Y cells containing 0. 16-0.39 pmol/mg receptor. The association of ¿35SGTPgammaS binding was faster in membranes from C6mu cells than from C6delta cells. A 10-fold reduction in functional G-<span class="hlt">protein</span>, following pertussis toxin treatment, lowered the maximal level of ¿35SGTPgammaS binding but not the association rate. These data indicate a compartmentalization of opioid receptors and G <span class="hlt">protein</span> at the cell membrane. PMID:10822058</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27439774','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27439774"><span id="translatedtitle">Enhanced <span class="hlt">protein</span> internalization and efficient endosomal escape using polyampholyte-modified liposomes and freeze <span class="hlt">concentration</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Ahmed, Sana; Fujita, Satoshi; Matsumura, Kazuaki</p> <p>2016-09-21</p> <p>Here we show a new strategy for efficient freeze <span class="hlt">concentration</span>-mediated cytoplasmic delivery of <span class="hlt">proteins</span>, obtained via the endosomal escape property of polyampholyte-modified liposomes. The freeze <span class="hlt">concentration</span> method successfully induces the efficient internalization of <span class="hlt">proteins</span> simply by freezing cells with <span class="hlt">protein</span> and nanocarrier complexes. However, the mechanism of <span class="hlt">protein</span> internalization remains unclear. Here, we designed a novel <span class="hlt">protein</span> delivery carrier by modifying liposomes through incorporating hydrophobic polyampholytes therein. These complexes were characterized for particle size, encapsulation efficiency, and cytotoxicity. Flow cytometry and microscopic analysis showed that the adsorption and internalization of <span class="hlt">protein</span>-loaded polyampholyte-modified liposomes after freezing were enhanced compared with that observed in unfrozen complexes. Inhibition studies demonstrated that the internalization mechanism differs between unmodified and polyampholyte-modified liposomes. Furthermore, polyampholyte-modified liposomes exhibited high efficacy in facilitating endosomal escape to enhance <span class="hlt">protein</span> delivery to the cytoplasm with low toxicity. These results strongly suggest that the freeze <span class="hlt">concentration</span>-based strategy could be widely utilised for efficient cargo delivery into the cytoplasm in vitro not only in cancer treatment but also for gene therapy as well. PMID:27439774</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26004574','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26004574"><span id="translatedtitle">Impact of confinement on <span class="hlt">proteins</span> <span class="hlt">concentrated</span> in lithocholic acid based organic nanotubes.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Lu, Qin; Kim, Youngchan; Bassim, Nabil; Collins, Greg E</p> <p>2015-09-15</p> <p>Organic nanotubes form in aqueous solution near physiological pH by self-assembly of lithocholic acid (LCA) with inner diameters of 20-40nm. The encapsulation of enhanced green fluorescent <span class="hlt">protein</span> (eGFP) and resultant confinement effect for eGFP within these nanotubes is studied via confocal microscopy. Timed release rate studies of eGFP encapsulated in LCA nanotubes and fluorescence recovery after photobleaching (FRAP) indicate that the diffusive transport of eGFP out of and/or within the nanotubes is very slow, in contrast to the rapid introduction of eGFP into the nanotubes. By encapsulating two fluorescent <span class="hlt">proteins</span> in LCA nanotubes, eGFP and mCherry, as a fluorescence resonance energy transfer (FRET) pair, the FRET efficiencies are determined using FRET imaging microscopy at three different <span class="hlt">protein</span> <span class="hlt">concentrations</span> with a fixed donor-to-acceptor ratio of 1:1. Förster theory reveals that the <span class="hlt">proteins</span> are spatially separated by 4.8-7.2nm in distance inside these nanotubes. The biomimetic nanochannels of LCA nanotubes not only afford a confining effect on eGFP that results in enhanced chemical and thermal stability under conditions of high denaturant <span class="hlt">concentration</span> and temperature, but also function as <span class="hlt">protein</span> <span class="hlt">concentrators</span> for enriching <span class="hlt">protein</span> in the nanochannels from a diluted <span class="hlt">protein</span> solution by up to two orders of magnitude.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26574036','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26574036"><span id="translatedtitle">Replacing soybean meal with gelatin extracted from cow skin and corn <span class="hlt">protein</span> <span class="hlt">concentrate</span> as a <span class="hlt">protein</span> source in broiler diets.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Khalaji, S; Manafi, M; Olfati, Z; Hedyati, M; Latifi, M; Veysi, A</p> <p>2016-02-01</p> <p>Two experiments were conducted to investigate the effects of replacing soybean meal with gelatin extracted from cow skin and corn <span class="hlt">protein</span> <span class="hlt">concentrate</span> as a <span class="hlt">protein</span> source in broiler diets. Experiments were carried out as a completely randomized design where each experiment involved 4 treatments of 6 replicates and 10 chicks in each pen. Soybean meal <span class="hlt">proteins</span> in a corn-soy control diet were replaced with 15, 30, and 45% of cow skin gelatin (CSG) or corn <span class="hlt">protein</span> <span class="hlt">concentrate</span> (CPC), respectively, in experiments 1 and 2. BW and cumulative feed intake were measured at 7, 21, and 42 d of age. Blood characteristics, relative organs weight and length, ileal digesta viscosity, ileal morphology, and cecal coliform and Salmonella population were measured at 42 d of age. Apparent total tract digestibility of <span class="hlt">protein</span> was determined during 35 to 42 d of age. Replacement of soybean meal with CSG severely inhibited BW gain, decreased feed intake, and increased FCR in broilers during the experimental period (P ≤ 0.01). The inclusion of CPC reduced BW and increased FCR significantly (P ≤ 0.05) at 21 and 42 d of age without any consequence in feed intake. <span class="hlt">Protein</span> digestibility was reduced and ileal digesta viscosity was increased linearly by increasing the amount of CSG and CPC in the control diet (P ≤ 0.01). Replacement of soybean meal with CSG and CPC did not significantly alter blood cell profile and plasma phosphorus, creatinine, blood urea nitrogen, Aspartate transaminase, and HDL and LDL cholesterol <span class="hlt">concentration</span>. The inclusion of CSG linearly (P ≤ 0.05) increased plasma uric acid <span class="hlt">concentration</span> and alkaline phosphatase activity. Triglyceride and cholesterol levels were decreased significantly (P ≤ 0.05) when the amount of CSG replacement was 15%. The results of this experiment showed that using CSG and CPC negatively affects broiler performance and therefore is not a suitable alternative to soybean meal in commercial diets.</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_7");'>7</a></li> <li><a href="#" onclick='return showDiv("page_8");'>8</a></li> <li class="active"><span>9</span></li> <li><a href="#" onclick='return showDiv("page_10");'>10</a></li> <li><a href="#" onclick='return showDiv("page_11");'>11</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_9 --> <div id="page_10" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_8");'>8</a></li> <li><a href="#" onclick='return showDiv("page_9");'>9</a></li> <li class="active"><span>10</span></li> <li><a href="#" onclick='return showDiv("page_11");'>11</a></li> <li><a href="#" onclick='return showDiv("page_12");'>12</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="181"> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26574036','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26574036"><span id="translatedtitle">Replacing soybean meal with gelatin extracted from cow skin and corn <span class="hlt">protein</span> <span class="hlt">concentrate</span> as a <span class="hlt">protein</span> source in broiler diets.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Khalaji, S; Manafi, M; Olfati, Z; Hedyati, M; Latifi, M; Veysi, A</p> <p>2016-02-01</p> <p>Two experiments were conducted to investigate the effects of replacing soybean meal with gelatin extracted from cow skin and corn <span class="hlt">protein</span> <span class="hlt">concentrate</span> as a <span class="hlt">protein</span> source in broiler diets. Experiments were carried out as a completely randomized design where each experiment involved 4 treatments of 6 replicates and 10 chicks in each pen. Soybean meal <span class="hlt">proteins</span> in a corn-soy control diet were replaced with 15, 30, and 45% of cow skin gelatin (CSG) or corn <span class="hlt">protein</span> <span class="hlt">concentrate</span> (CPC), respectively, in experiments 1 and 2. BW and cumulative feed intake were measured at 7, 21, and 42 d of age. Blood characteristics, relative organs weight and length, ileal digesta viscosity, ileal morphology, and cecal coliform and Salmonella population were measured at 42 d of age. Apparent total tract digestibility of <span class="hlt">protein</span> was determined during 35 to 42 d of age. Replacement of soybean meal with CSG severely inhibited BW gain, decreased feed intake, and increased FCR in broilers during the experimental period (P ≤ 0.01). The inclusion of CPC reduced BW and increased FCR significantly (P ≤ 0.05) at 21 and 42 d of age without any consequence in feed intake. <span class="hlt">Protein</span> digestibility was reduced and ileal digesta viscosity was increased linearly by increasing the amount of CSG and CPC in the control diet (P ≤ 0.01). Replacement of soybean meal with CSG and CPC did not significantly alter blood cell profile and plasma phosphorus, creatinine, blood urea nitrogen, Aspartate transaminase, and HDL and LDL cholesterol <span class="hlt">concentration</span>. The inclusion of CSG linearly (P ≤ 0.05) increased plasma uric acid <span class="hlt">concentration</span> and alkaline phosphatase activity. Triglyceride and cholesterol levels were decreased significantly (P ≤ 0.05) when the amount of CSG replacement was 15%. The results of this experiment showed that using CSG and CPC negatively affects broiler performance and therefore is not a suitable alternative to soybean meal in commercial diets. PMID:26574036</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4396178','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4396178"><span id="translatedtitle">Effect of <span class="hlt">Protein</span> Binding on Unbound Atazanavir and Darunavir Cerebrospinal Fluid <span class="hlt">Concentrations</span></span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Delille, Cecile A.; Pruett, Sarah T.; Marconi, Vincent C.; Lennox, Jeffrey L.; Armstrong, Wendy S.; Arrendale, Richard F.; Sheth, Anandi N.; Easley, Kirk A.; Acosta, Edward P.; Vunnava, Aswani; Ofotokun, Ighovwerha</p> <p>2015-01-01</p> <p>HIV-1 protease inhibitors (PIs) exhibit different <span class="hlt">protein</span> binding affinities and achieve variable plasma and tissue <span class="hlt">concentrations</span>. Degree of plasma <span class="hlt">protein</span> binding may impact central nervous system penetration. This cross-sectional study assessed cerebrospinal fluid (CSF) unbound PI <span class="hlt">concentrations</span>, HIV-1 RNA, and neopterin levels in subjects receiving either ritonavir-boosted darunavir (DRV), 95% plasma <span class="hlt">protein</span> bound, or atazanavir (ATV), 86% bound. Unbound PI trough <span class="hlt">concentrations</span> were measured using rapid equilibrium dialysis and liquid chromatography/tandem mass spectrometry. Plasma and CSF HIV-1 RNA and neopterin were measured by Ampliprep/COBAS® Taqman® 2.0 assay (Roche) and enzyme-linked immunosorbent assay (ALPCO), respectively. CSF/plasma unbound drug <span class="hlt">concentration</span> ratio was higher for ATV, 0.09 [95% confidence interval (CI) 0.06–0.12] than DRV, 0.04 (95%CI 0.03–0.06). Unbound CSF <span class="hlt">concentrations</span> were lower than <span class="hlt">protein</span> adjusted wild-type inhibitory <span class="hlt">concentration</span>-50 (IC50) in all ATV and 1 DRV-treated subjects (P < 0.001). CSF HIV-1 RNA was detected in 2/15 ATV and 4/15 DRV subjects (P = 0.65). CSF neopterin levels were low and similar between arms. ATV relative to DRV had higher CSF/plasma unbound drug ratio. Low CSF HIV-1 RNA and neopterin suggest that both regimens resulted in CSF virologic suppression and controlled inflammation. PMID:24691856</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://pubs.er.usgs.gov/publication/70126407','USGSPUBS'); return false;" href="http://pubs.er.usgs.gov/publication/70126407"><span id="translatedtitle">Ground level environmental <span class="hlt">protein</span> <span class="hlt">concentrations</span> in various ecuadorian environments: potential uses of aerosolized <span class="hlt">protein</span> for ecological research</span></a></p> <p><a target="_blank" href="http://pubs.er.usgs.gov/pubs/index.jsp?view=adv">USGS Publications Warehouse</a></p> <p>Staton, Sarah J.R.; Woodward, Andrea; Castillo, Josemar A.; Swing, Kelly; Hayes, Mark A.</p> <p>2014-01-01</p> <p>Large quantities of free <span class="hlt">protein</span> in the environment and other bioaerosols are ubiquitous throughout terrestrial ground level environments and may be integrative indicators of ecosystem status. Samples of ground level bioaerosols were collected from various ecosystems throughout Ecuador, including pristine humid tropical forest (pristine), highly altered secondary humid tropical forest (highly altered), secondary transitional very humid forest (regrowth transitional), and suburban dry montane deforested (suburban deforested). The results explored the sensitivity of localized aerosol <span class="hlt">protein</span> <span class="hlt">concentrations</span> to spatial and temporal variations within ecosystems, and their value for assessing environmental change. Ecosystem specific variations in environmental <span class="hlt">protein</span> <span class="hlt">concentrations</span> were observed: pristine 0.32 ± 0.09 μg/m3, highly altered 0.07 ± 0.05 μg/m3, regrowth transitional 0.17 ± 0.06 μg/m3, and suburban deforested 0.09 ± 0.04 μg/m3. Additionally, comparisons of intra-environmental differences in seasonal/daily weather (dry season 0.08 ± 0.03 μg/m3 and wet season 0.10 ± 0.04 μg/m3), environmental fragmentation (buffered 0.19 ± 0.06 μg/m3 and edge 0.15 ± 0.06 μg/m3), and sampling height (ground level 0.32 ± 0.09 μg/m3 and 10 m 0.24 ± 0.04 μg/m3) demonstrated the sensitivity of <span class="hlt">protein</span> <span class="hlt">concentrations</span> to environmental conditions. Local <span class="hlt">protein</span> <span class="hlt">concentrations</span> in altered environments correlated well with satellite-based spectral indices describing vegetation productivity: normalized difference vegetation index (NDVI) (r2 = 0.801), net primary production (NPP) (r2 = 0.827), leaf area index (LAI) (r2 = 0.410). Moreover, <span class="hlt">protein</span> <span class="hlt">concentrations</span> distinguished the pristine site, which was not differentiated in spectral indices, potentially due to spectral saturation typical of highly vegetated environments. Bioaerosol <span class="hlt">concentrations</span> represent an inexpensive method to increase understanding of environmental changes, especially in densely vegetated</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/19871859','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/19871859"><span id="translatedtitle">THE SIGNIFICANCE OF THE HYDROGEN ION <span class="hlt">CONCENTRATION</span> FOR THE DIGESTION OF <span class="hlt">PROTEINS</span> BY PEPSIN.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Northrop, J H</p> <p>1920-11-20</p> <p>The experiments described above show that the rate of digestion and the conductivity of <span class="hlt">protein</span> solutions are very closely parallel. If the isoelectric point of a <span class="hlt">protein</span> is at a lower hydrogen ion <span class="hlt">concentration</span> than that of another, the conductivity and also the rate of digestion of the first <span class="hlt">protein</span> extends further to the alkaline side. The optimum hydrogen ion <span class="hlt">concentration</span> for the rate of digestion and the degree of ionization (conductivity) of gelatin solutions is the same, and the curves for the ionization and rate of digestion as plotted against the pH are nearly parallel throughout. The addition of a salt with the same anion as the acid to a solution of <span class="hlt">protein</span> already containing the optimum amount of the acid has the same depressing effect on the digestion as has the addition of the equivalent amount of acid. These facts are in quantitative agreement with the hypothesis that the determining factor in the digestion of <span class="hlt">proteins</span> by pepsin is the amount of ionized <span class="hlt">protein</span> present in the solution. It was shown in a previous paper that this would also account for the peculiar relation between the rate of digestion and the <span class="hlt">concentration</span> of <span class="hlt">protein</span>. The amount of ionized <span class="hlt">protein</span> in the solution depends on the amount of salt formed between the <span class="hlt">protein</span> (a weak base) and the acid. This quantity, in turn, according to the hydrolysis theory of the salts of weak bases and strong acids, is a function of the hydrogen ion <span class="hlt">concentration</span>, up to the point at which all the <span class="hlt">protein</span> is combined with the acid as a salt. This point is the optimum hydrogen ion <span class="hlt">concentration</span> for digestion, since the solution now contains the maximum <span class="hlt">concentration</span> of <span class="hlt">protein</span> ions. The hydrogen ion <span class="hlt">concentration</span> in this range therefore is merely a convenient indicator of the amount of ionized <span class="hlt">protein</span> present in the solution and takes no active part in the hydrolysis. After sufficient acid has been added to combine with all the <span class="hlt">protein</span>, i.e. at pH of about 2.0, the further addition of acid serves to</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26375304','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26375304"><span id="translatedtitle">Squeeze flow rheometry as a novel tool for the characterization of highly <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Schermeyer, Marie-Therese; Sigloch, Heike; Bauer, Katharina C; Oelschlaeger, Claude; Hubbuch, Jürgen</p> <p>2016-03-01</p> <p>This study aims at defining rheological parameters for the characterization of highly <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions. As a basis for comparing rheological behavior with <span class="hlt">protein</span> solution characteristics the <span class="hlt">protein</span> phase behavior of Lysozyme from chicken egg white with <span class="hlt">concentrations</span> up to 225 mg/mL, changing pH values and additive <span class="hlt">concentrations</span> was studied in a microbatch scale format. The prepared phase diagrams, scored after 40 days (t40) give insights into the kind and kinetics of the phase transitions that occur. Oscillatory frequency sweep measurements of samples with exactly the same conditions were conducted immediately after preparation (t0). The <span class="hlt">protein</span> solutions behave viscoelastic and show a characteristic curve shape of the storage modulus (G') and the loss modulus (G″). The graphs provide information about the cross-linking degree of the respective sample. The measured rheological parameters were sensitive concerning solution composition, <span class="hlt">protein</span> <span class="hlt">concentration</span> and solution inner structure. The rheological moduli G' and G″ and especially the ratio of these parameters over a frequency range from 100 to 40000 rad/sec give information about the aggregation tendency of the <span class="hlt">protein</span> under tested conditions. We succeeded to correlate <span class="hlt">protein</span> phase behavior with the defined rheological key parameter ωCO. This point represents the frequency value of the intersection point from G' and G″. In our study Lysozyme expressed a ωCO threshold value of 20000 rad/sec as a lower limit for stable <span class="hlt">protein</span> solutions. The predictability of lysozyme aggregation tendency and crystallization by means of squeeze flow rheometry is shown. PMID:26375304</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26364115','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26364115"><span id="translatedtitle">Effect of temperature and <span class="hlt">concentration</span> on benzoyl peroxide bleaching efficacy and benzoic acid levels in whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Smith, T J; Gerard, P D; Drake, M A</p> <p>2015-11-01</p> <p>Much of the fluid whey produced in the United States is a by-product of Cheddar cheese manufacture and must be bleached. Benzoyl peroxide (BP) is currently 1 of only 2 legal chemical bleaching agents for fluid whey in the United States, but benzoic acid is an unavoidable by-product of BP bleaching. Benzoyl peroxide is typically a powder, but new liquid BP dispersions are available. A greater understanding of the bleaching characteristics of BP is necessary. The objective of the study was to compare norbixin destruction, residual benzoic acid, and flavor differences between liquid whey and 80% whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> (WPC80) bleached at different temperatures with 2 different benzoyl peroxides (soluble and insoluble). Two experiments were conducted in this study. For experiment 1, 3 factors (temperature, bleach type, bleach <span class="hlt">concentration</span>) were evaluated for norbixin destruction using a response surface model-central composite design in liquid whey. For experiment 2, norbixin <span class="hlt">concentration</span>, residual benzoic acid, and flavor differences were explored in WPC80 from whey bleached by the 2 commercially available BP (soluble and insoluble) at 5 mg/kg. In liquid whey, soluble BP bleached more norbixin than insoluble BP, especially at lower <span class="hlt">concentrations</span> (5 and 10 mg/kg) at both cold (4°C) and hot (50°C) temperatures. The WPC80 from liquid whey bleached with BP at 50°C had lower norbixin <span class="hlt">concentration</span>, benzoic acid levels, cardboard flavor, and aldehyde levels than WPC80 from liquid whey bleached with BP at 4°C. Regardless of temperature, soluble BP destroyed more norbixin at lower <span class="hlt">concentrations</span> than insoluble BP. The WPC80 from soluble-BP-bleached wheys had lower cardboard flavor and lower aldehyde levels than WPC80 from insoluble-BP-bleached whey. This study suggests that new, soluble (liquid) BP can be used at lower <span class="hlt">concentrations</span> than insoluble BP to achieve equivalent bleaching and that less residual benzoic acid remains in WPC80 powder from liquid whey</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26364115','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26364115"><span id="translatedtitle">Effect of temperature and <span class="hlt">concentration</span> on benzoyl peroxide bleaching efficacy and benzoic acid levels in whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Smith, T J; Gerard, P D; Drake, M A</p> <p>2015-11-01</p> <p>Much of the fluid whey produced in the United States is a by-product of Cheddar cheese manufacture and must be bleached. Benzoyl peroxide (BP) is currently 1 of only 2 legal chemical bleaching agents for fluid whey in the United States, but benzoic acid is an unavoidable by-product of BP bleaching. Benzoyl peroxide is typically a powder, but new liquid BP dispersions are available. A greater understanding of the bleaching characteristics of BP is necessary. The objective of the study was to compare norbixin destruction, residual benzoic acid, and flavor differences between liquid whey and 80% whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> (WPC80) bleached at different temperatures with 2 different benzoyl peroxides (soluble and insoluble). Two experiments were conducted in this study. For experiment 1, 3 factors (temperature, bleach type, bleach <span class="hlt">concentration</span>) were evaluated for norbixin destruction using a response surface model-central composite design in liquid whey. For experiment 2, norbixin <span class="hlt">concentration</span>, residual benzoic acid, and flavor differences were explored in WPC80 from whey bleached by the 2 commercially available BP (soluble and insoluble) at 5 mg/kg. In liquid whey, soluble BP bleached more norbixin than insoluble BP, especially at lower <span class="hlt">concentrations</span> (5 and 10 mg/kg) at both cold (4°C) and hot (50°C) temperatures. The WPC80 from liquid whey bleached with BP at 50°C had lower norbixin <span class="hlt">concentration</span>, benzoic acid levels, cardboard flavor, and aldehyde levels than WPC80 from liquid whey bleached with BP at 4°C. Regardless of temperature, soluble BP destroyed more norbixin at lower <span class="hlt">concentrations</span> than insoluble BP. The WPC80 from soluble-BP-bleached wheys had lower cardboard flavor and lower aldehyde levels than WPC80 from insoluble-BP-bleached whey. This study suggests that new, soluble (liquid) BP can be used at lower <span class="hlt">concentrations</span> than insoluble BP to achieve equivalent bleaching and that less residual benzoic acid remains in WPC80 powder from liquid whey</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27542494','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27542494"><span id="translatedtitle">Effect of extraction method on functional properties of flaxseed <span class="hlt">protein</span> <span class="hlt">concentrates</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Tirgar, Mina; Silcock, Patrick; Carne, Alan; Birch, E John</p> <p>2017-01-15</p> <p>Physicochemical (zeta potential (ζ), conductivity, surface hydrophobicity (H0), <span class="hlt">protein</span> solubility (PS)) and emulsifying (emulsion capacity (EC), droplet size, polydispersity (PDI), emulsifying activity (EAI), and stability (ESI) indexes) properties of alkali-(A-FPC), enzymatic-(E-FPC), and enzymatic-solvent-(ES-FPC) extracted <span class="hlt">protein</span> <span class="hlt">concentrates</span> from flaxseed meal (FM) were investigated and compared to commercial pea <span class="hlt">protein</span> <span class="hlt">concentrate</span> (PPC). The yield, composition, and properties of the <span class="hlt">protein</span> <span class="hlt">concentrates</span> were significantly influenced by the methods of extraction. All emulsions were similar in polydispersity with mono-modal droplet distribution and size of ⩽0.43μm that carried a net negative charge at neutral conditions (pH 7.0). A-FPC showed significantly higher H0 (66.14) than that of ES-FPC (52.63), and E-FPC (43.27) and was comparable to PPC (68.47). The highest solubility was found for E-FPC followed by A-FPC at neutral pH. A-FPC displayed significantly (p<0.05) the highest EC (87.91%), EAI (87.18m(2)/g) and ESI (12.51min) compared to the other <span class="hlt">protein</span> <span class="hlt">concentrates</span>. PMID:27542494</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27542494','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27542494"><span id="translatedtitle">Effect of extraction method on functional properties of flaxseed <span class="hlt">protein</span> <span class="hlt">concentrates</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Tirgar, Mina; Silcock, Patrick; Carne, Alan; Birch, E John</p> <p>2017-01-15</p> <p>Physicochemical (zeta potential (ζ), conductivity, surface hydrophobicity (H0), <span class="hlt">protein</span> solubility (PS)) and emulsifying (emulsion capacity (EC), droplet size, polydispersity (PDI), emulsifying activity (EAI), and stability (ESI) indexes) properties of alkali-(A-FPC), enzymatic-(E-FPC), and enzymatic-solvent-(ES-FPC) extracted <span class="hlt">protein</span> <span class="hlt">concentrates</span> from flaxseed meal (FM) were investigated and compared to commercial pea <span class="hlt">protein</span> <span class="hlt">concentrate</span> (PPC). The yield, composition, and properties of the <span class="hlt">protein</span> <span class="hlt">concentrates</span> were significantly influenced by the methods of extraction. All emulsions were similar in polydispersity with mono-modal droplet distribution and size of ⩽0.43μm that carried a net negative charge at neutral conditions (pH 7.0). A-FPC showed significantly higher H0 (66.14) than that of ES-FPC (52.63), and E-FPC (43.27) and was comparable to PPC (68.47). The highest solubility was found for E-FPC followed by A-FPC at neutral pH. A-FPC displayed significantly (p<0.05) the highest EC (87.91%), EAI (87.18m(2)/g) and ESI (12.51min) compared to the other <span class="hlt">protein</span> <span class="hlt">concentrates</span>.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/17983235','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/17983235"><span id="translatedtitle">Relaxation rate for an ultrafast folding <span class="hlt">protein</span> is independent of chemical denaturant <span class="hlt">concentration</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Cellmer, Troy; Henry, Eric R; Kubelka, Jan; Hofrichter, James; Eaton, William A</p> <p>2007-11-28</p> <p>The connection between free-energy surfaces and chevron plots has been investigated in a laser temperature jump kinetic study of a small ultrafast folding <span class="hlt">protein</span>, the 35-residue subdomain from the villin headpiece. Unlike all other <span class="hlt">proteins</span> that have been studied so far, no measurable dependence of the unfolding/refolding relaxation rate on denaturant <span class="hlt">concentration</span> was observed over a wide range of guanidinium chloride <span class="hlt">concentration</span>. Analysis with a simple Ising-like theoretical model shows that this denaturant-invariant relaxation rate can be explained by a large movement of the major free energy barrier, together with a denaturant- and reaction coordinate-dependent diffusion coefficient.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25694714','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25694714"><span id="translatedtitle">Turkish Tombul hazelnut (Corylus avellana L.) <span class="hlt">protein</span> <span class="hlt">concentrates</span>: functional and rheological properties.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Tatar, F; Tunç, M T; Kahyaoglu, T</p> <p>2015-02-01</p> <p>Turkish Tombul hazelnut consumed as natural or processed forms were evaluated to obtain <span class="hlt">protein</span> <span class="hlt">concentrate</span>. Defatted hazelnut flour <span class="hlt">protein</span> (DHFP) and defatted hazelnut cake <span class="hlt">protein</span> (DHCP) were produced from defatted hazelnut flour (DHF) and defatted hazelnut cake (DHC), respectively. The functional properties (<span class="hlt">protein</span> solubility, emulsifying properties, foaming capacity, and colour), and dynamic rheological characteristics of <span class="hlt">protein</span> <span class="hlt">concentrates</span> were measured. The <span class="hlt">protein</span> contents of samples varied in the range of 35-48 % (w/w, db) and 91-92 % (w/w, db) for DHF/DHC and DHFP/DHCP samples, respectively. The significant difference for water/fat absorption capacity, emulsion stability between DHF and DHC were determined. On the other hand, the solubility and emulsion activity of DHF and DHC were not significantly different (p > 0.05). Emulsion stability of DHFP (%46) was higher than that of DHCP (%35) but other functional properties were found similar. According to these results, the DHCP could be used as DHFP in food product formulations. The DHFP and DHCP samples showed different apparent viscosity at the same temperature and <span class="hlt">concentration</span>, the elastic modulus (G' value) of DHPC was also found higher than that of DHFP samples.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25559719','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25559719"><span id="translatedtitle">Predictive response surface model for heat-induced rheological changes and aggregation of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Alvarez, Pedro A; Emond, Charles; Gomaa, Ahmed; Remondetto, Gabriel E; Subirade, Muriel</p> <p>2015-02-01</p> <p>Whey <span class="hlt">proteins</span> are now far more than a by-product of cheese processing. In the last 2 decades, food manufacturers have developed them as ingredients, with the dairy industry remaining as a major user. For many applications, whey <span class="hlt">proteins</span> are modified (denatured) to alter their structure and functional properties. The objective of this research was to study the influence of 85 to 100 °C, with <span class="hlt">protein</span> <span class="hlt">concentration</span> of 8% to 12%, and treatment times of 5 to 30 min, while measuring rheological properties (storage modulus, loss modulus, and complex viscosity) and aggregation (intermolecular beta-sheet formation) in dispersions of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC). A Box-Behnken Response Surface Methodology modeled the heat denaturation of liquid sweet WPC at 3 variables and 3 levels. The model revealed a very significant fit for viscoelastic properties, and a lesser fit for <span class="hlt">protein</span> aggregation, at temperatures not previously studied. An exponential increase of rheological parameters was governed by <span class="hlt">protein</span> <span class="hlt">concentration</span> and temperature, while a modest linear relationship of aggregation was governed by temperature. Models such as these can serve as valuable guides to the ingredient and dairy industries to develop target products, as whey is a major ingredient in many functional foods.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/25694714','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/25694714"><span id="translatedtitle">Turkish Tombul hazelnut (Corylus avellana L.) <span class="hlt">protein</span> <span class="hlt">concentrates</span>: functional and rheological properties.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Tatar, F; Tunç, M T; Kahyaoglu, T</p> <p>2015-02-01</p> <p>Turkish Tombul hazelnut consumed as natural or processed forms were evaluated to obtain <span class="hlt">protein</span> <span class="hlt">concentrate</span>. Defatted hazelnut flour <span class="hlt">protein</span> (DHFP) and defatted hazelnut cake <span class="hlt">protein</span> (DHCP) were produced from defatted hazelnut flour (DHF) and defatted hazelnut cake (DHC), respectively. The functional properties (<span class="hlt">protein</span> solubility, emulsifying properties, foaming capacity, and colour), and dynamic rheological characteristics of <span class="hlt">protein</span> <span class="hlt">concentrates</span> were measured. The <span class="hlt">protein</span> contents of samples varied in the range of 35-48 % (w/w, db) and 91-92 % (w/w, db) for DHF/DHC and DHFP/DHCP samples, respectively. The significant difference for water/fat absorption capacity, emulsion stability between DHF and DHC were determined. On the other hand, the solubility and emulsion activity of DHF and DHC were not significantly different (p > 0.05). Emulsion stability of DHFP (%46) was higher than that of DHCP (%35) but other functional properties were found similar. According to these results, the DHCP could be used as DHFP in food product formulations. The DHFP and DHCP samples showed different apparent viscosity at the same temperature and <span class="hlt">concentration</span>, the elastic modulus (G' value) of DHPC was also found higher than that of DHFP samples. PMID:25694714</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27413238','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27413238"><span id="translatedtitle">Effect of <span class="hlt">protein</span> <span class="hlt">concentrations</span> on the properties of fish myofibrillar <span class="hlt">protein</span> based film compared with PVC film.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Kaewprachu, Pimonpan; Osako, Kazufumi; Benjakul, Soottawat; Rawdkuen, Saroat</p> <p>2016-04-01</p> <p>The effect of <span class="hlt">protein</span> <span class="hlt">concentrations</span> on the properties of fish myofibrillar <span class="hlt">protein</span> film (FMP) were investigated and compared with commercial wrap film (polyvinyl chloride; PVC). FMP (2 %, w/v) showed the highest mechanical properties [tensile strength: 4.38 MPa and elongation at break: 133.05 %], and water vapor permeability [2.81 × 10(-10) g m(-1) s(-1) Pa(-1)]. FMP contained high molecular weight cross-links, resulting in complex film network, as indicated by lower film solubility (19-22 %) and <span class="hlt">protein</span> solubility (0.6-1.3 %). FMP showed excellent barrier properties to UV light at the wavelength of 200-280 nm. FMP had the thickness [0.007-0.032 mm], color attributes and transparency similar to PVC film [thickness: 0.010 mm]. Therefore, <span class="hlt">protein</span> <span class="hlt">concentration</span> majority influenced the properties of develop FMP. The <span class="hlt">protein</span> content of 1 % (w/v) had potential to be developed the biodegradable film with comparable properties to the commercial wrap film.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27413238','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27413238"><span id="translatedtitle">Effect of <span class="hlt">protein</span> <span class="hlt">concentrations</span> on the properties of fish myofibrillar <span class="hlt">protein</span> based film compared with PVC film.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Kaewprachu, Pimonpan; Osako, Kazufumi; Benjakul, Soottawat; Rawdkuen, Saroat</p> <p>2016-04-01</p> <p>The effect of <span class="hlt">protein</span> <span class="hlt">concentrations</span> on the properties of fish myofibrillar <span class="hlt">protein</span> film (FMP) were investigated and compared with commercial wrap film (polyvinyl chloride; PVC). FMP (2 %, w/v) showed the highest mechanical properties [tensile strength: 4.38 MPa and elongation at break: 133.05 %], and water vapor permeability [2.81 × 10(-10) g m(-1) s(-1) Pa(-1)]. FMP contained high molecular weight cross-links, resulting in complex film network, as indicated by lower film solubility (19-22 %) and <span class="hlt">protein</span> solubility (0.6-1.3 %). FMP showed excellent barrier properties to UV light at the wavelength of 200-280 nm. FMP had the thickness [0.007-0.032 mm], color attributes and transparency similar to PVC film [thickness: 0.010 mm]. Therefore, <span class="hlt">protein</span> <span class="hlt">concentration</span> majority influenced the properties of develop FMP. The <span class="hlt">protein</span> content of 1 % (w/v) had potential to be developed the biodegradable film with comparable properties to the commercial wrap film. PMID:27413238</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26593557','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26593557"><span id="translatedtitle">Preparation of iron bound succinylated milk <span class="hlt">protein</span> <span class="hlt">concentrate</span> and evaluation of its stability.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Shilpashree, B G; Arora, Sumit; Sharma, Vivek; Bajaj, Rajesh Kumar; Tomar, S K</p> <p>2016-04-01</p> <p>Major problems associated with the fortification of soluble iron salts include chemical reactivity and incompatibility with other components. Milk <span class="hlt">protein</span> <span class="hlt">concentrate</span> (MPC) are able to bind significant amount of iron due to the presence of both casein and whey <span class="hlt">protein</span>. MPC in its native state possess very poor solubility, therefore, succinylated derivatives of MPC (succ. MPC) were also used for the preparation of <span class="hlt">protein</span>-iron complex. Preparation of the complex involved centrifugation (to remove insoluble iron), ultrafiltration (to remove unbound iron) and lyophilisation (to attain in dry form). Iron binding ability of MPC enhanced significantly (P<0.05) upon succinylation. Stability of bound iron from both varieties of complexes was monitored under different conditions encountered during processing. Higher stability (P<0.05) of bound iron was observed in succ. MPC-iron complex than native <span class="hlt">protein</span> complex. This method could be adopted for the production of stable iron enriched <span class="hlt">protein</span>, an organic iron source. PMID:26593557</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26593557','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26593557"><span id="translatedtitle">Preparation of iron bound succinylated milk <span class="hlt">protein</span> <span class="hlt">concentrate</span> and evaluation of its stability.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Shilpashree, B G; Arora, Sumit; Sharma, Vivek; Bajaj, Rajesh Kumar; Tomar, S K</p> <p>2016-04-01</p> <p>Major problems associated with the fortification of soluble iron salts include chemical reactivity and incompatibility with other components. Milk <span class="hlt">protein</span> <span class="hlt">concentrate</span> (MPC) are able to bind significant amount of iron due to the presence of both casein and whey <span class="hlt">protein</span>. MPC in its native state possess very poor solubility, therefore, succinylated derivatives of MPC (succ. MPC) were also used for the preparation of <span class="hlt">protein</span>-iron complex. Preparation of the complex involved centrifugation (to remove insoluble iron), ultrafiltration (to remove unbound iron) and lyophilisation (to attain in dry form). Iron binding ability of MPC enhanced significantly (P<0.05) upon succinylation. Stability of bound iron from both varieties of complexes was monitored under different conditions encountered during processing. Higher stability (P<0.05) of bound iron was observed in succ. MPC-iron complex than native <span class="hlt">protein</span> complex. This method could be adopted for the production of stable iron enriched <span class="hlt">protein</span>, an organic iron source.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3040988','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3040988"><span id="translatedtitle">Volumetric Interpretation of <span class="hlt">Protein</span> Adsorption: Interfacial Packing of <span class="hlt">Protein</span> Adsorbed to Hydrophobic Surfaces from Surface-Saturating Solution <span class="hlt">Concentrations</span></span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Kao, Ping; Parhi, Purnendu; Krishnan, Anandi; Noh, Hyeran; Haider, Waseem; Tadigadapa, Srinivas; Allara, David L.; Vogler, Erwin A.</p> <p>2010-01-01</p> <p>The maximum capacity of a hydrophobic adsorbent is interpreted in terms of square or hexagonal (cubic and face-centered-cubic, FCC) interfacial packing models of adsorbed blood <span class="hlt">proteins</span> in a way that accommodates experimental measurements by the solution-depletion method and quartz-crystal-microbalance (QCM) for the human <span class="hlt">proteins</span> serum albumin (HSA, 66 kDa), immunoglobulin G (IgG, 160 kDa), fibrinogen (Fib, 341 kDa), and immunoglobulin M (IgM, 1000 kDa). A simple analysis shows that adsorbent capacity is capped by a fixed mass/volume (e.g. mg/mL) surface-region (interphase) <span class="hlt">concentration</span> and not molar <span class="hlt">concentration</span>. Nearly analytical agreement between the packing models and experiment suggests that, at surface saturation, above-mentioned <span class="hlt">proteins</span> assemble within the interphase in a manner that approximates a well-ordered array. HSA saturates a hydrophobic adsorbent with the equivalent of a single square-or-hexagonally-packed layer of hydrated molecules whereas the larger <span class="hlt">proteins</span> occupy two-or-more layers, depending on the specific <span class="hlt">protein</span> under consideration and analytical method used to measure adsorbate mass (solution depletion or QCM). Square-or-hexagonal (cubic and FCC) packing models cannot be clearly distinguished by comparison to experimental data. QCM measurement of adsorbent capacity is shown to be significantly different than that measured by solution depletion for similar hydrophobic adsorbents. The underlying reason is traced to the fact that QCM measures contribution of both core <span class="hlt">protein</span>, water of hydration, and interphase water whereas solution depletion measures only the contribution of core <span class="hlt">protein</span>. It is further shown that thickness of the interphase directly measured by QCM systematically exceeds that inferred from solution-depletion measurements, presumably because the static model used to interpret solution depletion does not accurately capture the complexities of the viscoelastic interfacial environment probed by QCM. PMID:21035180</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26519975','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26519975"><span id="translatedtitle">Effect of ceramic membrane channel diameter on limiting retentate <span class="hlt">protein</span> <span class="hlt">concentration</span> during skim milk microfiltration.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Adams, Michael C; Barbano, David M</p> <p>2016-01-01</p> <p>Our objective was to determine the effect of retentate flow channel diameter (4 or 6mm) of nongraded permeability 100-nm pore size ceramic membranes operated in nonuniform transmembrane pressure mode on the limiting retentate <span class="hlt">protein</span> <span class="hlt">concentration</span> (LRPC) while microfiltering (MF) skim milk at a temperature of 50°C, a flux of 55 kg · m(-2) · h(-1), and an average cross-flow velocity of 7 m · s(-1). At the above conditions, the retentate true <span class="hlt">protein</span> <span class="hlt">concentration</span> was incrementally increased from 7 to 11.5%. When temperature, flux, and average cross-flow velocity were controlled, ceramic membrane retentate flow channel diameter did not affect the LRPC. This indicates that LRPC is not a function of the Reynolds number. Computational fluid dynamics data, which indicated that both membranes had similar radial velocity profiles within their retentate flow channels, supported this finding. Membranes with 6-mm flow channels can be operated at a lower pressure decrease from membrane inlet to membrane outlet (ΔP) or at a higher cross-flow velocity, depending on which is controlled, than membranes with 4-mm flow channels. This implies that 6-mm membranes could achieve a higher LRPC than 4-mm membranes at the same ΔP due to an increase in cross-flow velocity. In theory, the higher LRPC of the 6-mm membranes could facilitate 95% serum <span class="hlt">protein</span> removal in 2 MF stages with diafiltration between stages if no serum <span class="hlt">protein</span> were rejected by the membrane. At the same flux, retentate <span class="hlt">protein</span> <span class="hlt">concentration</span>, and average cross-flow velocity, 4-mm membranes require 21% more energy to remove a given amount of permeate than 6-mm membranes, despite the lower surface area of the 6-mm membranes. Equations to predict skim milk MF retentate viscosity as a function of <span class="hlt">protein</span> <span class="hlt">concentration</span> and temperature are provided. Retentate viscosity, retentate recirculation pump frequency required to maintain a given cross-flow velocity at a given retentate viscosity, and retentate <span class="hlt">protein</span></p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25828972','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25828972"><span id="translatedtitle">Effect of serum monoclonal <span class="hlt">protein</span> <span class="hlt">concentration</span> on haemostasis in patients with multiple myeloma.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Huang, Heyu; Li, Huijun; Li, Dengju</p> <p>2015-07-01</p> <p>Abnormalities in haemostasis are often detected in patients with multiple myeloma and the fundamental factors that lead to these abnormities are worthy of exploration. The objective of this study was to investigate bleeding diathesis and coagulopathy in different multiple myeloma types or stages and assess how paraprotein <span class="hlt">concentration</span> contributes to differences in these conditions. Haemostasis screening tests and serum monoclonal <span class="hlt">protein</span> (M <span class="hlt">protein</span>) <span class="hlt">concentration</span> were retrospectively analysed in 101 patients newly diagnosed with multiple myeloma from January 2012 to April 2014. No significant differences were found between bleeding diathesis and types or International Staging System (ISS) stages of multiple myeloma; however, prolonged thrombin time (TT) was found in most of patients (77.7%) and was positively related to light-chain <span class="hlt">concentration</span> (P ≤ 0.01). Prolonged prothrombin time (PT) was more obvious in IgA and IgG-type multiple myeloma than in the light-chain type (P ≤ 0.01). With increased clinical staging, PT remarkably increased (P ≤ 0.01). M <span class="hlt">protein</span> <span class="hlt">concentration</span> was significantly higher in patients with prolonged PT than in those with normal PT (P ≤ 0.01). The D-dimer mean was significantly higher than normal (>0.5 μg/ml) (P ≤ 0.01). Fibrinogen was negatively related to M <span class="hlt">protein</span> levels (P ≤ 0.01); however, there was no correlation between activated partial thromboplastin time (APTT) and multiple myeloma stages or types, M <span class="hlt">protein</span> levels and serum light-chain <span class="hlt">concentration</span> (P ≥ 0.05). Patients with light-chain type multiple myeloma were more likely to have prolonged TT than patients with other types. M <span class="hlt">protein</span> levels had an obvious effect on PT. Prolonged PT was more common in IgA and IgG-type multiple myeloma. Abnormal haemostasis test results are not always accompanied by clinically apparent haemostatic complications.</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_8");'>8</a></li> <li><a href="#" onclick='return showDiv("page_9");'>9</a></li> <li class="active"><span>10</span></li> <li><a href="#" onclick='return showDiv("page_11");'>11</a></li> <li><a href="#" onclick='return showDiv("page_12");'>12</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_10 --> <div id="page_11" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_9");'>9</a></li> <li><a href="#" onclick='return showDiv("page_10");'>10</a></li> <li class="active"><span>11</span></li> <li><a href="#" onclick='return showDiv("page_12");'>12</a></li> <li><a href="#" onclick='return showDiv("page_13");'>13</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="201"> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26259025','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26259025"><span id="translatedtitle">The impact of the <span class="hlt">concentration</span> of drug binding plasma <span class="hlt">proteins</span> on drug distribution according to Øie-Tozer's model.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Svennebring, Andreas Mats</p> <p>2016-01-01</p> <p>1. New equations have been developed from an updated version of Øie-Tozer's model expressing how the free <span class="hlt">concentration</span> and volume of distribution change in relation to changes in the <span class="hlt">concentration</span> of drug binding plasma <span class="hlt">proteins</span>. This updated model accommodates more than one drug binding plasma <span class="hlt">protein</span> to contribute to the plasma <span class="hlt">protein</span> binding. 2. Demonstrations of the model show that variability in the <span class="hlt">concentration</span> of one plasma <span class="hlt">protein</span> has considerably less impact on the free drug <span class="hlt">concentration</span> and volume of distribution if other plasma <span class="hlt">proteins</span> contribute to binding, than if they don't.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/15910173','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/15910173"><span id="translatedtitle">Products of DNA, <span class="hlt">protein</span> and lipid oxidative damage in relation to vitamin C plasma <span class="hlt">concentration</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Krajcovicová-Kudlácková, M; Dusinská, M; Valachovicová, M; Blazícek, P; Pauková, V</p> <p>2006-01-01</p> <p>Oxidative stress plays an important role in the pathogenesis of numerous chronic age-related free radical-induced diseases. Improved antioxidant status minimizes oxidative damage to DNA, <span class="hlt">proteins</span>, lipids and other biomolecules. Diet-derived antioxidants such as vitamin C, vitamin E, carotenoids and related plant pigments are important in antioxidative defense and maintaining health. The results of long-term epidemiological and clinical studies suggest that protective vitamin C plasma <span class="hlt">concentration</span> for minimum risk of free radical disease is higher than 50 micromol/l. Products of oxidative damage to DNA (DNA strand breaks with oxidized purines and pyrimidines), <span class="hlt">proteins</span> (carbonyls) and lipids (conjugated dienes of fatty acids, malondialdehyde) were estimated in a group of apparently healthy adult non-smoking population in dependence on different vitamin C plasma <span class="hlt">concentrations</span>. Under conditions of protective plasma vitamin C <span class="hlt">concentrations</span> (>50 micromol/l) significantly lower values of DNA, <span class="hlt">protein</span> and lipid oxidative damage were found in comparison with the vitamin C-deficient group (<50 micromol/l). The inhibitory effect of higher fruit and vegetable consumption (leading to higher vitamin C intake and higher vitamin C plasma <span class="hlt">concentrations</span>) on oxidation of DNA, <span class="hlt">proteins</span> and lipids is also expressed by an inverse significant correlation between plasma vitamin C and products of oxidative damage. The results suggest an important role of higher and frequent consumption of protective food (fruit, vegetables, vegetable oils, nuts, seeds and cereal grains) in prevention of free radical disease.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=317414','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=317414"><span id="translatedtitle">Economic feasibility of segregating dark northern spring wheat by <span class="hlt">protein</span> <span class="hlt">concentration</span> during harvest</span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>In-line, optical sensing has been developed for on-combine measurement and mapping of grain <span class="hlt">protein</span> <span class="hlt">concentration</span> (GPC). The objective of this study was to estimate changes in costs and net returns from using this technology for segregation of the dark northern spring (DNS) subclass of hard red whe...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=314848','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=314848"><span id="translatedtitle">Changes in volatile compounds in whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> stored at elevated temperature and humidity</span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>Whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) has been recommended for use in emergency aid programs, but it is often stored overseas without temperature and relative humidity (RH) control, which may cause it to be rejected because of yellowing, off-flavors, or clumping. Therefore, the volatile compounds present ...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/15202660','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/15202660"><span id="translatedtitle">Minimizing variations in functionality of whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> from different sources.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Onwulata, C I; Konstance, R P; Tomasula, P M</p> <p>2004-03-01</p> <p>Enhancement in processing technology has improved the nutritional and functional properties of whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> by increasing the content and quality of the <span class="hlt">protein</span>, leading to their increased use in different food products. The extent of heat treatment affects the quality of the whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>, and wide variation in product quality exists due to the various means of manufacture and from the whey product history from farm to factory. The study was carried out with 6 commercial whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> with 80% <span class="hlt">protein</span> (WPC80) to determine variations in physical properties, particle size and density, and functional properties--solubility, gel strength, foam volume, and stability. Significant differences were observed among all the products for every property compared. Particulate size was the most important determinant of functional characteristics. Larger particulate WPC80 had significantly higher fat content and were less soluble with poor foam stability; but narrowing the particle size distribution through sieving, minimized variations. We determined that sieving all products within the particle size distribution range of 100 to 150 microns minimized variation in physical composition, making functionality uniform. WPC80 from different manufacturers can be made to perform uniformly within a narrow functionality range by reducing the particle size distribution through sieving. PMID:15202660</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/15202660','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/15202660"><span id="translatedtitle">Minimizing variations in functionality of whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> from different sources.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Onwulata, C I; Konstance, R P; Tomasula, P M</p> <p>2004-03-01</p> <p>Enhancement in processing technology has improved the nutritional and functional properties of whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> by increasing the content and quality of the <span class="hlt">protein</span>, leading to their increased use in different food products. The extent of heat treatment affects the quality of the whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>, and wide variation in product quality exists due to the various means of manufacture and from the whey product history from farm to factory. The study was carried out with 6 commercial whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> with 80% <span class="hlt">protein</span> (WPC80) to determine variations in physical properties, particle size and density, and functional properties--solubility, gel strength, foam volume, and stability. Significant differences were observed among all the products for every property compared. Particulate size was the most important determinant of functional characteristics. Larger particulate WPC80 had significantly higher fat content and were less soluble with poor foam stability; but narrowing the particle size distribution through sieving, minimized variations. We determined that sieving all products within the particle size distribution range of 100 to 150 microns minimized variation in physical composition, making functionality uniform. WPC80 from different manufacturers can be made to perform uniformly within a narrow functionality range by reducing the particle size distribution through sieving.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/18550484','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/18550484"><span id="translatedtitle">Urine <span class="hlt">protein</span> electrophoresis and immunoelectrophoresis using unconcentrated or minimally <span class="hlt">concentrated</span> urine samples.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Roden, Anja C; Lockington, Karen S; Tostrud, Linda J; Katzmann, Jerry A</p> <p>2008-07-01</p> <p>Our objective was to evaluate a gel system that uses unconcentrated urine specimens for <span class="hlt">protein</span> electrophoresis (PEL) and immunofixation electrophoresis (IFE) in patients with monoclonal gammopathies. For the study, 222 urine specimens were analyzed by our current PEL method (Helena Laboratories, Beaumont, TX) and by a system that recommends use of unconcentrated urine (Sebia, Norcross, GA). M <span class="hlt">protein</span> <span class="hlt">concentrations</span> were compared in the 43 cases with a measurable M spike. IFE was performed on 111 of the samples using both methods. There was a 97% concordance for detection of PEL abnormalities. The concordance for IFE was 98%. M <span class="hlt">protein</span> <span class="hlt">concentrations</span> by the 2 methods correlated well (r2=0.99; slope, 1.04). Cases with insufficient urine volumes for <span class="hlt">concentration</span> (PEL, 7; IFE, 20) were analyzed in the Sebia gel system, and in 11 cases (PEL, 2; IFE, 9) an M <span class="hlt">protein</span> was identified.High-resolution gel electrophoresis of urine using the Sebia system offers similar performance for detection, characterization, and quantification of M <span class="hlt">proteins</span> when compared with our current gel system. Testing unconcentrated urine specimens will mean fewer sample rejections owing to insufficient sample volume.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27313585','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27313585"><span id="translatedtitle">Split Nitrogen Application Improves Wheat Baking Quality by Influencing <span class="hlt">Protein</span> Composition Rather Than <span class="hlt">Concentration</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Xue, Cheng; Auf'm Erley, Gunda Schulte; Rossmann, Anne; Schuster, Ramona; Koehler, Peter; Mühling, Karl-Hermann</p> <p>2016-01-01</p> <p>The use of late nitrogen (N) fertilization (N application at late growth stages of wheat, e.g., booting, heading or anthesis) to improve baking quality of wheat has been questioned. Although it increases <span class="hlt">protein</span> <span class="hlt">concentration</span>, the beneficial effect on baking quality (bread loaf volume) needs to be clearly understood. Two pot experiments were conducted aiming to evaluate whether late N is effective under controlled conditions and if these effects result from increased N rate or N splitting. Late N fertilizers were applied either as additional N or split from the basal N at late boot stage or heading in the form of nitrate-N or urea. Results showed that late N fertilization improved loaf volume of wheat flour by increasing grain <span class="hlt">protein</span> <span class="hlt">concentration</span> and altering its composition. Increasing N rate mainly enhanced grain <span class="hlt">protein</span> quantitatively. However, N splitting changed grain <span class="hlt">protein</span> composition by enhancing the percentages of gliadins and glutenins as well as certain high molecular weight glutenin subunits (HMW-GS), which led to an improved baking quality of wheat flour. The late N effects were greater when applied as nitrate-N than urea. The proportions of glutenin and x-type HMW-GS were more important than the overall <span class="hlt">protein</span> <span class="hlt">concentration</span> in determining baking quality. N splitting is more effective in improving wheat quality than the increase in the N rate by late N, which offers the potential to cut down N fertilization rates in wheat production systems.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27313585','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27313585"><span id="translatedtitle">Split Nitrogen Application Improves Wheat Baking Quality by Influencing <span class="hlt">Protein</span> Composition Rather Than <span class="hlt">Concentration</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Xue, Cheng; Auf'm Erley, Gunda Schulte; Rossmann, Anne; Schuster, Ramona; Koehler, Peter; Mühling, Karl-Hermann</p> <p>2016-01-01</p> <p>The use of late nitrogen (N) fertilization (N application at late growth stages of wheat, e.g., booting, heading or anthesis) to improve baking quality of wheat has been questioned. Although it increases <span class="hlt">protein</span> <span class="hlt">concentration</span>, the beneficial effect on baking quality (bread loaf volume) needs to be clearly understood. Two pot experiments were conducted aiming to evaluate whether late N is effective under controlled conditions and if these effects result from increased N rate or N splitting. Late N fertilizers were applied either as additional N or split from the basal N at late boot stage or heading in the form of nitrate-N or urea. Results showed that late N fertilization improved loaf volume of wheat flour by increasing grain <span class="hlt">protein</span> <span class="hlt">concentration</span> and altering its composition. Increasing N rate mainly enhanced grain <span class="hlt">protein</span> quantitatively. However, N splitting changed grain <span class="hlt">protein</span> composition by enhancing the percentages of gliadins and glutenins as well as certain high molecular weight glutenin subunits (HMW-GS), which led to an improved baking quality of wheat flour. The late N effects were greater when applied as nitrate-N than urea. The proportions of glutenin and x-type HMW-GS were more important than the overall <span class="hlt">protein</span> <span class="hlt">concentration</span> in determining baking quality. N splitting is more effective in improving wheat quality than the increase in the N rate by late N, which offers the potential to cut down N fertilization rates in wheat production systems. PMID:27313585</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4887469','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4887469"><span id="translatedtitle">Split Nitrogen Application Improves Wheat Baking Quality by Influencing <span class="hlt">Protein</span> Composition Rather Than <span class="hlt">Concentration</span></span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Xue, Cheng; auf’m Erley, Gunda Schulte; Rossmann, Anne; Schuster, Ramona; Koehler, Peter; Mühling, Karl-Hermann</p> <p>2016-01-01</p> <p>The use of late nitrogen (N) fertilization (N application at late growth stages of wheat, e.g., booting, heading or anthesis) to improve baking quality of wheat has been questioned. Although it increases <span class="hlt">protein</span> <span class="hlt">concentration</span>, the beneficial effect on baking quality (bread loaf volume) needs to be clearly understood. Two pot experiments were conducted aiming to evaluate whether late N is effective under controlled conditions and if these effects result from increased N rate or N splitting. Late N fertilizers were applied either as additional N or split from the basal N at late boot stage or heading in the form of nitrate-N or urea. Results showed that late N fertilization improved loaf volume of wheat flour by increasing grain <span class="hlt">protein</span> <span class="hlt">concentration</span> and altering its composition. Increasing N rate mainly enhanced grain <span class="hlt">protein</span> quantitatively. However, N splitting changed grain <span class="hlt">protein</span> composition by enhancing the percentages of gliadins and glutenins as well as certain high molecular weight glutenin subunits (HMW-GS), which led to an improved baking quality of wheat flour. The late N effects were greater when applied as nitrate-N than urea. The proportions of glutenin and x-type HMW-GS were more important than the overall <span class="hlt">protein</span> <span class="hlt">concentration</span> in determining baking quality. N splitting is more effective in improving wheat quality than the increase in the N rate by late N, which offers the potential to cut down N fertilization rates in wheat production systems. PMID:27313585</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=301759','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=301759"><span id="translatedtitle">The effect of urea infusion on the urinary <span class="hlt">concentrating</span> mechanism in <span class="hlt">protein</span>-depleted rats.</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Pennell, J P; Sanjana, V; Frey, N R; Jamison, R L</p> <p>1975-01-01</p> <p>To explore the role of urea in the urinary <span class="hlt">concentrating</span> mechanism, the contents of vasa recta, Henle's descending limbs and collecting ducts were sampled by micropuncture of the renal papilla before and after infusion of urea in 10 <span class="hlt">protein</span>-depleted rats. Eight <span class="hlt">protein</span>-depleted rats not given urea were similarly studied as a control group. After urea administration, osmolality and the <span class="hlt">concentrations</span> of urea and nonurea solute of urine from both exposed and contralateral kideny increased significantly. The osmolality and urea <span class="hlt">concentration</span> of fluid from the end of Henle's descending limb and vasa recta plasma and the tubule fluid-to-plasma inulin ratio in the end-descending limb all increased significantly after urea infusion. We interpret these observations to indicate that urea enhances urinary <span class="hlt">concentration</span> by increasing the abstraction of water from the juxtamedullary nephron (presumably the descending limb), in agreement with the prediction of recent passive models of the urinary <span class="hlt">concentrating</span> mechanism. However, the <span class="hlt">concentration</span> of urea in fluid from the descending limb after urea infusion was high (261 plus or minus 31 mM) and the difference in solium <span class="hlt">concentration</span> between descending limb fluid and vasa recta was small and statistically insignificant. PMID:1127107</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/18558706','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/18558706"><span id="translatedtitle">Immunoglobulin E-reactive <span class="hlt">proteins</span> in cashew (Anacardium occidentale) apple juice <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Comstock, Sarah S; Robotham, Jason M; Tawde, Pallavi; Kshirsagar, Harshal; Sathe, Shridhar K; Roux, Kenneth H; Teuber, Suzanne S</p> <p>2008-07-23</p> <p>Cashew apple juice has the potential to be a natural source of vitamin C and sugar in processed foods. The juice of the cashew apple is obtained by pressing the fleshy peduncle or receptacle, which forms a rounded apple that sits above the true fruit, the cashew nut. Cashew nut allergy is the second most commonly reported tree nut allergy in the United States. To determine if cashew apple juice contains cashew nut allergens, immunoblotting was performed using a cashew apple juice 6X <span class="hlt">concentrate</span> that was extracted and further <span class="hlt">concentrated</span> through dialysis, lyophilization, and resuspension. Serum IgE of individuals allergic to cashew nut bound <span class="hlt">proteins</span> in the cashew apple juice <span class="hlt">concentrate</span> extract. For some serum samples, IgE reactivity could be inhibited by preincubation of the serum with cashew nut extract, suggesting the presence of cashew nut-related allergens. Using monoclonal antibodies specific for cashew nut allergens, the <span class="hlt">concentrate</span> was found to contain Ana o 1 (vicilin) and Ana o 2 (legumin). Neither IgE from cashew nut allergic sera nor the monoclonal antibodies bound any peptides in 5 kDa filtered cashew apple juice <span class="hlt">concentrate</span>. The cashew apple juice <span class="hlt">concentrate</span> used in these studies contains <span class="hlt">proteins</span> with IgE-reactive epitopes, including cashew nut legumin and vicilin. No IgE-binding peptides remained after 5 kDa filtration of the <span class="hlt">concentrate</span>.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/24856986','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/24856986"><span id="translatedtitle">Effect of whey <span class="hlt">concentration</span> on <span class="hlt">protein</span> recovery in fresh ovine ricotta cheese.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Salvatore, E; Pes, M; Falchi, G; Pagnozzi, D; Furesi, S; Fiori, M; Roggio, T; Addis, M F; Pirisi, A</p> <p>2014-01-01</p> <p>Ricotta cheese, particularly the ovine type, is a typical Italian dairy product obtained by heat-coagulation of the <span class="hlt">proteins</span> in whey. The aim of this work was to investigate the influence of whey <span class="hlt">protein</span> <span class="hlt">concentration</span>, obtained by ultrafiltration, on yield of fresh ovine ricotta cheese. Ricotta cheeses were obtained by thermocoagulation of mixtures with <span class="hlt">protein</span> content of 1.56, 3.10, 4.16, and 7.09g/100g from the mixing of skim whey and ultrafiltered skim whey. A fat-to-<span class="hlt">protein</span> ratio of 1.1 (wt/wt) was obtained for all mixtures by adding fresh cream. The initial mixtures, as well as the final ricotta cheeses, were analyzed for their composition and by SDS-PAGE. <span class="hlt">Protein</span> bands were quantified by QuantityOne software (Bio-Rad, Hercules, CA) and identified by liquid chromatography-tandem mass spectrometry. Significant differences in the composition of the ricotta cheese were observed depending on <span class="hlt">protein</span> <span class="hlt">concentration</span>. Particularly, ricotta cheese resulting from the mixture containing 7.09g/100g of <span class="hlt">protein</span> presented higher moisture (72.88±1.50g/100g) and <span class="hlt">protein</span> (10.18±0.45g/100g) contents than that prepared from the mixture with 1.56g/100g of <span class="hlt">protein</span> (69.52±1.75 and 6.70±0.85g/100g, respectively), and fat content was lower in this sample (12.20±1.60g/100g) compared with the other treatments, with mean values between 15.72 and 20.50g/100g. Each <span class="hlt">protein</span> fraction presented a different behavior during thermocoagulation. In particular, the recovery of β-lactoglobulin and α-lactalbumin in the cheese increased as their content increased in the mixtures. It was concluded that <span class="hlt">concentrating</span> ovine rennet whey improved the extent of heat-induced <span class="hlt">protein</span> aggregation during the thermal coagulation process. This resulted in a better recovery of each <span class="hlt">protein</span> fraction in the product, and in a consequent increase of ricotta cheese yield.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/24856986','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/24856986"><span id="translatedtitle">Effect of whey <span class="hlt">concentration</span> on <span class="hlt">protein</span> recovery in fresh ovine ricotta cheese.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Salvatore, E; Pes, M; Falchi, G; Pagnozzi, D; Furesi, S; Fiori, M; Roggio, T; Addis, M F; Pirisi, A</p> <p>2014-01-01</p> <p>Ricotta cheese, particularly the ovine type, is a typical Italian dairy product obtained by heat-coagulation of the <span class="hlt">proteins</span> in whey. The aim of this work was to investigate the influence of whey <span class="hlt">protein</span> <span class="hlt">concentration</span>, obtained by ultrafiltration, on yield of fresh ovine ricotta cheese. Ricotta cheeses were obtained by thermocoagulation of mixtures with <span class="hlt">protein</span> content of 1.56, 3.10, 4.16, and 7.09g/100g from the mixing of skim whey and ultrafiltered skim whey. A fat-to-<span class="hlt">protein</span> ratio of 1.1 (wt/wt) was obtained for all mixtures by adding fresh cream. The initial mixtures, as well as the final ricotta cheeses, were analyzed for their composition and by SDS-PAGE. <span class="hlt">Protein</span> bands were quantified by QuantityOne software (Bio-Rad, Hercules, CA) and identified by liquid chromatography-tandem mass spectrometry. Significant differences in the composition of the ricotta cheese were observed depending on <span class="hlt">protein</span> <span class="hlt">concentration</span>. Particularly, ricotta cheese resulting from the mixture containing 7.09g/100g of <span class="hlt">protein</span> presented higher moisture (72.88±1.50g/100g) and <span class="hlt">protein</span> (10.18±0.45g/100g) contents than that prepared from the mixture with 1.56g/100g of <span class="hlt">protein</span> (69.52±1.75 and 6.70±0.85g/100g, respectively), and fat content was lower in this sample (12.20±1.60g/100g) compared with the other treatments, with mean values between 15.72 and 20.50g/100g. Each <span class="hlt">protein</span> fraction presented a different behavior during thermocoagulation. In particular, the recovery of β-lactoglobulin and α-lactalbumin in the cheese increased as their content increased in the mixtures. It was concluded that <span class="hlt">concentrating</span> ovine rennet whey improved the extent of heat-induced <span class="hlt">protein</span> aggregation during the thermal coagulation process. This resulted in a better recovery of each <span class="hlt">protein</span> fraction in the product, and in a consequent increase of ricotta cheese yield. PMID:24856986</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/24976461','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/24976461"><span id="translatedtitle">Effect of rising atmospheric carbon dioxide <span class="hlt">concentration</span> on the <span class="hlt">protein</span> composition of cereal grain.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Wroblewitz, Stefanie; Hüther, Liane; Manderscheid, Remy; Weigel, Hans-Joachim; Wätzig, Hermann; Dänicke, Sven</p> <p>2014-07-16</p> <p>The present study investigates effects of rising atmospheric CO2 <span class="hlt">concentration</span> on <span class="hlt">protein</span> composition of maize, wheat, and barley grain, especially on the fractions prolamins and glutelins. Cereals were grown at different atmospheric CO2 <span class="hlt">concentrations</span> to simulate future climate conditions. Influences of two nitrogen fertilization levels were studied for wheat and barley. Enriched CO2 caused an increase of globulin and B-hordein of barley. In maize, the content of globulin, α-zein, and LMW polymers decreased, whereas total glutelin, zein, δ-zein, and HMW polymers rose. Different N supplies resulted in variations of barley subfractions and wheat globulin. Other environmental influences showed effects on the content of nearly all fractions and subfractions. Variations in starch-<span class="hlt">protein</span> bodies caused by different CO2 treatments could be visualized by scanning electron microscopy. In conclusion, climate change would have impacts on structural composition of <span class="hlt">proteins</span> and, consequently, on the nutritional value of cereals.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://ntrs.nasa.gov/search.jsp?R=20040090197&hterms=cookies&qs=N%3D0%26Ntk%3DAll%26Ntx%3Dmode%2Bmatchall%26Ntt%3Dcookies','NASA-TRS'); return false;" href="http://ntrs.nasa.gov/search.jsp?R=20040090197&hterms=cookies&qs=N%3D0%26Ntk%3DAll%26Ntx%3Dmode%2Bmatchall%26Ntt%3Dcookies"><span id="translatedtitle">Potential utilization of algal <span class="hlt">protein</span> <span class="hlt">concentrate</span> as a food ingredient in space habitats</span></a></p> <p><a target="_blank" href="http://ntrs.nasa.gov/search.jsp">NASA Technical Reports Server (NTRS)</a></p> <p>Nakhost, Z.; Karel, M.</p> <p>1989-01-01</p> <p>Green alga Scenedesmus obliquus was studied as one of the potential sources of macronutrients in a space habitat. Algal <span class="hlt">protein</span> <span class="hlt">concentrate</span> (70.5% <span class="hlt">protein</span>) was incorporated into a variety of food products such as bran muffins, fettuccine (spinach noodle imitation) and chocolate chip cookies. Food products containing 20 to 40% of incorporated algal <span class="hlt">proteins</span> were considered. In the sensory analysis the greenish color of the bran muffins and cookies was not found to be objectional. The mild spinachy flavor (algae flavor) was less detectable in chocolate chip cookies than in bran muffins. The color and taste of the algae noodles were found to be pleasant and compared well with commercially available spinach noodles. Commercially available spray-dried Spirulina algae was also incorporated so the products can be compared with those containing Scenedesmus obliquus <span class="hlt">concentrate</span>. Food products containing commercial algae had a dark green color and a "burnt after taste" and were less acceptable to the panelists.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/11538068','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/11538068"><span id="translatedtitle">Potential utilization of algal <span class="hlt">protein</span> <span class="hlt">concentrate</span> as a food ingredient in space habitats.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Nakhost, Z; Karel, M</p> <p>1989-01-01</p> <p>Green alga Scenedesmus obliquus was studied as one of the potential sources of macronutrients in a space habitat. Algal <span class="hlt">protein</span> <span class="hlt">concentrate</span> (70.5% <span class="hlt">protein</span>) was incorporated into a variety of food products such as bran muffins, fettuccine (spinach noodle imitation) and chocolate chip cookies. Food products containing 20 to 40% of incorporated algal <span class="hlt">proteins</span> were considered. In the sensory analysis the greenish color of the bran muffins and cookies was not found to be objectional. The mild spinachy flavor (algae flavor) was less detectable in chocolate chip cookies than in bran muffins. The color and taste of the algae noodles were found to be pleasant and compared well with commercially available spinach noodles. Commercially available spray-dried Spirulina algae was also incorporated so the products can be compared with those containing Scenedesmus obliquus <span class="hlt">concentrate</span>. Food products containing commercial algae had a dark green color and a "burnt after taste" and were less acceptable to the panelists.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/16106389','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/16106389"><span id="translatedtitle">Antifungal activity of tuberose <span class="hlt">absolute</span> and some of its constituents.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Nidiry, Eugene Sebastian J; Babu, C S Bujji</p> <p>2005-05-01</p> <p>The antifungal activity of the <span class="hlt">absolute</span> of tuberose (Polianthes tuberosa ) and some of its constituents were evaluated against the mycelial growth of Colletotrichum gloeosporioides on potato-dextrose-agar medium. Tuberose <span class="hlt">absolute</span> showed only mild activity at a <span class="hlt">concentration</span> of 500 mg/L. However, three constituents present in the <span class="hlt">absolute</span>, namely geraniol, indole and methyl anthranilate exhibited significant activity showing total inhibition of the mycelial growth at this <span class="hlt">concentration</span>.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/1995NJSR...33..147L','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/1995NJSR...33..147L"><span id="translatedtitle">Seasonal differences in <span class="hlt">concentrations</span> of particulate lipids, <span class="hlt">proteins</span> and chitin in the North Sea</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Lardinois, D.; Eisma, D.; Chen, S.</p> <p></p> <p>The <span class="hlt">concentrations</span> of particulate lipids, <span class="hlt">proteins</span> and chitin were determined in the North Sea in January 1992, October 1992 and March 1993, with additional measurements of total suspended matter <span class="hlt">concentrations</span> and organic matter contents in the suspended matter (POC) by ashing and wet-oxidation. During each of the three cruises, the <span class="hlt">proteins</span> were by far the most important of the three components measured, followed by the lipids. The <span class="hlt">concentrations</span> of chitin were always very low. The <span class="hlt">concentrations</span> of these three components were highest in March and lowest in January; there was also a variation in the distribution over the North Sea between the three cruises. In January 1992, the suspended matter contained more organic matter in the northern North Sea than in the southern North Sea, but the higher <span class="hlt">concentrations</span> of total suspended matter in the southern North Sea resulted in an inverse distribution for the <span class="hlt">concentrations</span> of organic matter per volume of water. In March 1993, highest <span class="hlt">concentrations</span> of the three organic compounds were observed in the Skagerrak and along the eastern side of the North Sea, decreasing towards the west. The suspended matter was richest in organic compounds in the Skagerrak and in the Norwegian Channel. In October 1992, the situation was very similar to that observed in January 1992, but the <span class="hlt">concentrations</span> of organic compounds in the suspended matter and per volume of water were higher. The ratio of <span class="hlt">proteins</span> to lipids was similar to this ratio in phytoplankton. The composition of the particulate organic matter became very close to that of phytoplankton if we assume that we missed a large amount of carbohydrates; the small differences persisting were probably due to the contributions of zooplankton, bacteria and terrestrial sources. The total contents of particulate lipids + <span class="hlt">proteins</span> + chitin were low, but when estimated amounts of carbohydrates were added, the total particulate organic-matter <span class="hlt">concentrations</span> found were very similar to the</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1412312','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1412312"><span id="translatedtitle">Relationship between endotoxaemia and <span class="hlt">protein</span> <span class="hlt">concentration</span> of ascites in cirrhotic patients.</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Tarao, K; Moroi, T; Nagakura, Y; Ikeuchi, T; Suyama, T; Endo, O; Fukushima, K</p> <p>1979-01-01</p> <p>Endotoxaemia was investigated by the Limulus assay in 42 cirrhotic patients with ascites and in 33 without ascites. The incidence of endotoxaemia in the former group (59.5%) was significantly (P less than 0.05) higher than in the latter (36.4%). Correlation between endotoxaemia and specific gravity and <span class="hlt">concentrations</span> of total <span class="hlt">protein</span>, albumin, and globulin in ascitic fluid was studied in the group with ascites. The specific gravity of ascites in 25 patients with endotoxaemia was significantly greater than that in 17 patients without endotoxaemia (P less than 0.01). The <span class="hlt">concentration</span> of total <span class="hlt">protein</span> in patients with endotoxaemia (13.95 +/- 7.18 milligram, mean +/- SD) was nearly twice as high (P less than 0.01) as in patients without endotoxaemia (7.49 +/- 3.60 milligram). The <span class="hlt">protein</span> content of those who showed reactions greater or equal to 2(+) in the Limulus assay (16.78 +/- 7.14 milligram) was a significantly (P less than 0.05) higher than in those with 1(+) reaction (11.26 +/- 6.33 milligram). Moreover, the <span class="hlt">concentration</span> of albumin in patients with endotoxaemia (7.68 +/- 4.60 milligram) was more than twice that of the patients without endotoxaemia (3.39 +/- 1.58 milligram, P less than 0.01). On the other hand, globulin <span class="hlt">concentration</span> in patients with endotoxaemia was 1.6 times that of patients without endotoxaemia (P less than 0.01). Similar differences were noted between endotoxaemic and non-endotoxaemic patients in the ascites-to-serum ratio in <span class="hlt">protein</span>, albumin, and globulin. These results suggest that in liver cirrhosis endotoxaemia may cause an increase in <span class="hlt">protein</span> <span class="hlt">concentrations</span> in ascitic fluid, and that it may be a precipitating factor in the formation of ascites. PMID:437553</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_9");'>9</a></li> <li><a href="#" onclick='return showDiv("page_10");'>10</a></li> <li class="active"><span>11</span></li> <li><a href="#" onclick='return showDiv("page_12");'>12</a></li> <li><a href="#" onclick='return showDiv("page_13");'>13</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_11 --> <div id="page_12" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_10");'>10</a></li> <li><a href="#" onclick='return showDiv("page_11");'>11</a></li> <li class="active"><span>12</span></li> <li><a href="#" onclick='return showDiv("page_13");'>13</a></li> <li><a href="#" onclick='return showDiv("page_14");'>14</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="221"> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3698866','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3698866"><span id="translatedtitle"><span class="hlt">Concentration</span>-dependent control of pyruvate kinase M mutually exclusive splicing by hnRNP <span class="hlt">proteins</span></span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Chen, Mo; David, Charles J.; Manley, James L.</p> <p>2013-01-01</p> <p>Expression of the mammalian pyruvate kinase M (PKM) gene provides an important example of mutually exclusive splicing. We showed previously that the hnRNP <span class="hlt">proteins</span> A1, A2 and PTB play a critical role in this process. Here we provide evidence that <span class="hlt">concentration</span>-dependent interactions involving a network of these <span class="hlt">proteins</span> are sufficient to determine the outcome of PKM splicing. At high <span class="hlt">concentrations</span>, such as found in most cancer cells, hnRNP A1 binding to two sites in the upstream regulated exon (exon 9) orchestrates cooperative interactions leading to exon 9 exclusion. At lower <span class="hlt">concentrations</span>, binding shifts to downstream intronic sites such that exon 9 is included and exon 10 largely excluded, with any mRNA including both exons degraded by nonsense-mediated decay. Together our results provide a mechanism by which a small number of general factors control alternative splicing of a widely expressed transcript. PMID:22307054</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25248720','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25248720"><span id="translatedtitle">New procyanidin B3-human salivary <span class="hlt">protein</span> complexes by mass spectrometry. Effect of salivary <span class="hlt">protein</span> profile, tannin <span class="hlt">concentration</span>, and time stability.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Perez-Gregorio, Maria Rosa; Mateus, Nuno; De Freitas, Victor</p> <p>2014-10-15</p> <p>Several factors could influence the tannin-<span class="hlt">protein</span> interaction such as the human salivary <span class="hlt">protein</span> profile, the tannin tested, and the tannin/<span class="hlt">protein</span> ratio. The goal of this study aims to study the effect of different salivas (A, B, and C) and different tannin <span class="hlt">concentrations</span> (0.5 and 1 mg/mL) on the interaction process as well as the complex's stability over time. This study is focused on the identification of new procyanidin B3-human salivary <span class="hlt">protein</span> complexes. Thus, 48 major B3-human salivary <span class="hlt">protein</span> aggregates were identified regardless of the saliva and tannin <span class="hlt">concentration</span> tested. A higher number of aggregates was found at lower tannin <span class="hlt">concentration</span>. Moreover, the number of <span class="hlt">protein</span> moieties involved in the aggregation process was higher when the tannin <span class="hlt">concentration</span> was also higher. The selectivity of the different groups of <span class="hlt">proteins</span> to bind tannin was also confirmed. It was also verified that the B3-human salivary <span class="hlt">protein</span> complexes formed evolved over time.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2014NatCo...5E3019S','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2014NatCo...5E3019S"><span id="translatedtitle">A fully genetically encoded <span class="hlt">protein</span> architecture for optical control of peptide ligand <span class="hlt">concentration</span></span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Schmidt, Daniel; Tillberg, Paul W.; Chen, Fei; Boyden, Edward S.</p> <p>2014-01-01</p> <p>Ion channels are among the most important <span class="hlt">proteins</span> in biology, regulating the activity of excitable cells and changing in diseases. Ideally it would be possible to actuate endogenous ion channels, in a temporally precise and reversible manner, and without requiring chemical cofactors. Here we present a modular <span class="hlt">protein</span> architecture for fully genetically encoded, light-modulated control of ligands that modulate ion channels of a targeted cell. Our reagent, which we call a lumitoxin, combines a photoswitch and an ion channel-blocking peptide toxin. Illumination causes the photoswitch to unfold, lowering the toxin's local <span class="hlt">concentration</span> near the cell surface, and enabling the ion channel to function. We explore lumitoxin modularity by showing operation with peptide toxins that target different voltage-dependent K+ channels. The lumitoxin architecture may represent a new kind of modular <span class="hlt">protein</span>-engineering strategy for designing light-activated <span class="hlt">proteins</span>, and thus may enable development of novel tools for modulating cellular physiology.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27136017','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27136017"><span id="translatedtitle">Relationship between residual feed intake and lymphocyte mitochondrial complex <span class="hlt">protein</span> <span class="hlt">concentration</span> and ratio in crossbred steers.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Davis, M P; Brooks, M A; Kerley, M S</p> <p>2016-04-01</p> <p>Rate of oxygen uptake by muscle mitochondria and respiratory chain <span class="hlt">protein</span> <span class="hlt">concentrations</span> differed between high- and low-residual feed intake (RFI) animals. The hypothesis of this research was that complex I (CI), II (CII), and III (CIII) mitochondria <span class="hlt">protein</span> <span class="hlt">concentrations</span> in lymphocyte (blood) mitochondria were related to the RFI phenotype of beef steers. Daily feed intake (ADFI) was individually recorded for 92 Hereford-crossbreed steers over 63 d using GrowSafe individual feed intake system. Predicted ADFI was calculated as the regression of ADFI on ADG and midtest BW. Difference between ADFI and predicted ADFI was RFI. Lymphocytes were isolated from low-RFI (-1.32 ± 0.11 kg/d; = 10) and high-RFI (1.34 ± 0.18 kg/d; = 8) steers. Immunocapture of CI, CII, and CIII <span class="hlt">proteins</span> from the lymphocyte was done using MitoProfile CI, CII, and CIII immunocapture kits (MitoSciences Inc., Eugene, OR). <span class="hlt">Protein</span> <span class="hlt">concentrations</span> of CI, CII, and CIII and total <span class="hlt">protein</span> were quantified using bicinchoninic acid colorimetric procedures. Low-RFI steers consumed 30% less ( = 0.0004) feed and had a 40% improvement ( < 0.0001) in feed efficiency compared with high-RFI steers with similar growth ( = 0.78) and weight measurements ( > 0.65). High- and low-RFI steers did not differ in CI ( = 0.22), CII ( = 0.69), and CIII ( = 0.59) <span class="hlt">protein</span> <span class="hlt">concentrations</span>. The <span class="hlt">protein</span> <span class="hlt">concentration</span> ratios for CI to CII ( = 0.03) were 20% higher and the ratios of CI to CIII ( = 0.01) were 30% higher, but the ratios of CII to CIII ( = 0.89) did not differ when comparing low-RFI steers with high-RFI steers. The similar magnitude difference in feed intake, feed efficiency measurements, and CI-to-CIII ratio between RFI phenotypes provides a plausible explanation for differences between the phenotypes. We also concluded that mitochondria isolated from lymphocytes could be used to study respiratory chain differences among differing RFI phenotypes. Further research is needed to determine if lymphocyte mitochondrial</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/24476471','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/24476471"><span id="translatedtitle">Comparing serum responses to acute feedings of an extensively hydrolyzed whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> versus a native whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> in rats: a metabolomics approach.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Roberts, Michael D; Cruthirds, Clayton L; Lockwood, Christopher M; Pappan, Kirk; Childs, Thomas E; Company, Joseph M; Brown, Jacob D; Toedebusch, Ryan G; Booth, Frank W</p> <p>2014-02-01</p> <p>We examined how gavage feeding extensively hydrolyzed whey <span class="hlt">protein</span> (WPH) versus a native whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) transiently affected serum biochemical profiles in rodents. Male Wistar rats (250-300 g) were 8 h fasted and subsequently fed isonitrogenous amounts of WPH or WPC, or remained unfed (control). Animals were sacrificed 15 min, 30 min, and 60 min post-gavage for serum extraction, and serum was analyzed using untargeted global metabolic profiling via gas chromatography/mass spectrometry (MS) and liquid chromatography/MS/MS platforms. We detected 333 serum metabolites amongst the experimental and control groups. Both WPH and WPC generally increased amino acids (1.2-2.8-fold), branched-chain amino acids (1.2-1.7-fold), and serum di- and oligo-peptides (1.1-2.7-fold) over the 60 min time course compared with control (q < 0.05). However, WPH increased lysine (false discovery rate using a q-value <0.05) and tended to increase isoleucine and valine 15 min post-feeding (q < 0.10) as well as aspartylleucine 30 min post-feeding compared with WPC (q < 0.05). While both <span class="hlt">protein</span> sources led to a dramatic increase in free fatty acids compared with control (up to 6-fold increases, q < 0.05), WPH also uniquely resulted in a 30 min post-feeding elevation in free fatty acids compared with WPC (q < 0.05), an effect which may be due to the robust 30 min postprandial increase in epinephrine in the WPH cohort. These data provide a unique postprandial time-course perspective on how WPH versus WPC feedings affect circulating biochemicals and will guide future research comparing these 2 <span class="hlt">protein</span> sources.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25349364','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25349364"><span id="translatedtitle"><span class="hlt">Concentration</span> of metabolizable energy and digestibility of energy, phosphorus, and amino acids in lemna <span class="hlt">protein</span> <span class="hlt">concentrate</span> fed to growing pigs.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Rojas, O J; Liu, Y; Stein, H H</p> <p>2014-11-01</p> <p>Lemna <span class="hlt">protein</span> <span class="hlt">concentrate</span> (LPC; 68.0% CP) is produced by extracting <span class="hlt">protein</span> from de-oiled and dehydrated biomaterials from plants of the Lemnaceae family and may be used as a <span class="hlt">protein</span> source for animals. There are, however, no published data on the nutritional value of LPC fed to pigs. Three experiments were, therefore, conducted to determine the <span class="hlt">concentration</span> of ME, the standardized total tract digestibility (STTD) of P, and the standardized ileal digestibility (SID) of AA in LPC and to compare these values to values for fish meal and soybean meal (SBM). Experiment 1 was conducted to determine the ME of LPC, fish meal, SBM, and corn. Thirty-two barrows (initial BW: 16.8 ± 2.8 kg) were placed in metabolism cages and allotted to a randomized complete block design with 4 diets and 8 replicate pigs per diet. A corn-based diet and 3 diets that contained corn and LPC, fish meal, or SBM were formulated. Feces and urine were collected for 5 d after a 5-d adaptation period, and all samples were analyzed for GE. Results indicated that the <span class="hlt">concentration</span> of ME was not different among corn, fish meal, and SBM (3,855, 3,904, and 4,184 kcal/kg DM, respectively), but there was a tendency (P = 0.08) for a reduced ME in LPC (3,804 kcal/kg DM) compared with SBM. In Exp. 2, 24 barrows (initial BW: 12.5 ± 2.5 kg) were allotted to a randomized complete block design with 3 diets and 8 replicate pigs per diet and used to determine the STTD of P in LPC, fish meal, and SBM. Three diets that each contained 1 of the 3 test ingredients as the sole source of P were formulated. Pigs were placed in metabolism cages, and feces were collected for 5 d after a 5-d adaptation period. The STTD of P in LPC (72.8%) was not different from the STTD of P in fish meal (65.6%), but tended (P = 0.07) to be greater than in SBM (62.8%). The SID of AA in LPC, SBM, and fish meal was determined in Exp. 3. Eight barrows (initial BW: 21.4 ± 4.0 kg) were equipped with a T-cannula in the distal ileum and randomly</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/23151538','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/23151538"><span id="translatedtitle">In vitro <span class="hlt">protein</span> digestibility and physico-chemical properties of flours and <span class="hlt">protein</span> <span class="hlt">concentrates</span> from two varieties of lentil (Lens culinaris).</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Barbana, Chockry; Boye, Joyce Irene</p> <p>2013-02-01</p> <p>The chemical composition of whole lentil flours and lentil <span class="hlt">protein</span> <span class="hlt">concentrates</span> prepared by alkaline extraction and iso-electric precipitation from Blaze and Laird varieties of lentil were studied. The <span class="hlt">protein</span> composition of the flours and <span class="hlt">concentrates</span>, determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and size-exclusion high-performance liquid chromatography (SE-HPLC) showed that the extracted <span class="hlt">proteins</span> were composed mainly of globulins and albumins. Trypsin inhibitor activity ranged between 0.94 and 1.94 trypsin inhibitor units (TIU) mg(-1) for the flours, but was markedly lower in the <span class="hlt">protein</span> <span class="hlt">concentrates</span> ranging between 0.17 and 0.66 TIU mg(-1). In vitro <span class="hlt">protein</span> digestibility ranged between 75.90 and 77.05% for the flours, whereas significantly (P < 0.05) higher values, ~82.80 to 83.20%, were determined for the <span class="hlt">concentrates</span>. Significant (P < 0.05) differences in colour (ΔE) were observed between the flours and the <span class="hlt">concentrates</span> from both varieties. Thermal properties of both flours as studied by differential scanning calorimetry (DSC) were comparable. However, the endothermic parameters of the two <span class="hlt">protein</span> <span class="hlt">concentrates</span> were significantly (P < 0.05) different. Overall, the results show that in vitro <span class="hlt">protein</span> digestibility of lentil <span class="hlt">protein</span> <span class="hlt">concentrates</span> is higher than that of the flours, however, both lentil flours and <span class="hlt">protein</span> <span class="hlt">concentrates</span> contain useful <span class="hlt">proteins</span> that could serve as value-added ingredients in food formulations.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://ntrs.nasa.gov/search.jsp?R=19930074626&hterms=carbohydrates&qs=Ntx%3Dmode%2Bmatchall%26Ntk%3DAll%26N%3D0%26No%3D10%26Ntt%3Dcarbohydrates','NASA-TRS'); return false;" href="http://ntrs.nasa.gov/search.jsp?R=19930074626&hterms=carbohydrates&qs=Ntx%3Dmode%2Bmatchall%26Ntk%3DAll%26N%3D0%26No%3D10%26Ntt%3Dcarbohydrates"><span id="translatedtitle">Meal composition and plasma amino acid ratios: Effect of various <span class="hlt">proteins</span> or carbohydrates, and of various <span class="hlt">protein</span> <span class="hlt">concentrations</span></span></a></p> <p><a target="_blank" href="http://ntrs.nasa.gov/search.jsp">NASA Technical Reports Server (NTRS)</a></p> <p>Yokogoshi, Hidehiko; Wurtman, Richard J.</p> <p>1986-01-01</p> <p>The effects of meals containing various <span class="hlt">proteins</span> and carbohydrates, and of those containing various proportions of <span class="hlt">protein</span> (0 percent to 20 percent of a meal, by weight) or of carbohydrate (0 percent to 75 percent), on plasma levels of certain large neutral amino acids (LNAA) in rats previously fasted for 19 hours were examined. Also the plasma tryptophan ratios (the ratio of the plasma trytophan <span class="hlt">concentration</span> to the summed <span class="hlt">concentrations</span> of the other large neutral amino acids) and other plasma amino acid ratios were calculated. (The plasma tryptophan ratio has been shown to determine brain tryptophan levels and, thereby, to affect the synthesis and release of the neurotransmitter serotonin). A meal containing 70 percent to 75 percent of an insulin-secreting carbohydrate (dextrose or dextrin) increased plasma insulin levels and the tryptophan ratio; those containing 0 percent or 25 percent carbohydrate failed to do so. Addition of as little as 5 percent casein to a 70 percent carbohydrate meal fully blocked the increase in the plasma tryptophan ratio without affecting the secretion of insulin - probably by contributing much larger quantities of the other LNAA than of tryptophan to the blood. Dietary <span class="hlt">proteins</span> differed in their ability to suppress the carbohydrate-induced rise in the plasma tryptophan ratio. Addition of 10 percent casein, peanut meal, or gelatin fully blocked this increase, but lactalbumin failed to do so, and egg white did so only partially. (Consumption of the 10 percent gelatin meal also produced a major reduction in the plasma tyrosine ratio, and may thereby have affected brain tyrosine levels and catecholamine synthesis.) These observations suggest that serotonin-releasing neurons in brains of fasted rats are capable of distinguishing (by their metabolic effects) between meals poor in <span class="hlt">protein</span> but rich in carbohydrates that elicit insulin secretion, and all other meals. The changes in brain serotonin caused by carbohydrate-rich, <span class="hlt">protein</span></p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/25475399','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/25475399"><span id="translatedtitle">Concomitant Raman spectroscopy and dynamic light scattering for characterization of therapeutic <span class="hlt">proteins</span> at high <span class="hlt">concentrations</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Zhou, Chen; Qi, Wei; Lewis, E Neil; Carpenter, John F</p> <p>2015-03-01</p> <p>A Raman spectrometer and dynamic light scattering system were combined in a single platform (Raman-DLS) to provide concomitant higher order structural and hydrodynamic size data for therapeutic <span class="hlt">proteins</span> at high <span class="hlt">concentration</span>. As model therapeutic <span class="hlt">proteins</span>, we studied human serum albumin (HSA) and intravenous immunoglobulin (IVIG). HSA <span class="hlt">concentration</span> and temperature interval during heating did not affect the onset temperatures for conformation perturbation or aggregation. The impact of pH on thermal stability of HSA was tested at pHs 3, 5, and 8. Stability was the greatest at pH 8, but distinct unfolding and aggregation behaviors were observed at the different pHs. HSA structural transitions and aggregation kinetics were also studied in real time during isothermal incubations at pH 7. In a forced oxidation study, it was found that hydrogen peroxide (H2O2) treatment reduced the thermal stability of HSA. Finally, the structure and thermal stability of IVIG were studied, and a comprehensive characterization of heating-induced structural perturbations and aggregation was obtained. In conclusion, by providing comprehensive data on <span class="hlt">protein</span> tertiary and secondary structures and hydrodynamic size during real-time heating or isothermal incubation experiments, the Raman-DLS system offers unique physical insights into the properties of high-<span class="hlt">concentration</span> <span class="hlt">protein</span> samples. PMID:25475399</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/11722895','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/11722895"><span id="translatedtitle"><span class="hlt">Proteins</span> induced during adaptation of Acetobacter aceti to high acetate <span class="hlt">concentrations</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Steiner, P; Sauer, U</p> <p>2001-12-01</p> <p>As a typical product of microbial metabolism, the weak acid acetate is well known for its cytotoxic effects. In contrast to most other microbes, the so-called acetic acid bacteria can acquire significant resistance to high acetate <span class="hlt">concentrations</span> when properly adapted to such hostile conditions. To characterize the molecular events that are associated with this adaptation, we analyzed global <span class="hlt">protein</span> expression levels during adaptation of Acetobacter aceti by two-dimensional gel electrophoresis. Adaptation was achieved by using serial batch and continuous cultivations with increasing acetate supplementation. Computer-aided analysis revealed a complex proteome response with at least 50 <span class="hlt">proteins</span> that are specifically induced by adaptation to acetate but not by other stress conditions, such as heat or oxidative or osmotic stress. Of these <span class="hlt">proteins</span>, 19 were significantly induced in serial batch and continuous cultures and were thus noted as acetate adaptation <span class="hlt">proteins</span> (Aaps). Here we present first microsequence information on such Aaps from A. aceti. Membrane-associated processes appear to be of major importance for adaptation, because some of the Aap bear N-terminal sequence homology to membrane <span class="hlt">proteins</span> and 11 of about 40 resolved <span class="hlt">proteins</span> from membrane <span class="hlt">protein</span>-enriched fractions are significantly induced.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=93332','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=93332"><span id="translatedtitle"><span class="hlt">Proteins</span> Induced during Adaptation of Acetobacter aceti to High Acetate <span class="hlt">Concentrations</span></span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Steiner, Peter; Sauer, Uwe</p> <p>2001-01-01</p> <p>As a typical product of microbial metabolism, the weak acid acetate is well known for its cytotoxic effects. In contrast to most other microbes, the so-called acetic acid bacteria can acquire significant resistance to high acetate <span class="hlt">concentrations</span> when properly adapted to such hostile conditions. To characterize the molecular events that are associated with this adaptation, we analyzed global <span class="hlt">protein</span> expression levels during adaptation of Acetobacter aceti by two-dimensional gel electrophoresis. Adaptation was achieved by using serial batch and continuous cultivations with increasing acetate supplementation. Computer-aided analysis revealed a complex proteome response with at least 50 <span class="hlt">proteins</span> that are specifically induced by adaptation to acetate but not by other stress conditions, such as heat or oxidative or osmotic stress. Of these <span class="hlt">proteins</span>, 19 were significantly induced in serial batch and continuous cultures and were thus noted as acetate adaptation <span class="hlt">proteins</span> (Aaps). Here we present first microsequence information on such Aaps from A. aceti. Membrane-associated processes appear to be of major importance for adaptation, because some of the Aap bear N-terminal sequence homology to membrane <span class="hlt">proteins</span> and 11 of about 40 resolved <span class="hlt">proteins</span> from membrane <span class="hlt">protein</span>-enriched fractions are significantly induced. PMID:11722895</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://ntrs.nasa.gov/search.jsp?R=20040112533&hterms=infarction&qs=Ntx%3Dmode%2Bmatchall%26Ntk%3DAll%26N%3D0%26No%3D30%26Ntt%3Dinfarction','NASA-TRS'); return false;" href="http://ntrs.nasa.gov/search.jsp?R=20040112533&hterms=infarction&qs=Ntx%3Dmode%2Bmatchall%26Ntk%3DAll%26N%3D0%26No%3D30%26Ntt%3Dinfarction"><span id="translatedtitle">Absence of diurnal variation of C-reactive <span class="hlt">protein</span> <span class="hlt">concentrations</span> in healthy human subjects</span></a></p> <p><a target="_blank" href="http://ntrs.nasa.gov/search.jsp">NASA Technical Reports Server (NTRS)</a></p> <p>Meier-Ewert, H. K.; Ridker, P. M.; Rifai, N.; Price, N.; Dinges, D. F.; Mullington, J. M.</p> <p>2001-01-01</p> <p>BACKGROUND: The <span class="hlt">concentration</span> of C-reactive <span class="hlt">protein</span> (CRP) in otherwise healthy subjects has been shown to predict future risk of myocardial infarction and stroke. CRP is synthesized by the liver in response to interleukin-6, the serum <span class="hlt">concentration</span> of which is subject to diurnal variation. METHODS: To examine the existence of a time-of-day effect for baseline CRP values, we determined CRP <span class="hlt">concentrations</span> in hourly blood samples drawn from healthy subjects (10 males, 3 females; age range, 21-35 years) during a baseline day in a controlled environment (8 h of nighttime sleep). RESULTS: Overall CRP <span class="hlt">concentrations</span> were low, with only three subjects having CRP <span class="hlt">concentrations</span> >2 mg/L. Comparison of raw data showed stability of CRP <span class="hlt">concentrations</span> throughout the 24 h studied. When compared with cutoff values of CRP quintile derived from population-based studies, misclassification of greater than one quintile did not occur as a result of diurnal variation in any of the subjects studied. Nonparametric ANOVA comparing different time points showed no significant differences for both raw and z-transformed data. Analysis for rhythmic diurnal variation using a method fitting a cosine curve to the group data was negative. CONCLUSIONS: Our data show that baseline CRP <span class="hlt">concentrations</span> are not subject to time-of-day variation and thus help to explain why CRP <span class="hlt">concentrations</span> are a better predictor of vascular risk than interleukin-6. Determination of CRP for cardiovascular risk prediction may be performed without concern for diurnal variation.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/8002703','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/8002703"><span id="translatedtitle">[Development of a feeding formula from a <span class="hlt">protein</span> <span class="hlt">concentrate</span> of chick-pea (Cicer arietinum)].</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Ulloa, J A; Valencia, M E</p> <p>1993-03-01</p> <p>A medical formula was developed from a chick-pea (Cicer arietinum) <span class="hlt">protein</span> <span class="hlt">concentrate</span> obtained by ultrafiltration (67.8% of <span class="hlt">protein</span>). Additionally sucrose, methionine, milk flavor, and mixtures of corn and coconut oils, vitamins and minerals were used, to perform FAO/WHO standards. All ingredients were blended in water to 50 degrees C, and the mixture was spray-dried with a Spray-drier using inlet and outlet air temperatures of 170 and 90 degrees C respectively. The nutritive value of the formula was evaluated with the Net <span class="hlt">Protein</span> Ratio (NPR), Nitrogen Utilization (NU) and both relatives values to casein ANRC (R-NPR and R-NU). The proximal analysis of the infant formula was: <span class="hlt">protein</span> 16.0% (with 4.9 g/16 g N of reactive lysine), fat 25.8%, moisture 4.0%, ash 3.2% and carbohydrates 51.0%. The values of NPR, R-NPR, NU and R-NU were 3.95, 83.6, 3.55 and 82.5 respectively. This results shown the chick-pea <span class="hlt">protein</span> <span class="hlt">concentrate</span>, potencially utilizable as an ingredient in the formulas for medical purposes. PMID:8002703</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=5037556','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=5037556"><span id="translatedtitle">Calorie Restricted High <span class="hlt">Protein</span> Diets Downregulate Lipogenesis and Lower Intrahepatic Triglyceride <span class="hlt">Concentrations</span> in Male Rats</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Margolis, Lee M.; Rivas, Donato A.; Ezzyat, Yassine; Gaffney-Stomberg, Erin; Young, Andrew J.; McClung, James P.; Fielding, Roger A.; Pasiakos, Stefan M.</p> <p>2016-01-01</p> <p>The purpose of this investigation was to assess the influence of calorie restriction (CR) alone, higher-<span class="hlt">protein</span>/lower-carbohydrate intake alone, and combined CR higher-<span class="hlt">protein</span>/lower-carbohydrate intake on glucose homeostasis, hepatic de novo lipogenesis (DNL), and intrahepatic triglycerides. Twelve-week old male Sprague Dawley rats consumed ad libitum (AL) or CR (40% restriction), adequate (10%), or high (32%) <span class="hlt">protein</span> (PRO) milk-based diets for 16 weeks. Metabolic profiles were assessed in serum, and intrahepatic triglyceride <span class="hlt">concentrations</span> and molecular markers of de novo lipogenesis were determined in liver. Independent of calorie intake, 32% PRO tended to result in lower homeostatic model assessment of insulin resistance (HOMA-IR) values compared to 10% PRO, while insulin and homeostatic model assessment of β-cell function (HOMA-β) values were lower in CR than AL, regardless of <span class="hlt">protein</span> intake. Intrahepatic triglyceride <span class="hlt">concentrations</span> were 27.4 ± 4.5 and 11.7 ± 4.5 µmol·g−1 lower (p < 0.05) in CR and 32% PRO compared to AL and 10% PRO, respectively. Gene expression of fatty acid synthase (FASN), stearoyl-CoA destaurase-1 (SCD1) and pyruvate dehydrogenase kinase, isozyme 4 (PDK4) were 45% ± 1%, 23% ± 1%, and 57% ± 1% lower (p < 0.05), respectively, in CR than AL, regardless of <span class="hlt">protein</span> intake. Total <span class="hlt">protein</span> of FASN and SCD were 50% ± 1% and 26% ± 1% lower (p < 0.05) in 32% PRO compared to 10% PRO, independent of calorie intake. Results from this investigation provide evidence that the metabolic health benefits associated with CR—specifically reduction in intrahepatic triglyceride content—may be enhanced by consuming a higher-<span class="hlt">protein</span>/lower-carbohydrate diet. PMID:27649241</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27649241','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27649241"><span id="translatedtitle">Calorie Restricted High <span class="hlt">Protein</span> Diets Downregulate Lipogenesis and Lower Intrahepatic Triglyceride <span class="hlt">Concentrations</span> in Male Rats.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Margolis, Lee M; Rivas, Donato A; Ezzyat, Yassine; Gaffney-Stomberg, Erin; Young, Andrew J; McClung, James P; Fielding, Roger A; Pasiakos, Stefan M</p> <p>2016-01-01</p> <p>The purpose of this investigation was to assess the influence of calorie restriction (CR) alone, higher-<span class="hlt">protein</span>/lower-carbohydrate intake alone, and combined CR higher-<span class="hlt">protein</span>/lower-carbohydrate intake on glucose homeostasis, hepatic de novo lipogenesis (DNL), and intrahepatic triglycerides. Twelve-week old male Sprague Dawley rats consumed ad libitum (AL) or CR (40% restriction), adequate (10%), or high (32%) <span class="hlt">protein</span> (PRO) milk-based diets for 16 weeks. Metabolic profiles were assessed in serum, and intrahepatic triglyceride <span class="hlt">concentrations</span> and molecular markers of de novo lipogenesis were determined in liver. Independent of calorie intake, 32% PRO tended to result in lower homeostatic model assessment of insulin resistance (HOMA-IR) values compared to 10% PRO, while insulin and homeostatic model assessment of β-cell function (HOMA-β) values were lower in CR than AL, regardless of <span class="hlt">protein</span> intake. Intrahepatic triglyceride <span class="hlt">concentrations</span> were 27.4 ± 4.5 and 11.7 ± 4.5 µmol·g(-1) lower (p < 0.05) in CR and 32% PRO compared to AL and 10% PRO, respectively. Gene expression of fatty acid synthase (FASN), stearoyl-CoA destaurase-1 (SCD1) and pyruvate dehydrogenase kinase, isozyme 4 (PDK4) were 45% ± 1%, 23% ± 1%, and 57% ± 1% lower (p < 0.05), respectively, in CR than AL, regardless of <span class="hlt">protein</span> intake. Total <span class="hlt">protein</span> of FASN and SCD were 50% ± 1% and 26% ± 1% lower (p < 0.05) in 32% PRO compared to 10% PRO, independent of calorie intake. Results from this investigation provide evidence that the metabolic health benefits associated with CR-specifically reduction in intrahepatic triglyceride content-may be enhanced by consuming a higher-<span class="hlt">protein</span>/lower-carbohydrate diet. PMID:27649241</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27649241','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27649241"><span id="translatedtitle">Calorie Restricted High <span class="hlt">Protein</span> Diets Downregulate Lipogenesis and Lower Intrahepatic Triglyceride <span class="hlt">Concentrations</span> in Male Rats.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Margolis, Lee M; Rivas, Donato A; Ezzyat, Yassine; Gaffney-Stomberg, Erin; Young, Andrew J; McClung, James P; Fielding, Roger A; Pasiakos, Stefan M</p> <p>2016-09-15</p> <p>The purpose of this investigation was to assess the influence of calorie restriction (CR) alone, higher-<span class="hlt">protein</span>/lower-carbohydrate intake alone, and combined CR higher-<span class="hlt">protein</span>/lower-carbohydrate intake on glucose homeostasis, hepatic de novo lipogenesis (DNL), and intrahepatic triglycerides. Twelve-week old male Sprague Dawley rats consumed ad libitum (AL) or CR (40% restriction), adequate (10%), or high (32%) <span class="hlt">protein</span> (PRO) milk-based diets for 16 weeks. Metabolic profiles were assessed in serum, and intrahepatic triglyceride <span class="hlt">concentrations</span> and molecular markers of de novo lipogenesis were determined in liver. Independent of calorie intake, 32% PRO tended to result in lower homeostatic model assessment of insulin resistance (HOMA-IR) values compared to 10% PRO, while insulin and homeostatic model assessment of β-cell function (HOMA-β) values were lower in CR than AL, regardless of <span class="hlt">protein</span> intake. Intrahepatic triglyceride <span class="hlt">concentrations</span> were 27.4 ± 4.5 and 11.7 ± 4.5 µmol·g(-1) lower (p < 0.05) in CR and 32% PRO compared to AL and 10% PRO, respectively. Gene expression of fatty acid synthase (FASN), stearoyl-CoA destaurase-1 (SCD1) and pyruvate dehydrogenase kinase, isozyme 4 (PDK4) were 45% ± 1%, 23% ± 1%, and 57% ± 1% lower (p < 0.05), respectively, in CR than AL, regardless of <span class="hlt">protein</span> intake. Total <span class="hlt">protein</span> of FASN and SCD were 50% ± 1% and 26% ± 1% lower (p < 0.05) in 32% PRO compared to 10% PRO, independent of calorie intake. Results from this investigation provide evidence that the metabolic health benefits associated with CR-specifically reduction in intrahepatic triglyceride content-may be enhanced by consuming a higher-<span class="hlt">protein</span>/lower-carbohydrate diet.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/24072788','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/24072788"><span id="translatedtitle">Effect of <span class="hlt">protein</span> and glycerol <span class="hlt">concentration</span> on the mechanical, optical, and water vapor barrier properties of canola <span class="hlt">protein</span> isolate-based edible films.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Chang, Chang; Nickerson, Michael T</p> <p>2015-01-01</p> <p>Biodegradable edible films prepared using <span class="hlt">proteins</span> are both economically and environmentally important to the food packaging industry relative to traditional petroleum-derived synthetic materials. In the present study, the mechanical and water vapor barrier properties of casted canola <span class="hlt">protein</span> isolate edible films were investigated as a function of <span class="hlt">protein</span> (5.0% and 7.5%) and glycerol (30%, 35%, 40%, 45%, and 50%) content. Specifically, tensile strength and elongation, elastic modulus, puncture strength and deformation, opacity, and water vapor permeability were measured. Results indicated that tensile strength, puncture strength, and elastic modulus decreased, while tensile elongation and puncture deformation values increased as glycerol <span class="hlt">concentration</span> increased for both 5.0% and 7.5% canola <span class="hlt">protein</span> isolate films. Furthermore, tensile strength, puncture strength, and elastic modulus values were found to increase at higher <span class="hlt">protein</span> <span class="hlt">concentrations</span> within the canola <span class="hlt">protein</span> isolate films, whereas puncture deformation values decreased. Tensile elongation was found to be similar for both canola <span class="hlt">protein</span> isolate <span class="hlt">protein</span> levels. Canola <span class="hlt">protein</span> isolate films became more transparent with increasing of glycerol <span class="hlt">concentration</span> and decreasing of canola <span class="hlt">protein</span> isolate <span class="hlt">concentration</span>. Water vapor permeability value was also found to increase with increasing glycerol and <span class="hlt">protein</span> contents. Overall, results indicated that canola <span class="hlt">protein</span> isolate films were less brittle, more malleable and transparent, and had greater water vapor permeability at higher glycerol levels. However, as <span class="hlt">protein</span> level increased, canola <span class="hlt">protein</span> isolate films were more brittle, less malleable and more opaque, and also had increased water vapor permeability.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/24072788','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/24072788"><span id="translatedtitle">Effect of <span class="hlt">protein</span> and glycerol <span class="hlt">concentration</span> on the mechanical, optical, and water vapor barrier properties of canola <span class="hlt">protein</span> isolate-based edible films.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Chang, Chang; Nickerson, Michael T</p> <p>2015-01-01</p> <p>Biodegradable edible films prepared using <span class="hlt">proteins</span> are both economically and environmentally important to the food packaging industry relative to traditional petroleum-derived synthetic materials. In the present study, the mechanical and water vapor barrier properties of casted canola <span class="hlt">protein</span> isolate edible films were investigated as a function of <span class="hlt">protein</span> (5.0% and 7.5%) and glycerol (30%, 35%, 40%, 45%, and 50%) content. Specifically, tensile strength and elongation, elastic modulus, puncture strength and deformation, opacity, and water vapor permeability were measured. Results indicated that tensile strength, puncture strength, and elastic modulus decreased, while tensile elongation and puncture deformation values increased as glycerol <span class="hlt">concentration</span> increased for both 5.0% and 7.5% canola <span class="hlt">protein</span> isolate films. Furthermore, tensile strength, puncture strength, and elastic modulus values were found to increase at higher <span class="hlt">protein</span> <span class="hlt">concentrations</span> within the canola <span class="hlt">protein</span> isolate films, whereas puncture deformation values decreased. Tensile elongation was found to be similar for both canola <span class="hlt">protein</span> isolate <span class="hlt">protein</span> levels. Canola <span class="hlt">protein</span> isolate films became more transparent with increasing of glycerol <span class="hlt">concentration</span> and decreasing of canola <span class="hlt">protein</span> isolate <span class="hlt">concentration</span>. Water vapor permeability value was also found to increase with increasing glycerol and <span class="hlt">protein</span> contents. Overall, results indicated that canola <span class="hlt">protein</span> isolate films were less brittle, more malleable and transparent, and had greater water vapor permeability at higher glycerol levels. However, as <span class="hlt">protein</span> level increased, canola <span class="hlt">protein</span> isolate films were more brittle, less malleable and more opaque, and also had increased water vapor permeability. PMID:24072788</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/servlets/purl/921934','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/servlets/purl/921934"><span id="translatedtitle"><span class="hlt">ABSOLUTE</span> POLARIMETRY AT RHIC.</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>OKADA; BRAVAR, A.; BUNCE, G.; GILL, R.; HUANG, H.; MAKDISI, Y.; NASS, A.; WOOD, J.; ZELENSKI, Z.; ET AL.</p> <p>2007-09-10</p> <p>Precise and <span class="hlt">absolute</span> beam polarization measurements are critical for the RHIC spin physics program. Because all experimental spin-dependent results are normalized by beam polarization, the normalization uncertainty contributes directly to final physics uncertainties. We aimed to perform the beam polarization measurement to an accuracy Of {Delta}P{sub beam}/P{sub beam} < 5%. The <span class="hlt">absolute</span> polarimeter consists of Polarized Atomic Hydrogen Gas Jet Target and left-right pairs of silicon strip detectors and was installed in the RHIC-ring in 2004. This system features proton-proton elastic scattering in the Coulomb nuclear interference (CNI) region. Precise measurements of the analyzing power A{sub N} of this process has allowed us to achieve {Delta}P{sub beam}/P{sub beam} = 4.2% in 2005 for the first long spin-physics run. In this report, we describe the entire set up and performance of the system. The procedure of beam polarization measurement and analysis results from 2004-2005 are described. Physics topics of AN in the CNI region (four-momentum transfer squared 0.001 < -t < 0.032 (GeV/c){sup 2}) are also discussed. We point out the current issues and expected optimum accuracy in 2006 and the future.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26243665','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26243665"><span id="translatedtitle">Jatropha curcas <span class="hlt">Protein</span> <span class="hlt">Concentrate</span> Stimulates Insulin Signaling, Lipogenesis, <span class="hlt">Protein</span> Synthesis and the PKCα Pathway in Rat Liver.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>León-López, Liliana; Márquez-Mota, Claudia C; Velázquez-Villegas, Laura A; Gálvez-Mariscal, Amanda; Arrieta-Báez, Daniel; Dávila-Ortiz, Gloria; Tovar, Armando R; Torres, Nimbe</p> <p>2015-09-01</p> <p>Jatropha curcas is an oil seed plant that belongs to the Euphorbiaceae family. Nontoxic genotypes have been reported in Mexico. The purpose of the present work was to evaluate the effect of a Mexican variety of J. curcas <span class="hlt">protein</span> <span class="hlt">concentrate</span> (JCP) on weight gain, biochemical parameters, and the expression of genes and <span class="hlt">proteins</span> involved in insulin signaling, lipogenesis, cholesterol and <span class="hlt">protein</span> synthesis in rats. The results demonstrated that short-term consumption of JCP increased serum glucose, insulin, triglycerides and cholesterol levels as well as the expression of transcription factors involved in lipogenesis and cholesterol synthesis (SREBP-1 and LXRα). Moreover, there was an increase in insulin signaling mediated by Akt phosphorylation and mTOR. JCP also increased PKCα <span class="hlt">protein</span> abundance and the activation of downstream signaling pathway targets such as the AP1 and NF-κB transcription factors typically activated by phorbol esters. These results suggested that phorbol esters are present in JCP, and that they could be involved in the activation of PKC which may be responsible for the high insulin secretion and consequently the activation of insulin-dependent pathways. Our data suggest that this Mexican Jatropha variety contains toxic compounds that produce negative metabolic effects which require caution when using in the applications of Jatropha-based products in medicine and nutrition. PMID:26243665</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_10");'>10</a></li> <li><a href="#" onclick='return showDiv("page_11");'>11</a></li> <li class="active"><span>12</span></li> <li><a href="#" onclick='return showDiv("page_13");'>13</a></li> <li><a href="#" onclick='return showDiv("page_14");'>14</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_12 --> <div id="page_13" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_11");'>11</a></li> <li><a href="#" onclick='return showDiv("page_12");'>12</a></li> <li class="active"><span>13</span></li> <li><a href="#" onclick='return showDiv("page_14");'>14</a></li> <li><a href="#" onclick='return showDiv("page_15");'>15</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="241"> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26243665','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26243665"><span id="translatedtitle">Jatropha curcas <span class="hlt">Protein</span> <span class="hlt">Concentrate</span> Stimulates Insulin Signaling, Lipogenesis, <span class="hlt">Protein</span> Synthesis and the PKCα Pathway in Rat Liver.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>León-López, Liliana; Márquez-Mota, Claudia C; Velázquez-Villegas, Laura A; Gálvez-Mariscal, Amanda; Arrieta-Báez, Daniel; Dávila-Ortiz, Gloria; Tovar, Armando R; Torres, Nimbe</p> <p>2015-09-01</p> <p>Jatropha curcas is an oil seed plant that belongs to the Euphorbiaceae family. Nontoxic genotypes have been reported in Mexico. The purpose of the present work was to evaluate the effect of a Mexican variety of J. curcas <span class="hlt">protein</span> <span class="hlt">concentrate</span> (JCP) on weight gain, biochemical parameters, and the expression of genes and <span class="hlt">proteins</span> involved in insulin signaling, lipogenesis, cholesterol and <span class="hlt">protein</span> synthesis in rats. The results demonstrated that short-term consumption of JCP increased serum glucose, insulin, triglycerides and cholesterol levels as well as the expression of transcription factors involved in lipogenesis and cholesterol synthesis (SREBP-1 and LXRα). Moreover, there was an increase in insulin signaling mediated by Akt phosphorylation and mTOR. JCP also increased PKCα <span class="hlt">protein</span> abundance and the activation of downstream signaling pathway targets such as the AP1 and NF-κB transcription factors typically activated by phorbol esters. These results suggested that phorbol esters are present in JCP, and that they could be involved in the activation of PKC which may be responsible for the high insulin secretion and consequently the activation of insulin-dependent pathways. Our data suggest that this Mexican Jatropha variety contains toxic compounds that produce negative metabolic effects which require caution when using in the applications of Jatropha-based products in medicine and nutrition.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3317419','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3317419"><span id="translatedtitle">Myofibroblast Differentiation Modulates Keratocyte Crystallin <span class="hlt">Protein</span> Expression, <span class="hlt">Concentration</span>, and Cellular Light Scattering</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Brown, Donald; Pappa, Aglaia; Vasiliou, Vasilis</p> <p>2012-01-01</p> <p>Purpose. The purpose of this study was to determine whether myofibroblast differentiation altered keratocyte crystallin <span class="hlt">protein</span> <span class="hlt">concentration</span> and increased cellular light scattering. Methods. Serum-free cultured rabbit corneal keratocytes and TGFβ (5 ng/mL) induced myofibroblasts were harvested and counted and <span class="hlt">protein</span>/RNA extracted. Expression of myofibroblast and keratocyte markers was determined by real-time PCR and Western blot analysis. The cell volume of calcein AM–loaded keratocytes and myofibroblasts was determined by using nonlinear optical microscopy. Cellular light scattering of transformed myofibroblasts expressing human keratocyte crystallins was measured by reflectance confocal microscopy. Results. Differentiated myofibroblasts showed a significant decrease in RNA levels for the keratocyte markers ALDH1A1, lumican, and keratocan and a significant increase in the myofibroblast marker α-smooth muscle actin. Volumetric and <span class="hlt">protein</span> measurements showed that myofibroblast differentiation significantly increased cytoplasmic volume (293%; P < 0.001) and water-soluble and -insoluble <span class="hlt">protein</span> content per cell (respectively, 442% and 431%; P < 0.002) compared to keratocytes. Western blot analysis showed that the level of ALDH1A1 <span class="hlt">protein</span> per cell was similar between myofibroblasts and keratocytes, but was substantially reduced as a percentage of total water-soluble <span class="hlt">protein</span>. Light scattering measurements showed that induced expression of corneal crystallins significantly decreased light scattering. Conclusions. These data suggest that myofibroblast differentiation leads to a marked increase in cell volume and dilution of corneal crystallins associated with an increase in cellular light scattering. PMID:22247459</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25712620','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25712620"><span id="translatedtitle">Dosimetry determines the initial OH radical <span class="hlt">concentration</span> in fast photochemical oxidation of <span class="hlt">proteins</span> (FPOP).</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Niu, Ben; Zhang, Hao; Giblin, Daryl; Rempel, Don L; Gross, Michael L</p> <p>2015-05-01</p> <p>Fast photochemical oxidation of <span class="hlt">proteins</span> (FPOP) employs laser photolysis of hydrogen peroxide to give OH radicals that label amino acid side-chains of <span class="hlt">proteins</span> on the microsecond time scale. A method for quantitation of hydroxyl radicals after laser photolysis is of importance to FPOP because it establishes a means to adjust the yield of •OH, offers the opportunity of tunable modifications, and provides a basis for kinetic measurements. The initial <span class="hlt">concentration</span> of OH radicals has yet to be measured experimentally. We report here an approach using isotope dilution gas chromatography/mass spectrometry (GC/MS) to determine quantitatively the initial •OH <span class="hlt">concentration</span> (we found ~0.95 mM from 15 mM H2O2) from laser photolysis and to investigate the quenching efficiencies for various •OH scavengers.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/19897911','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/19897911"><span id="translatedtitle">Effects of salt <span class="hlt">concentration</span> on the reaction rate of Glc with amino acids, peptides, and <span class="hlt">proteins</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Yamaguchi, Keiko; Noumi, Yuri; Nakajima, Katsumi; Nagatsuka, Chiharu; Aizawa, Haruko; Nakawaki, Rie; Mizude, Eri; Otsuka, Yuzuru; Homma, Takeshi; Chuyen, Nguyen Van</p> <p>2009-11-01</p> <p>The reaction between the amino group and the carbonyl group is important in food quality control. Furthermore, advanced glycation end products from foods are considered to relate to aging and diabetes. Thus, it is important to control this reaction. In this study, we investigated the effects of salt <span class="hlt">concentration</span> on the rates of browning reaction of amino acid, peptides, and <span class="hlt">proteins</span>. A high <span class="hlt">concentration</span> of sodium chloride retarded the reaction rate of Glc with amino acids as measured with the absorbance at 470 nm, but did not change the browning rate of Glc with peptides. On the other hand, sodium chloride retarded the browning reaction rate of <span class="hlt">proteins</span> as measured with polymerization degree or by the loss of Lys. It is hoped that the results of this study will be applied in the control of amino-carbonyl reaction rates in the food industry. PMID:19897911</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26452893','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26452893"><span id="translatedtitle">Calibration-free <span class="hlt">concentration</span> analysis of <span class="hlt">protein</span> biomarkers in human serum using surface plasmon resonance.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Grover Shah, Veenita; Ray, Sandipan; Karlsson, Robert; Srivastava, Sanjeeva</p> <p>2015-11-01</p> <p>In complex biological samples such as serum, determination of specific and active <span class="hlt">concentration</span> of target <span class="hlt">proteins</span>, independent of a calibration curve, will be valuable in many applications. Calibration-free <span class="hlt">concentration</span> analysis (CFCA) is a surface plasmon resonance (SPR)-based label-free approach, which calculates active <span class="hlt">concentration</span> of <span class="hlt">proteins</span> using their known diffusion coefficient and observed changes in binding rates at different flow rates under diffusion-limited conditions. Here, for the first time we demonstrate the application of CFCA for determining <span class="hlt">protein</span> biomarker abundance, specifically serum amyloid A (SAA), directly in the serum samples of patients suffering from different infectious and non-infectious diseases. The assay involves preparation of appropriate reaction surfaces by immobilizing antibodies on CM5 chips via amine coupling followed by serum sample preparation and injection over activated and reference surfaces at flow-rates of 5 and 100 μL/min. The system was validated in healthy and diseased (infectious and non-infectious) serum samples by quantifying two different <span class="hlt">proteins</span>: β2-microglobulin (β2M) and SAA. All <span class="hlt">concentration</span> assays were performed for nearly 100 serum samples, which showed reliable quantification in unattended runs with high accuracy and sensitivity. The method could detect the serum β2M to as low as 13 ng/mL in 1000-fold serum dilution, indicating the possible utility of this approach to detect low abundance <span class="hlt">protein</span> biomarkers in body fluids. Applying the CFCA approach, significant difference in serum abundance of SAA was identified in diseased subjects as compared to the healthy controls, which correlated well with our previous proteomic investigations. Estimation of SAA <span class="hlt">concentration</span> for a subset of healthy and diseased sera was also performed using ELISA, and the trend was observed to be similar in both SPR assay and ELISA. The reproducibility of CFCA in various serum samples made the interpretation of assay</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/17293018','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/17293018"><span id="translatedtitle">The safety of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> derived from the milk of cows immunized against Clostridium difficile.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Young, Karen W H; Munro, Ian C; Taylor, Steve L; Veldkamp, Peter; van Dissel, Jaap T</p> <p>2007-04-01</p> <p>A whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> prepared from the milk of cows that have been immunized against Clostridium difficile (C. difficile) and its toxins, toxin A and toxin B, is produced for use as a medical food for the dietary management of patients with C. difficile-associated diarrhea (CDAD) to prevent a relapse of the infection. The safety of anti-C. difficile whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (anti-CD WPC) is supported by analytical data comparing the composition of raw milk from immunized cows versus that from non-immunized cows, and the composition of anti-CD WPC versus that of regular whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>. Additionally, a prospective clinical study was conducted in 77 patients with CDAD to demonstrate the safety of consuming anti-CD WPC to prevent relapse of the infection. This study, which included adverse event monitoring, physical examinations, and extensive hematological and biochemical assessments, showed that anti-CD WPC is safe to consume by patients with CDAD. The available analytical and clinical evidence demonstrate that anti-CD WPC is safe for use by individuals with CDAD, under the described conditions of use.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4363168','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4363168"><span id="translatedtitle">VEGF mRNA and <span class="hlt">Protein</span> <span class="hlt">Concentrations</span> in the Developing Human Eye</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Ma, Irene T.; McConaghy, Suzanne; Namachivayam, Kopperuncholan; Halloran, Brian A.; Kurundkar, Ashish R.; MohanKumar, Krishnan; Maheshwari, Akhil; Ohls, Robin K.</p> <p>2014-01-01</p> <p>Background Vascular endothelial growth factor (VEGF), a well-characterized regulator of angiogenesis, has been mechanistically implicated in retinal neovascularization and in the pathogenesis of ROP. However, the ontogeny of VEGF expression in the human fetal retina is not well known. Because retinal vasculature grows with gestational maturation, we hypothesized that VEGF expression also increases in the midgestation human fetal eye as a function of gestational age. Methods To identify changes in VEGF gene expression during normal human development, we measured VEGF mRNA by quantitative PCR and measured VEGF <span class="hlt">protein</span> by ELISA and western blots in 10-24 week gestation fetal vitreous, retina, and serum. Results VEGF mRNA expression in the retina increased with gestational age. VEGF isoform A, particularly its VEGF121 splice variant, contributed to this positive correlation. Consistent with these findings, we detected increasing VEGF121 <span class="hlt">protein</span> <span class="hlt">concentrations</span> in vitreous humor from fetuses of 10-24 weeks gestation, while VEGF <span class="hlt">concentrations</span> decreased in fetal serum. Conclusions VEGF121 mRNA and <span class="hlt">protein</span> <span class="hlt">concentrations</span> increase with increasing gestational age in the developing human retina. We speculate that VEGF plays an important role in normal retinal vascular development, and that preterm delivery affects production of this vascular growth factor. PMID:25588190</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26778305','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26778305"><span id="translatedtitle">Physical and chemical changes in whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> stored at elevated temperature and humidity.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Tunick, Michael H; Thomas-Gahring, Audrey; Van Hekken, Diane L; Iandola, Susan K; Singh, Mukti; Qi, Phoebe X; Ukuku, Dike O; Mukhopadhyay, Sudarsan; Onwulata, Charles I; Tomasula, Peggy M</p> <p>2016-03-01</p> <p>In a case study, we monitored the physical properties of 2 batches of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) under adverse storage conditions to provide information on shelf life in hot, humid areas. Whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> with 34.9 g of <span class="hlt">protein</span>/100g (WPC34) and 76.8 g of <span class="hlt">protein</span>/100g (WPC80) were stored for up to 18 mo under ambient conditions and at elevated temperature and relative humidity. The samples became yellower with storage; those stored at 35 °C were removed from the study by 12 mo because of their unsatisfactory appearance. Decreases in lysine and increases in water activity, volatile compound formation, and powder caking values were observed in many specimens. Levels of aerobic mesophilic bacteria, coliforms, yeast, and mold were <3.85 log10 cfu/g in all samples. Relative humidity was not a factor in most samples. When stored in sealed bags, these samples of WPC34 and WPC80 had a shelf life of 9 mo at 35 °C but at least 18 mo at lower temperatures, which should extend the market for these products.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26778305','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26778305"><span id="translatedtitle">Physical and chemical changes in whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> stored at elevated temperature and humidity.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Tunick, Michael H; Thomas-Gahring, Audrey; Van Hekken, Diane L; Iandola, Susan K; Singh, Mukti; Qi, Phoebe X; Ukuku, Dike O; Mukhopadhyay, Sudarsan; Onwulata, Charles I; Tomasula, Peggy M</p> <p>2016-03-01</p> <p>In a case study, we monitored the physical properties of 2 batches of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) under adverse storage conditions to provide information on shelf life in hot, humid areas. Whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> with 34.9 g of <span class="hlt">protein</span>/100g (WPC34) and 76.8 g of <span class="hlt">protein</span>/100g (WPC80) were stored for up to 18 mo under ambient conditions and at elevated temperature and relative humidity. The samples became yellower with storage; those stored at 35 °C were removed from the study by 12 mo because of their unsatisfactory appearance. Decreases in lysine and increases in water activity, volatile compound formation, and powder caking values were observed in many specimens. Levels of aerobic mesophilic bacteria, coliforms, yeast, and mold were <3.85 log10 cfu/g in all samples. Relative humidity was not a factor in most samples. When stored in sealed bags, these samples of WPC34 and WPC80 had a shelf life of 9 mo at 35 °C but at least 18 mo at lower temperatures, which should extend the market for these products. PMID:26778305</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/6501649','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/6501649"><span id="translatedtitle">Effect of ruminal ammonia-nitrogen <span class="hlt">concentration</span> on <span class="hlt">protein</span> degradation in situ.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Grummer, R R; Clark, J H; Davis, C L; Murphy, M R</p> <p>1984-10-01</p> <p>Two experiments were conducted to determine the effect of ruminal ammonia-nitrogen <span class="hlt">concentration</span> on rate of ruminal <span class="hlt">protein</span> degradation. In Experiment 1, four Holstein steers were fed a basal diet of corn grain and corn silage at hourly intervals. Continuous intraruminal infusions of solutions containing sodium bicarbonate and either sodium chloride or ammonium chloride resulted in ruminal ammonia-nitrogen <span class="hlt">concentrations</span> that averaged 4.8 and 17.3 mg/dl. Ruminal fluid pH, fluid volume, and turnover rate of fluid and molar percentage of acetate, propionate, and butyrate were similar across treatments, reflecting steady state conditions. Rates of nitrogen and dry matter disappearance from polyester bags containing soybean <span class="hlt">protein</span> supplements with 10.2 or 50.1% soluble nitrogen were not affected by increase of ruminal ammonia-nitrogen <span class="hlt">concentrations</span> from 4.8 to 17.3 mg/dl. In Experiment 2, Holstein steers were fed twice daily a basal diet of urea-supplemented corn grain and corn silage. Polyester bags containing soybean <span class="hlt">protein</span> supplements were placed in the rumen at -4, 0, or 4 h with reference to feeding and incubated from 1 to 12 h. Peak ruminal ammonia-nitrogen <span class="hlt">concentrations</span> occurred during different periods of incubation for each treatment. Ruminal ammonia-nitrogen <span class="hlt">concentrations</span> ranged from 3 mg/dl at 6 h postfeeding to 46 mg/dl at 1 h postfeeding. Nitrogen and dry matter disappearance rates during 0 to 1 and 1 to 12 h of incubation did not differ among treatments.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://hdl.handle.net/2060/20040110742','NASA-TRS'); return false;" href="http://hdl.handle.net/2060/20040110742"><span id="translatedtitle"><span class="hlt">Absolute</span> Equilibrium Entropy</span></a></p> <p><a target="_blank" href="http://ntrs.nasa.gov/search.jsp">NASA Technical Reports Server (NTRS)</a></p> <p>Shebalin, John V.</p> <p>1997-01-01</p> <p>The entropy associated with <span class="hlt">absolute</span> equilibrium ensemble theories of ideal, homogeneous, fluid and magneto-fluid turbulence is discussed and the three-dimensional fluid case is examined in detail. A sigma-function is defined, whose minimum value with respect to global parameters is the entropy. A comparison is made between the use of global functions sigma and phase functions H (associated with the development of various H-theorems of ideal turbulence). It is shown that the two approaches are complimentary though conceptually different: H-theorems show that an isolated system tends to equilibrium while sigma-functions allow the demonstration that entropy never decreases when two previously isolated systems are combined. This provides a more complete picture of entropy in the statistical mechanics of ideal fluids.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/23295111','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/23295111"><span id="translatedtitle">Effect of bleaching permeate from microfiltered skim milk on 80% serum <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Campbell, Rachel E; Adams, Michael C; Drake, Maryanne; Barbano, David M</p> <p>2013-03-01</p> <p>Whey <span class="hlt">proteins</span> that have been removed before the cheese-making process are referred to as "native" whey <span class="hlt">proteins</span> or milk serum <span class="hlt">proteins</span>. Because serum <span class="hlt">proteins</span> isolated directly from milk are not exposed to the cheese-making process, they are free from functional or sensory effects arising from this process. Whey <span class="hlt">proteins</span> used in food and beverage applications are largely derived from annatto-colored Cheddar cheese. Some of the annatto is left in the whey and this color is converted to a colorless compound by bleaching. The effect of bleaching serum <span class="hlt">proteins</span> on flavor and functionality of spray-dried <span class="hlt">protein</span> provides a platform to investigate the effect of bleaching free from the confounding effects of cheese manufacture. The objective of this study was to characterize and compare the sensory and functional properties of 80% milk serum <span class="hlt">protein</span> <span class="hlt">concentrate</span> (SPC80) produced from bleached and unbleached microfiltration (MF) permeate made from skim milk with and without added annatto color. Colored and uncolored MF permeates were bleached with benzoyl peroxide (BP) or hydrogen peroxide (HP), ultrafiltered, diafiltered, and spray-dried. The SPC80 from unbleached colored and uncolored MF permeates were manufactured as controls. All treatments were manufactured in triplicate. All SPC80 were evaluated by sensory testing, instrumental analyses, functionality, color, and proximate analysis. The HP-bleached SPC80 was higher in lipid oxidation compounds than BP-bleached or unbleached SPC80, specifically hexanal, heptanal, nonanal, decanal, and 2,3-octadienone. The HP treatments were higher in aroma intensity and cardboard and fatty flavors compared with the unbleached and BP-bleached SPC80. The SPC80 bleached with BP had lower <span class="hlt">concentrations</span> of norbixin compared with SPC80 bleached with HP. Functionality testing demonstrated that HP treatments had more soluble <span class="hlt">protein</span> after 10min of heating at 90°C and pH 4.6 and pH 7 compared with the no bleach and BP treatments, regardless</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1892893','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1892893"><span id="translatedtitle">Effect of <span class="hlt">Protein</span>, Polysaccharide, and Oxygen <span class="hlt">Concentration</span> Profiles on Biofilm Cohesiveness▿</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Ahimou, Francois; Semmens, Michael J.; Haugstad, Greg; Novak, Paige J.</p> <p>2007-01-01</p> <p>It is important to control biofilm cohesiveness to optimize process performance. In this study, a membrane-aerated biofilm reactor inoculated with activated sludge was used to grow mixed-culture biofilms of different ages and thicknesses. The cohesions, or cohesive energy levels per unit volume of biofilm, based on a reproducible method using atomic force microscopy (F. Ahimou, M. J. Semmens, P. J. Novak, and G. Haugstad, Appl. Environ. Microbiol. 73:2897-2904, 2007), were determined at different locations within the depths of the biofilms. In addition, the <span class="hlt">protein</span> and polysaccharide <span class="hlt">concentrations</span> within the biofilm depths, as well as the dissolved oxygen (DO) <span class="hlt">concentration</span> profiles within the biofilms, were measured. It was found that biofilm cohesion increased with depth but not with age. Level of biofilm cohesive energy per unit volume was strongly correlated with biofilm polysaccharide <span class="hlt">concentration</span>, which increased with depth in the membrane-aerated biofilm. In a 12-day-old biofilm, DO also increased with depth and may therefore be linked to polysaccharide production. In contrast, <span class="hlt">protein</span> <span class="hlt">concentration</span> was relatively constant within the biofilm and did not appear to influence cohesion. PMID:17337565</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2014PhDT.......321C','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2014PhDT.......321C"><span id="translatedtitle">Aggregation in <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions: Insights from rheology, neutron scattering and molecular simulations</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Castellanos, Maria Monica</p> <p></p> <p>Aggregation of therapeutic <span class="hlt">proteins</span> is currently one of the major challenges in the bio-pharmaceutical industry, because aggregates could induce immunogenic responses and compromise the quality of the product. Current scientific efforts, both in industry and academia, are focused on developing rational approaches to screen different drug candidates and predict their stability under different conditions. Moreover, aggregation is promoted in highly <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions, which are typically required for subcutaneous injection. In order to gain further understanding about the mechanisms that lead to aggregation, an approach that combined rheology, neutron scattering, and molecular simulations was undertaken. Two model systems were studied in this work: Bovine Serum Albumin in surfactant-free Phosphate Buffered Saline at pH = 7.4 at <span class="hlt">concentrations</span> from 11 mg/mL up to ˜519 mg/mL, and a monoclonal antibody in 20 mM Histidine/Histidine Hydrochloride at pH = 6.0 with 60 mg/mL trehalose and 0.2 mg/mL polysorbate-80 at <span class="hlt">concentrations</span> from 53 mg/mL up to ˜220 mg/mL. The antibody used here has three mutations in the CH2 domain, which result in lower stability upon incubation at 40 °C with respect to the wild-type <span class="hlt">protein</span>, based on size-exclusion chromatography assays. This temperature is below 49 °C, where unfolding of the least stable, CH2 domain occurs, according to differential scanning calorimetry. This dissertation focuses on identifying the role of aggregation on the viscosity of <span class="hlt">protein</span> solutions. The <span class="hlt">protein</span> solutions of this work show an increase in the low shear viscosity in the absence of surfactants, because <span class="hlt">proteins</span> adsorb at the air/water interface forming a viscoelastic film that affects the measured rheology. Stable surfactant-laden <span class="hlt">protein</span> solutions behave as simple Newtonian fluids. However, the surfactant-laden antibody solution also shows an increase in the low shear viscosity from bulk aggregation, after prolonged incubation at 40 °C. Small</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/23415538','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/23415538"><span id="translatedtitle">Effect of annatto addition and bleaching treatments on ultrafiltration flux during production of 80% whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> and 80% serum <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Adams, Michael C; Zulewska, Justyna; Barbano, David M</p> <p>2013-04-01</p> <p>The goals of this study were to determine if adding annatto color to milk or applying a bleaching process to whey or microfiltration (MF) permeate influenced ultrafiltration (UF) flux, diafiltration (DF) flux, or membrane fouling during production of 80% whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC80) or 80% serum <span class="hlt">protein</span> <span class="hlt">concentrate</span> (SPC80). Separated Cheddar cheese whey (18 vats using 900 kg of whole milk each) and MF permeate of skim milk (18 processing runs using 800 kg of skim milk each) were produced to make WPC80 and SPC80, respectively. The 6 treatments, replicated 3 times each, that constituted the 18 processing runs within either whey or MF permeate UF were as follows: (1) no annatto; (2) no annatto+benzoyl peroxide (BPO); (3) no annatto+hydrogen peroxide (H2O2); (4) annatto; (5) annatto+BPO; and (6) annatto+H2O2. Approximately 700 kg of whey or 530 kg of MF permeate from each treatment were heated to 50°C and processed in 2 stages (UF and DF) with the UF system in batch recirculation mode using a polyethersulfone spiral-wound UF membrane with a molecular weight cutoff of 10,000 Da. Addition of annatto color had no effect on UF or DF flux. The processes of bleaching whey or MF permeate with or without added color improved flux during processing. Bleaching with H2O2 usually produced higher flux than bleaching with BPO. Bleaching with BPO increased WPC80 flux to a greater extent than it did SPC80 flux. Though no differences in mean flux were observed for a common bleaching treatment between the WPC80 and SPC80 production processes during the UF stage, mean flux during WPC80 DF was higher than mean flux during SPC80 DF for each bleaching treatment. Water flux values before and after processing were used to calculate a fouling coefficient that demonstrated differences in fouling which were consistent with flux differences among treatments. In both processes, bleaching with H2O2 led to the largest reduction in fouling. No effect of annatto on fouling was observed. The</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26049243','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26049243"><span id="translatedtitle">Production and functional evaluation of a <span class="hlt">protein</span> <span class="hlt">concentrate</span> from giant squid (Dosidicus gigas) by acid dissolution and isoelectric precipitation.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Cortés-Ruiz, Juan A; Pacheco-Aguilar, Ramón; Elena Lugo-Sánchez, M; Gisela Carvallo-Ruiz, M; García-Sánchez, Guillermina</p> <p>2008-09-15</p> <p>A <span class="hlt">protein</span> <span class="hlt">concentrate</span> from giant squid (Dosidicus gigas) was produced under acidic conditions and its functional-technological capability evaluated in terms of its gel-forming ability, water holding capacity and colour attributes. Technological functionality of the <span class="hlt">concentrate</span> was compared with that of squid muscle and a neutral <span class="hlt">concentrate</span>. <span class="hlt">Protein-protein</span> aggregates insoluble at high ionic strength (I=0.5M), were detected in the acidic <span class="hlt">concentrate</span> as result of processing with no preclusion of its gel-forming ability during the sol-to-gel thermal transition. Even though washing under acidic condition promoted autolysis of the myosin heavy chain, the acidic <span class="hlt">concentrate</span> displayed an outstanding ability to gel giving samples with a gel strength of 455 and 1160gcm at 75% and 90% compression respectively, and an AA folding test grade indicative of high gel strength, elasticity, and cohesiveness. The process proved to be a good alternative for obtaining a functional <span class="hlt">protein</span> <span class="hlt">concentrate</span> from giant squid muscle.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=302129','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=302129"><span id="translatedtitle">Effect of Peritubular <span class="hlt">Protein</span> <span class="hlt">Concentration</span> on Reabsorption of Sodium and Water in Isolated Perfused Proximal Tubules</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Imai, Masashi; Kokko, Juha P.</p> <p>1972-01-01</p> <p>Micropuncture studies have indicated that variation in peritubular oncotic pressure influences net transport of fluid out of the proximal tubule. The present in vitro studies on isolated perfused rabbit proximal convoluted tubules were designed to examine whether <span class="hlt">protein</span> <span class="hlt">concentration</span> gradient must act across the peritubular capillary membrane to influence reabsorption, or whether it can exert a direct effect across the tubular basement membrane 71 proximal tubules were perfused with ultrafiltrate made isosmolal to bathing fluids, the latter having identical electrolyte composition as the perfusing ultrafiltrate, but adjusted to three oncotic pressures: hypooncotic, <span class="hlt">protein</span> 0.0 g/100 ml; control isooncotic serum, <span class="hlt">protein</span> 6.4 g/100 ml; and hyperoncotic, <span class="hlt">protein</span> 12.5 g/100 ml. Net volume flux (nl/mm per min), net Na flux (nEq/mm per min), unidirectional Na flux from bath to lumen (nEq/mm per min), and passive permeability coefficient (× 10-5 cm/sec) for Na (PNa), urea (Purea), and sucrose (Psucrose) were determined using isotopic techniques. When the bath was hypooncotic, there was (as compared with isooncotic serum) a significant decrease in net volume (38%) and net sodium (40%) flux, but no change in PNa, Purea, or transtubular potential; however, Psucrose increased significantly (78%). In experiments in which hyperoncotic bath was used, there was (compared with isooncotic serum) an increase in net volume (28%) and net sodium (30%) flux, but transtubular potential difference did not change significantly. These data demonstrated that changes in the ambient <span class="hlt">protein</span> <span class="hlt">concentration</span> gradient exert direct effects upon proximal tubular reabsorption. Because penetration of sucrose (an index of intercellular movement) but not urea (an index of transcellular movement) varied with changes in tubular reabsorption, it is suggested that oncotic pressure acts by altering the rate of back-leak of reabsorbate through extracellular pathways between tubular cells. It is concluded</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4351878','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4351878"><span id="translatedtitle">Optimal <span class="hlt">Concentration</span> of 2,2,2-Trichloroacetic Acid for <span class="hlt">Protein</span> Precipitation Based on Response Surface Methodology</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Ngo, Albert N; Ezoulin, Miezan JM; Youm, Ibrahima; Youan, Bi-Botti C</p> <p>2014-01-01</p> <p>For low <span class="hlt">protein</span> <span class="hlt">concentrations</span> containing biological samples (in proteomics) and for non proteinaceous compound assays (in bioanalysis), there is a critical need for a simple, fast, and cost-effective <span class="hlt">protein</span> enrichment or precipitation method. However, 2,2,2-trichloroacetic acid (TCA) is traditionally used for <span class="hlt">protein</span> precipitation at ineffective <span class="hlt">concentrations</span> for very low <span class="hlt">protein</span> containing samples. It is hypothesized that response surface methodology, can be used to systematically identify the optimal TCA <span class="hlt">concentration</span> for <span class="hlt">protein</span> precipitation in a wider <span class="hlt">concentration</span> range. To test this hypothesis, a central composite design is used to assess the effects of two factors (X1 = volume of aqueous solution of <span class="hlt">protein</span>, and X2 = volume of TCA solution 6.1N) on the optical absorbance of the supernatant (Y1), and the percentage of <span class="hlt">protein</span> precipitated (Y2). Using either bovine serum albumin (BSA) as a model <span class="hlt">protein</span> or human urine (with 20 ppm <span class="hlt">protein</span> content), 4% w/v (a saddle point) is the optimal <span class="hlt">concentration</span> of the TCA solution for <span class="hlt">protein</span> precipitation that is visualized by SDS-PAGE analysis. At this optimal <span class="hlt">concentration</span>, the Y2-values range from 76.26 to 92.67% w/w for 0.016 to 2 mg/mL of BSA solution. It is also useful for <span class="hlt">protein</span> enrichment and xenobiotic analysis in <span class="hlt">protein</span>-free supernatant as applied to tenofovir (a model HIV microbicide). In these conditions, the limit of detection and limit of quantitation of tenofovir are respectively 0.0014 mg/mL and 0.0042 mg/mL. This optimal <span class="hlt">concentration</span> of TCA provides optimal condition for <span class="hlt">protein</span> purification and analysis of any xenobiotic compound like tenofovir. PMID:25750762</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/biblio/935899','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/biblio/935899"><span id="translatedtitle">Predicting <span class="hlt">protein</span> <span class="hlt">concentrations</span> with ELISA microarray assays, monotonic splines and Monte Carlo simulation</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>Daly, Don S.; Anderson, Kevin K.; White, Amanda M.; Gonzalez, Rachel M.; Varnum, Susan M.; Zangar, Richard C.</p> <p>2008-07-14</p> <p>Background: A microarray of enzyme-linked immunosorbent assays, or ELISA microarray, predicts simultaneously the <span class="hlt">concentrations</span> of numerous <span class="hlt">proteins</span> in a small sample. These predictions, however, are uncertain due to processing error and biological variability. Making sound biological inferences as well as improving the ELISA microarray process require require both <span class="hlt">concentration</span> predictions and creditable estimates of their errors. Methods: We present a statistical method based on monotonic spline statistical models, penalized constrained least squares fitting (PCLS) and Monte Carlo simulation (MC) to predict <span class="hlt">concentrations</span> and estimate prediction errors in ELISA microarray. PCLS restrains the flexible spline to a fit of assay intensity that is a monotone function of <span class="hlt">protein</span> <span class="hlt">concentration</span>. With MC, both modeling and measurement errors are combined to estimate prediction error. The spline/PCLS/MC method is compared to a common method using simulated and real ELISA microarray data sets. Results: In contrast to the rigid logistic model, the flexible spline model gave credible fits in almost all test cases including troublesome cases with left and/or right censoring, or other asymmetries. For the real data sets, 61% of the spline predictions were more accurate than their comparable logistic predictions; especially the spline predictions at the extremes of the prediction curve. The relative errors of 50% of comparable spline and logistic predictions differed by less than 20%. Monte Carlo simulation rendered acceptable asymmetric prediction intervals for both spline and logistic models while propagation of error produced symmetric intervals that diverged unrealistically as the standard curves approached horizontal asymptotes. Conclusions: The spline/PCLS/MC method is a flexible, robust alternative to a logistic/NLS/propagation-of-error method to reliably predict <span class="hlt">protein</span> <span class="hlt">concentrations</span> and estimate their errors. The spline method simplifies model selection and fitting</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/25328200','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/25328200"><span id="translatedtitle">Non-wheat pasta based on pearl millet flour containing barley and whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Yadav, Deep N; Balasubramanian, S; Kaur, Jaspreet; Anand, Tanupriya; Singh, Ashish K</p> <p>2014-10-01</p> <p>Non-wheat pasta was prepared with pearl millet supplemented with 10-30 % barley flour, 5-15 % whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>, 2.5-4 % carboxy methyl cellulose and 27-33 % water using response surface methodology (RSM) following central composite rotatable design (CCRD). Results showed that barley flour and whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) had significant (p ≤ 0.05) positive effect on lightness and negative effect on stickiness of pasta, thus improved the overall acceptability (OAA). Carboxymethyl cellulose (CMC) improved the textural attributes i.e. increased firmness and decreased stickiness significantly (P ≤ 0.05) and caused a significant (P ≤ 0.05) reduction in solids losses in gruel. Based upon the experiments, the optimized level of ingredients were barley flour 13.80 g 100 g(-1) pearl millet flour (PMF), WPC 12.27 g 100 g(-1) PMF, CMC 3.45 g 100 g(-1) PMF and water 27.6 mL 100 g(-1) ingredients premix with 88 % desirability. The developed pasta had <span class="hlt">protein</span> 16.47 g, calcium 98.53 mg, iron 5.43 mg, phosphorus 315.5 mg and β-glucan 0.33 g 100 g(-1) pasta (db). PMID:25328200</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_11");'>11</a></li> <li><a href="#" onclick='return showDiv("page_12");'>12</a></li> <li class="active"><span>13</span></li> <li><a href="#" onclick='return showDiv("page_14");'>14</a></li> <li><a href="#" onclick='return showDiv("page_15");'>15</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_13 --> <div id="page_14" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_12");'>12</a></li> <li><a href="#" onclick='return showDiv("page_13");'>13</a></li> <li class="active"><span>14</span></li> <li><a href="#" onclick='return showDiv("page_15");'>15</a></li> <li><a href="#" onclick='return showDiv("page_16");'>16</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="261"> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1885672','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1885672"><span id="translatedtitle"><span class="hlt">Concentration</span>-dependent organization of DNA by the dinoflagellate histone-like <span class="hlt">protein</span> HCc3</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Chan, Yuk-Hang; Wong, Joseph T. Y.</p> <p>2007-01-01</p> <p>The liquid crystalline chromosomes of dinoflagellates are the alternative to the nucleosome-based organization of chromosomes in the eukaryotes. These nucleosome-less chromosomes have to devise novel ways to maintain active parts of the genome. The dinoflagellate histone-like <span class="hlt">protein</span> HCc3 has significant sequence identity with the bacterial DNA-binding <span class="hlt">protein</span> HU. HCc3 also has a secondary structure resembling HU in silico. We have examined HCc3 in its recombinant form. Experiments on DNA-cellulose revealed its DNA-binding activity is on the C-terminal domain. The N-terminal domain is responsible for intermolecular oligomerization as demonstrated by cross-linking studies. However, HCc3 could not complement Escherichia coli HU-deficient mutants, suggesting functional differences. In ligation assays, HCc3-induced DNA concatenation but not ring closure as the DNA-bending HU does. The basic HCc3 was an efficient DNA condensing agent, but it did not behave like an ordinary polycationic compound. HCc3 also induced specific structures with DNA in a <span class="hlt">concentration</span>-dependent manner, as demonstrated by atomic force microscopy (AFM). At moderate <span class="hlt">concentration</span> of HCc3, DNA bridging and bundling were observed; at high <span class="hlt">concentrations</span>, the complexes were even more condensed. These results are consistent with a biophysical role for HCc3 in maintaining extended DNA loops at the periphery of liquid crystalline chromosomes. PMID:17412706</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/biblio/21611867','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/biblio/21611867"><span id="translatedtitle"><span class="hlt">Absolute</span> neutrino mass measurements</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>Wolf, Joachim</p> <p>2011-10-06</p> <p>The neutrino mass plays an important role in particle physics, astrophysics and cosmology. In recent years the detection of neutrino flavour oscillations proved that neutrinos carry mass. However, oscillation experiments are only sensitive to the mass-squared difference of the mass eigenvalues. In contrast to cosmological observations and neutrino-less double beta decay (0v2{beta}) searches, single {beta}-decay experiments provide a direct, model-independent way to determine the <span class="hlt">absolute</span> neutrino mass by measuring the energy spectrum of decay electrons at the endpoint region with high accuracy.Currently the best kinematic upper limits on the neutrino mass of 2.2eV have been set by two experiments in Mainz and Troitsk, using tritium as beta emitter. The next generation tritium {beta}-experiment KATRIN is currently under construction in Karlsruhe/Germany by an international collaboration. KATRIN intends to improve the sensitivity by one order of magnitude to 0.2eV. The investigation of a second isotope ({sup 137}Rh) is being pursued by the international MARE collaboration using micro-calorimeters to measure the beta spectrum. The technology needed to reach 0.2eV sensitivity is still in the R and D phase. This paper reviews the present status of neutrino-mass measurements with cosmological data, 0v2{beta} decay and single {beta}-decay.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4468161','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4468161"><span id="translatedtitle">Effects of Break Crops on Yield and Grain <span class="hlt">Protein</span> <span class="hlt">Concentration</span> of Barley in a Boreal Climate</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Zou, Ling; Yli-Halla, Markku; Stoddard, Frederick L.; Mäkelä, Pirjo S. A.</p> <p>2015-01-01</p> <p>Rotation with dicotyledonous crops to break cereal monoculture has proven to be beneficial to successive cereals. In two fields where the soil had been subjected to prolonged, continuous cereal production, two 3-year rotation trials were established. In the first year, faba bean, turnip rape and barley were grown, as first crops, in large blocks and their residues tilled into the soil after harvest. In the following year, barley, buckwheat, caraway, faba bean, hemp and white lupin were sown, as second crops, in each block and incorporated either at flowering stage (except barley) or after harvest. In the third year, barley was grown in all plots and its yield and grain <span class="hlt">protein</span> <span class="hlt">concentration</span> were determined. Mineral N in the plough layer was determined two months after incorporation of crops and again before sowing barley in the following year. The effect of faba bean and turnip rape on improving barley yields and grain <span class="hlt">protein</span> <span class="hlt">concentration</span> was still detectable two years after they were grown. The yield response of barley was not sensitive to the growth stage of second crops when they were incorporated, but was to different second crops, showing clear benefits averaging 6-7% after white lupin, faba bean and hemp but no benefit from caraway or buckwheat. The effect of increased N in the plough layer derived from rotation crops on barley yields was minor. Incorporation of plants at flowering stage slightly increased third-year barley grain <span class="hlt">protein</span> <span class="hlt">concentration</span> but posed a great potential for N loss compared with incorporation of crop residues after harvest, showing the value of either delayed incorporation or using catch crops. PMID:26076452</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26076452','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26076452"><span id="translatedtitle">Effects of Break Crops on Yield and Grain <span class="hlt">Protein</span> <span class="hlt">Concentration</span> of Barley in a Boreal Climate.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Zou, Ling; Yli-Halla, Markku; Stoddard, Frederick L; Mäkelä, Pirjo S A</p> <p>2015-01-01</p> <p>Rotation with dicotyledonous crops to break cereal monoculture has proven to be beneficial to successive cereals. In two fields where the soil had been subjected to prolonged, continuous cereal production, two 3-year rotation trials were established. In the first year, faba bean, turnip rape and barley were grown, as first crops, in large blocks and their residues tilled into the soil after harvest. In the following year, barley, buckwheat, caraway, faba bean, hemp and white lupin were sown, as second crops, in each block and incorporated either at flowering stage (except barley) or after harvest. In the third year, barley was grown in all plots and its yield and grain <span class="hlt">protein</span> <span class="hlt">concentration</span> were determined. Mineral N in the plough layer was determined two months after incorporation of crops and again before sowing barley in the following year. The effect of faba bean and turnip rape on improving barley yields and grain <span class="hlt">protein</span> <span class="hlt">concentration</span> was still detectable two years after they were grown. The yield response of barley was not sensitive to the growth stage of second crops when they were incorporated, but was to different second crops, showing clear benefits averaging 6-7% after white lupin, faba bean and hemp but no benefit from caraway or buckwheat. The effect of increased N in the plough layer derived from rotation crops on barley yields was minor. Incorporation of plants at flowering stage slightly increased third-year barley grain <span class="hlt">protein</span> <span class="hlt">concentration</span> but posed a great potential for N loss compared with incorporation of crop residues after harvest, showing the value of either delayed incorporation or using catch crops. PMID:26076452</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26740138','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26740138"><span id="translatedtitle">Effects of dietary <span class="hlt">protein</span> <span class="hlt">concentration</span> on performance and nutrient digestibility in Pekin ducks during aflatoxicosis.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Chen, X; Murdoch, R; Zhang, Q; Shafer, D J; Applegate, T J</p> <p>2016-04-01</p> <p>A 14-d study was conducted to determine the impact of dietary crude <span class="hlt">protein</span> <span class="hlt">concentration</span> on performance, serum biochemistry, and nutrient digestive functions in Pekin ducklings during aflatoxicosis. A total of 144 male Pekin ducklings were randomly allotted to 4 dietary treatments arranged in a 2×2 factorial with 2 crude <span class="hlt">protein</span> (CP) (20 and 24% on an analyzed basis) with or without 0.2 mg/kg aflatoxin B1 (AFB1) (0.21 mg/kg analyzed). The AFB1 reduced BW gain, feed intake, and breast muscle weight by 33 to 43% (P<0.0001). Serum <span class="hlt">concentration</span> of <span class="hlt">protein</span>, glucose, and Ca were also decreased by AFB1 (P≤0.0015), while pancreatic activities of amylase and lipase were increased by AFB1 (P<0.005). Apparent N digestibility was not affected by dietary treatment, whereas apparent ileal digestible energy was reduced 7.6% by AFB1 (P=0.0003). Higher dietary CP improved BW gain, gain:feed ratio, and breast muscle weight (P≤0.021), and tended to improve feed intake (P=0.094), but did not improve serum measures, digestive enzyme activity, or nutrient digestibility. No statistical interaction of AFB1 by CP was observed for any measures. Results from the current study suggest that AFB1 at low <span class="hlt">concentration</span> can significantly impair performance of Pekin ducklings primarily through inhibited feed intake, as well as influence nutrient digestion processes (jejunum morphology, digestive enzyme activity, and apparent energy digestibility). Higher dietary CP can improve growth performance of ducklings regardless of AF exposure, but did not interact with dietary AFB1 on performance, serum biochemistry, or nutrient digestion in Pekin ducklings from hatch to 14 d.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/10641273','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/10641273"><span id="translatedtitle">[Medical and biological evaluation of safety of <span class="hlt">protein</span> <span class="hlt">concentrate</span> from genetically-modified soybeans. Biochemical studies].</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Tutel'ian, V A; Kravchenko, L V; Lashneva, N V; Avren'eva, L I; Guseva, G V; Sorokina, E Iu; Chernysheva, O N</p> <p>1999-01-01</p> <p>The rats were fed with albuminous <span class="hlt">concentrate</span> from the genetically modified soybean 40-3-2 ("Monsanto Co", USA) 1.25 g/rat/day for 5 months. Their blood, urea and liver were investigated to measure total <span class="hlt">protein</span> and glucose levels, aminotransferase and alkaline phosphatase activities, pH, relative density and creatinine level in the urea, as well as hepatic enzyme activity of the I and II phases of xenobiotic metabolism, and the whole and non-sedimentated lysosomal enzyme activities. The lasting albuminous <span class="hlt">concentrate</span> supplementation from the genetically modified soybean to the rat's diet has been shown to modify hepatocyte membrane function and enzymatic activity within physiological standards. It was not harmful to the adaptation systems.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27037608','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27037608"><span id="translatedtitle">Instrumental and Sensory Texture Attributes of High-<span class="hlt">Protein</span> Nutrition Bars Formulated with Extruded Milk <span class="hlt">Protein</span> <span class="hlt">Concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Banach, J C; Clark, S; Lamsal, B P</p> <p>2016-05-01</p> <p>Previous instrumental study of high-<span class="hlt">protein</span> nutrition (HPN) bars formulated with extruded milk <span class="hlt">protein</span> <span class="hlt">concentrate</span> (MPC) indicated slower hardening compared to bars formulated with unmodified MPC. However, hardness, and its change during storage, insufficiently characterizes HPN bar texture. In this study, MPC80 was extruded at 2 different conditions and model HPN bars were prepared. A trained sensory panel and instrumental techniques were used to measure HPN bar firmness, crumbliness, fracturability, hardness, cohesiveness, and other attributes to characterize texture change during storage. Extrusion modification, storage temperature, and storage time significantly affected the instrumental and sensory panel measured texture attributes. The HPN bars became firmer and less cohesive during storage. When evaluated at the same storage conditions, the texture attributes of the HPN bars formulated with the different extrudates did not differ significantly from each other. However, textural differences were noted most of the time between the control and the HPN bars formulated with extruded MPC80. An adapted HPN bar crumbliness measurement technique produced results that were correlated with sensory panel measured crumbliness (r = 0.85) and cohesiveness (r = -0.84). Overall, the HPN bars formulated with extruded MPC80 were significantly softer, less crumbly, and more cohesive than the control during storage.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/22045330','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/22045330"><span id="translatedtitle">Continuous microfluidic DNA and <span class="hlt">protein</span> trapping and <span class="hlt">concentration</span> by balancing transverse electrokinetic forces.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Morales, Mercedes C; Lin, Hao; Zahn, Jeffrey D</p> <p>2012-01-01</p> <p>Sample pre-<span class="hlt">concentration</span> can be a critical element to improve sensitivity of integrated microchip assays. In this work a converging Y-inlet microfluidic channel with integrated coplanar electrodes was used to investigate transverse DNA and <span class="hlt">protein</span> migration under uniform direct current (DC) electric fields to assess the ability to <span class="hlt">concentrate</span> a sample prior to other enzymatic modifications or capillary electrophoretic separations. Employing a pressure-driven flow to perfuse the microchannel, negatively charged samples diluted in low and high ionic strength buffers were co-infused with a receiving buffer of the same ionic strength into a main daughter channel. Experimental results demonstrated that, depending of the buffer selection, different DNA migration and accumulation dynamics were seen. Charged analytes could traverse the channel width and accumulate at the positive bias electrode in a low electroosmotic mobility, high electrophoretic mobility, high ionic strength buffer or migrated towards an equilibrium position within the channel in a high electroosmotic mobility, high electrophoretic mobility, low ionic strength buffer. The various migration behaviours are the result of a balance between the electrophoretic force and a drag force induced by a recirculating electroosmotic flow generated across the channel width due to the bounding walls. Under continuous flow conditions, DNA samples were <span class="hlt">concentrated</span> several-fold by balancing these transverse electrokinetic forces. The electrokinetic trapping technique presented here is a simple technique which could be expanded to <span class="hlt">concentrate</span> or separate other analytes as a preconditioning step for downstream processes. PMID:22045330</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/18792928','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/18792928"><span id="translatedtitle">A gel-free MS-based quantitative proteomic approach accurately measures cytochrome P450 <span class="hlt">protein</span> <span class="hlt">concentrations</span> in human liver microsomes.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Wang, Michael Zhuo; Wu, Judy Qiju; Dennison, Jennifer B; Bridges, Arlene S; Hall, Stephen D; Kornbluth, Sally; Tidwell, Richard R; Smith, Philip C; Voyksner, Robert D; Paine, Mary F; Hall, James Edwin</p> <p>2008-10-01</p> <p>The human cytochrome P450 (P450) superfamily consists of membrane-bound <span class="hlt">proteins</span> that metabolize a myriad of xenobiotics and endogenous compounds. Quantification of P450 expression in various tissues under normal and induced conditions has an important role in drug safety and efficacy. Conventional immunoquantification methods have poor dynamic range, low throughput, and a limited number of specific antibodies. Recent advances in MS-based quantitative proteomics enable <span class="hlt">absolute</span> <span class="hlt">protein</span> quantification in a complex biological mixture. We have developed a gel-free MS-based <span class="hlt">protein</span> quantification strategy to quantify CYP3A enzymes in human liver microsomes (HLM). Recombinant <span class="hlt">protein</span>-derived proteotypic peptides and synthetic stable isotope-labeled proteotypic peptides were used as calibration standards and internal standards, respectively. The lower limit of quantification was approximately 20 fmol P450. In two separate panels of HLM examined (n = 11 and n = 22), CYP3A, CYP3A4 and CYP3A5 <span class="hlt">concentrations</span> were determined reproducibly (CV <or=27%). The MS-based method strongly correlated with the immunoquantification method (r(2)>or=0.87) and marker activities (r(2)>or=0.88), including testosterone 6beta-hydroxylation (CYP3A), midazolam 1'-hydroxylation (CYP3A), itraconazole 6-hydroxylation (CYP3A4) and CYP3A5-mediated vincristine M1 formation (CYP3A5). Taken together, our MS-based method provides a specific, sensitive and reliable means of P450 <span class="hlt">protein</span> quantification and should facilitate P450 characterization during drug development, especially when specific substrates and/or antibodies are unavailable.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/servlets/purl/1176532','DOE-PATENT-XML'); return false;" href="http://www.osti.gov/scitech/servlets/purl/1176532"><span id="translatedtitle"><span class="hlt">Absolute</span> cavity pyrgeometer</span></a></p> <p><a target="_blank" href="http://www.osti.gov/doepatents">DOEpatents</a></p> <p>Reda, Ibrahim</p> <p>2013-10-29</p> <p>Implementations of the present disclosure involve an apparatus and method to measure the long-wave irradiance of the atmosphere or long-wave source. The apparatus may involve a thermopile, a <span class="hlt">concentrator</span> and temperature controller. The incoming long-wave irradiance may be reflected from the <span class="hlt">concentrator</span> to a thermopile receiver located at the bottom of the <span class="hlt">concentrator</span> to receive the reflected long-wave irradiance. In addition, the thermopile may be thermally connected to a temperature controller to control the device temperature. Through use of the apparatus, the long-wave irradiance of the atmosphere may be calculated from several measurements provided by the apparatus. In addition, the apparatus may provide an international standard of pyrgeometers' calibration that is traceable back to the International System of Units (SI) rather than to a blackbody atmospheric simulator.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/21184728','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/21184728"><span id="translatedtitle">Quantification of <span class="hlt">protein</span> <span class="hlt">concentration</span> by the Bradford method in the presence of pharmaceutical polymers.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Carlsson, Nils; Borde, Annika; Wölfel, Sebastian; Kerman, Björn; Larsson, Anette</p> <p>2011-04-01</p> <p>We investigated how the Bradford assay for measurements of <span class="hlt">protein</span> released from a drug formulation may be affected by a concomitant release of a pharmaceutical polymer used to formulate the <span class="hlt">protein</span> delivery device. The main result is that polymer-caused perturbations of the Coomassie dye absorbance at the Bradford monitoring wavelength (595nm) can be identified and corrected by recording absorption spectra in the region of 350-850mm. The pharmaceutical polymers Carbopol and chitosan illustrate two potential types of perturbations in the Bradford assay, whereas the third polymer, hydroxypropylmethylcellulose (HPMC), acts as a nonperturbing control. Carbopol increases the apparent absorbance at 595nm because the polymer aggregates at the low pH of the Bradford protocol, causing a turbidity contribution that can be corrected quantitatively at 595nm by measuring the sample absorbance at 850nm outside the dye absorption band. Chitosan is a cationic polymer under Bradford conditions and interacts directly with the anionic Coomassie dye and perturbs its absorption spectrum, including 595nm. In this case, the Bradford method remains useful if the polymer <span class="hlt">concentration</span> is known but should be used with caution in release studies where the polymer <span class="hlt">concentration</span> may vary and needs to be measured independently.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/24969531','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/24969531"><span id="translatedtitle">Why to compare <span class="hlt">absolute</span> numbers of mitochondria.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Schmitt, Sabine; Schulz, Sabine; Schropp, Eva-Maria; Eberhagen, Carola; Simmons, Alisha; Beisker, Wolfgang; Aichler, Michaela; Zischka, Hans</p> <p>2014-11-01</p> <p>Prompted by pronounced structural differences between rat liver and rat hepatocellular carcinoma mitochondria, we suspected these mitochondrial populations to differ massively in their molecular composition. Aiming to reveal these mitochondrial differences, we came across the issue on how to normalize such comparisons and decided to focus on the <span class="hlt">absolute</span> number of mitochondria. To this end, fluorescently stained mitochondria were quantified by flow cytometry. For rat liver mitochondria, this approach resulted in mitochondrial <span class="hlt">protein</span> contents comparable to earlier reports using alternative methods. We determined similar <span class="hlt">protein</span> contents for rat liver, heart and kidney mitochondria. In contrast, however, lower <span class="hlt">protein</span> contents were determined for rat brain mitochondria and for mitochondria from the rat hepatocellular carcinoma cell line McA 7777. This result challenges mitochondrial comparisons that rely on equal <span class="hlt">protein</span> amounts as a typical normalization method. Exemplarily, we therefore compared the activity and susceptibility toward inhibition of complex II of rat liver and hepatocellular carcinoma mitochondria and obtained significant discrepancies by either normalizing to <span class="hlt">protein</span> amount or to <span class="hlt">absolute</span> mitochondrial number. Importantly, the latter normalization, in contrast to the former, demonstrated a lower complex II activity and higher susceptibility toward inhibition in hepatocellular carcinoma mitochondria compared to liver mitochondria. These findings demonstrate that solely normalizing to <span class="hlt">protein</span> amount may obscure essential molecular differences between mitochondrial populations.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25005955','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25005955"><span id="translatedtitle">Kinetics of enthalpy relaxation of milk <span class="hlt">protein</span> <span class="hlt">concentrate</span> powder upon ageing and its effect on solubility.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Haque, Enamul; Whittaker, Andrew K; Gidley, Michael J; Deeth, Hilton C; Fibrianto, Kiki; Bhandari, Bhesh R</p> <p>2012-10-01</p> <p>Kinetics of enthalpy relaxation of milk <span class="hlt">protein</span> <span class="hlt">concentrate</span> (MPC) powder upon short-term (up to 67 h) storage at 25 °C and aw 0.85, and long-term (up to 48 days) storage at 25 °C and a range of aw values (0-0.85) were studied by differential scanning calorimetry (DSC). The short-term study showed a rapid recovery of enthalpy for the first 48 h, followed by a slower steady increase with time. The non-exponential β parameter was calculated using the Kohlrausch-Williams-Watts function and found to be 0.39. Long-term storage showed that enthalpy relaxation depends on both storage period and water activity. The enthalpy value was much less for lower moisture content (mc) (aw ≤ 0.23, mc ≤ 5.5%) than for higher mc (aw ≥ 0.45, mc ≥ 8%) samples for a particular storage period. The results suggest that the presence of more water molecules, in close proximity to the <span class="hlt">protein</span> surface facilitates kinetic unfreezing and subsequent motion of molecular segments of <span class="hlt">protein</span> molecules towards thermodynamic equilibrium. Although de-ageing of stored samples did not reverse storage-induced solubility losses, the timescale of enthalpy relaxation was similar to that of solubility loss. It is suggested that enthalpy relaxation within stored samples allows structural rearrangements that are responsible for subsequent solubility decreases.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27394941','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27394941"><span id="translatedtitle">Composition and functionality of whey <span class="hlt">protein</span> phospholipid <span class="hlt">concentrate</span> and delactosed permeate.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Levin, M A; Burrington, K J; Hartel, R W</p> <p>2016-09-01</p> <p>Whey <span class="hlt">protein</span> phospholipid <span class="hlt">concentrate</span> (WPPC) and delactosed permeate (DLP) are 2 coproducts of cheese whey processing that are currently underused. Past research has shown that WPPC and DLP can be used together as a functional dairy ingredient in foods such as ice cream, soup, and caramel. However, the scope of the research has been limited to 1 WPPC supplier. The objective of this research was to fully characterize a range of WPPC. Four WPPC samples and 1 DLP sample were analyzed for chemical composition and functionality. This analysis showed that WPPC composition was highly variable between suppliers and lots. In addition, the functionality of the WPPC varies depending on the supplier and testing pH, and cannot be correlated with fat or <span class="hlt">protein</span> content because of differences in processing. The addition of DLP to WPPC affects functionality. In general, WPPC has a high water-holding capacity, is relatively heat stable, has low foamability, and does not aid in emulsion stability. The gel strength and texture are highly dependent on the amount of <span class="hlt">protein</span>. To be able to use these 2 dairy products, the composition and functionality must be fully understood. PMID:27394941</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://eric.ed.gov/?q=serial+AND+position+AND+effect&id=EJ735377','ERIC'); return false;" href="http://eric.ed.gov/?q=serial+AND+position+AND+effect&id=EJ735377"><span id="translatedtitle"><span class="hlt">Absolute</span> Identification by Relative Judgment</span></a></p> <p><a target="_blank" href="http://www.eric.ed.gov/ERICWebPortal/search/extended.jsp?_pageLabel=advanced">ERIC Educational Resources Information Center</a></p> <p>Stewart, Neil; Brown, Gordon D. A.; Chater, Nick</p> <p>2005-01-01</p> <p>In unidimensional <span class="hlt">absolute</span> identification tasks, participants identify stimuli that vary along a single dimension. Performance is surprisingly poor compared with discrimination of the same stimuli. Existing models assume that identification is achieved using long-term representations of <span class="hlt">absolute</span> magnitudes. The authors propose an alternative…</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://eric.ed.gov/?q=VALUE+AND+ABSOLUTE&id=EJ765743','ERIC'); return false;" href="http://eric.ed.gov/?q=VALUE+AND+ABSOLUTE&id=EJ765743"><span id="translatedtitle">Be Resolute about <span class="hlt">Absolute</span> Value</span></a></p> <p><a target="_blank" href="http://www.eric.ed.gov/ERICWebPortal/search/extended.jsp?_pageLabel=advanced">ERIC Educational Resources Information Center</a></p> <p>Kidd, Margaret L.</p> <p>2007-01-01</p> <p>This article explores how conceptualization of <span class="hlt">absolute</span> value can start long before it is introduced. The manner in which <span class="hlt">absolute</span> value is introduced to students in middle school has far-reaching consequences for their future mathematical understanding. It begins to lay the foundation for students' understanding of algebra, which can change…</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/1695679','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/1695679"><span id="translatedtitle">Pregnancy-specific <span class="hlt">protein</span> B and progesterone <span class="hlt">concentrations</span> in French Alpine goats throughout gestation.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Humblot, P; De Montigny, G; Jeanguyot, N; Tetedoie, F; Payen, B; Thibier, M; Sasser, R G</p> <p>1990-05-01</p> <p>The 34 French Alpine dairy goats originated from a single flock and were artificially inseminated 44 h after synchronization of oestrus. They were bled daily at the jugular vein from 15 to 27 days after AI. An early pregnancy diagnosis by RIA of progesterone <span class="hlt">concentration</span> was performed 21 days after AI. In pregnant goats (greater than 1.5 ng progesterone/ml) daily sampling was extended until 30 days after AI and, from those, 9 were bled every 2 weeks until the end of pregnancy and at 50 and 63 days post partum. Pregnancy-specific <span class="hlt">protein</span> B (PSPB) was also assayed. The kidding rate was 67.6% (23/34). PSPB <span class="hlt">concentrations</span> (ng/ml) in pregnant goats were significantly different from those of non-pregnant goats at 24 days after AI (0.82 +/- 0.18 vs 1.78 +/- 0.19; mean +/- s.e.m.) and rose to 40 ng/ml at the end of pregnancy. From Day 25 and throughout gestation, females with 2 fetuses had higher PSPB <span class="hlt">concentrations</span> than did those with a single fetus (P less than 0.05). In the 2 goats exhibiting late embryonic mortality according to progesterone <span class="hlt">concentrations</span>, one had a PSPB profile very similar to those of pregnant goats until 30 days while the other did not show any elevation of PSPB <span class="hlt">concentration</span>. It is concluded that PSPB profiles in goats are similar to those found in cows throughout pregnancy and that PSPB RIA may be useful for pregnancy diagnosis or diagnosis of late embryonic mortality. PMID:1695679</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/18702478','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/18702478"><span id="translatedtitle">Effects of ammonium sulfate and sodium chloride <span class="hlt">concentration</span> on PEG/<span class="hlt">protein</span> liquid-liquid phase separation.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Dumetz, André C; Lewus, Rachael A; Lenhoff, Abraham M; Kaler, Eric W</p> <p>2008-09-16</p> <p>When added to <span class="hlt">protein</span> solutions, poly(ethylene glycol) (PEG) creates an effective attraction between <span class="hlt">protein</span> molecules due to depletion forces. This effect has been widely used to crystallize <span class="hlt">proteins</span>, and PEG is among the most successful crystallization agents in current use. However, PEG is almost always used in combination with a salt at either low or relatively high <span class="hlt">concentrations</span>. Here the effects of sodium chloride and ammonium sulfate <span class="hlt">concentration</span> on PEG 8000/ovalbumin liquid-liquid (L-L) phase separation are investigated. At low salt the L-L phase separation occurs at decreasing <span class="hlt">protein</span> <span class="hlt">concentration</span> with increasing salt <span class="hlt">concentration</span>, presumably due to repulsive electrostatic interactions between <span class="hlt">proteins</span>. At high salt <span class="hlt">concentration</span>, the behavior depends on the nature of the salt. Sodium chloride has little effect on the L-L phase separation, but ammonium sulfate decreases the <span class="hlt">protein</span> <span class="hlt">concentration</span> at which the L-L phase separation occurs. This trend is attributed to the effects of critical fluctuations on depletion forces. The implications of these results for designing solution conditions optimal for <span class="hlt">protein</span> crystallization are discussed.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4608811','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4608811"><span id="translatedtitle">Accuracy and Reproducibility in Quantification of Plasma <span class="hlt">Protein</span> <span class="hlt">Concentrations</span> by Mass Spectrometry without the Use of Isotopic Standards</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Kramer, Gertjan; Woolerton, Yvonne; van Straalen, Jan P.; Vissers, Johannes P. C.; Dekker, Nick; Langridge, James I.; Beynon, Robert J.; Speijer, Dave; Sturk, Auguste; Aerts, Johannes M. F. G.</p> <p>2015-01-01</p> <p>Background Quantitative proteomic analysis with mass spectrometry holds great promise for simultaneously quantifying <span class="hlt">proteins</span> in various biosamples, such as human plasma. Thus far, studies addressing the reproducible measurement of endogenous <span class="hlt">protein</span> <span class="hlt">concentrations</span> in human plasma have focussed on targeted analyses employing isotopically labelled standards. Non-targeted proteomics, on the other hand, has been less employed to this end, even though it has been instrumental in discovery proteomics, generating large datasets in multiple fields of research. Results Using a non-targeted mass spectrometric assay (LCMSE), we quantified abundant plasma <span class="hlt">proteins</span> (43 mg/mL—40 ug/mL range) in human blood plasma specimens from 30 healthy volunteers and one blood serum sample (ProteomeXchange: PXD000347). Quantitative results were obtained by label-free mass spectrometry using a single internal standard to estimate <span class="hlt">protein</span> <span class="hlt">concentrations</span>. This approach resulted in quantitative results for 59 <span class="hlt">proteins</span> (cut off ≥11 samples quantified) of which 41 <span class="hlt">proteins</span> were quantified in all 31 samples and 23 of these with an inter-assay variability of ≤ 20%. Results for 7 apolipoproteins were compared with those obtained using isotope-labelled standards, while 12 <span class="hlt">proteins</span> were compared to routine immunoassays. Comparison of quantitative data obtained by LCMSE and immunoassays showed good to excellent correlations in relative <span class="hlt">protein</span> abundance (r = 0.72–0.96) and comparable median <span class="hlt">concentrations</span> for 8 out of 12 <span class="hlt">proteins</span> tested. Plasma <span class="hlt">concentrations</span> of 56 <span class="hlt">proteins</span> determined by LCMSE were of similar accuracy as those reported by targeted studies and 7 apolipoproteins quantified by isotope-labelled standards, when compared to reference <span class="hlt">concentrations</span> from literature. Conclusions This study shows that LCMSE offers good quantification of relative abundance as well as reasonable estimations of <span class="hlt">concentrations</span> of abundant plasma <span class="hlt">proteins</span>. PMID:26474480</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/23139249','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/23139249"><span id="translatedtitle">Association between use of specialty dietary supplements and C-reactive <span class="hlt">protein</span> <span class="hlt">concentrations</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Kantor, Elizabeth D; Lampe, Johanna W; Vaughan, Thomas L; Peters, Ulrike; Rehm, Colin D; White, Emily</p> <p>2012-12-01</p> <p>Laboratory evidence suggests that certain specialty dietary supplements have antiinflammatory properties, though evidence in humans remains limited. Data on a nationally representative sample of 9,947 adults from the 1999-2004 cycles of the National Health and Nutrition Examination Survey were used to assess the associations between specialty supplement use and inflammation, as measured by serum high-sensitivity C-reactive <span class="hlt">protein</span> (hs-CRP) <span class="hlt">concentration</span>. Using survey-weighted multivariate linear regression, significant reductions in hs-CRP <span class="hlt">concentrations</span> were associated with regular use of glucosamine (17%, 95% confidence interval (CI): 7, 26), chondroitin (22%, 95% CI: 8, 33), and fish oil (16%, 95% CI: 0.3, 29). No associations were observed between hs-CRP <span class="hlt">concentration</span> and regular use of supplements containing methylsulfonylmethane, garlic, ginkgo biloba, saw palmetto, or pycnogenol. These results suggest that glucosamine and chondroitin supplements are associated with reduced inflammation in humans and provide further evidence to support an inverse association between use of fish oil supplements and inflammation. It is important to further investigate the potential antiinflammatory role of these supplements, as there is a need to identify safe and effective ways to reduce inflammation and the burden of inflammation-related diseases such as cancer and cardiovascular disease.</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_12");'>12</a></li> <li><a href="#" onclick='return showDiv("page_13");'>13</a></li> <li class="active"><span>14</span></li> <li><a href="#" onclick='return showDiv("page_15");'>15</a></li> <li><a href="#" onclick='return showDiv("page_16");'>16</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_14 --> <div id="page_15" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_13");'>13</a></li> <li><a href="#" onclick='return showDiv("page_14");'>14</a></li> <li class="active"><span>15</span></li> <li><a href="#" onclick='return showDiv("page_16");'>16</a></li> <li><a href="#" onclick='return showDiv("page_17");'>17</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="281"> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27073847','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27073847"><span id="translatedtitle">Determinants of C-reactive <span class="hlt">protein</span> <span class="hlt">concentrations</span> in pregnant women with type 1 diabetes.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Gutaj, Paweł; Krzyżanowska, Patrycja; Brązert, Jacek; Wender-Ożegowska, Ewa</p> <p>2016-04-13</p> <p>INTRODUCTION    Increased C-reactive <span class="hlt">protein</span> (CRP) <span class="hlt">concentrations</span> during pregnancy are associated with several perinatal complications. OBJECTIVES    The aim of the study was to assess serum CRP <span class="hlt">concentrations</span> and identify its determinants in pregnant women with type 1 diabetes. PATIENTS AND METHODS    CRP <span class="hlt">concentrations</span> were determined using a high-sensitivity assay (hs-CRP) in the first trimester (I, week <12 of gestation), in mid-pregnancy (II, weeks 20 to 24 of gestation), and in the late third trimester (III, weeks 34 to 39 of gestation) in a group of 73 patients with type 1 diabetes. RESULTS    There was a significant increase in CRP <span class="hlt">concentrations</span> between the first trimester and mid‑pregnancy (median [interquartile range], 2.5 mg/l [1.3-4.5 mg/l] and 5.6 mg/l [2.5-11.6 mg/l]; P = 0.0001), which then stabilized with no further change between mid-pregnancy and the late third trimester (5.7 mg/l [2.5-9.6 mg/l]). CRP <span class="hlt">concentrations</span> in all 3 trimesters were positively correlated with the waist‑to-hip ratio (I, P <0.0001; II, P = 0.0004; III, P = 0.0369) and body mass index (I, P = 0.015; II, P = 0.0025; III, P = 0.0048), measured in the first trimester. CRP <span class="hlt">concentrations</span> during pregnancy were positively correlated with a measure of insulin resistance, namely, the estimated glucose disposal rate, assessed in the first trimester (I, P = 0.01; II, P = 0.0165; III, P = 0.0062). There was a positive correlation between the levels of hs-CRP and total cholesterol (P = 0.001), low-density lipoprotein cholesterol (P = 0.013), and triglycerides (P = 0.0014) in the first trimester. There was no significant correlation between CRP and hemoglobin A1c, daily insulin requirement/kg, high-density lipoprotein cholesterol levels, maternal age, and diabetes duration. CONCLUSIONS    Adiposity, abnormal body fat distribution, and insulin resistance are the major determinants of CRP <span class="hlt">concentrations</span> in pregnant women with type 1 diabetes. Our results confirm the</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://cfpub.epa.gov/si/si_public_record_report.cfm?dirEntryId=213575&keyword=wps&actType=&TIMSType=+&TIMSSubTypeID=&DEID=&epaNumber=&ntisID=&archiveStatus=Both&ombCat=Any&dateBeginCreated=&dateEndCreated=&dateBeginPublishedPresented=&dateEndPublishedPresented=&dateBeginUpdated=&dateEndUpdated=&dateBeginCompleted=&dateEndCompleted=&personID=&role=Any&journalID=&publisherID=&sortBy=revisionDate&count=50&CFID=80727729&CFTOKEN=34194884','EPA-EIMS'); return false;" href="http://cfpub.epa.gov/si/si_public_record_report.cfm?dirEntryId=213575&keyword=wps&actType=&TIMSType=+&TIMSSubTypeID=&DEID=&epaNumber=&ntisID=&archiveStatus=Both&ombCat=Any&dateBeginCreated=&dateEndCreated=&dateBeginPublishedPresented=&dateEndPublishedPresented=&dateBeginUpdated=&dateEndUpdated=&dateBeginCompleted=&dateEndCompleted=&personID=&role=Any&journalID=&publisherID=&sortBy=revisionDate&count=50&CFID=80727729&CFTOKEN=34194884"><span id="translatedtitle">Improved Strategies and Optimization of Calibration Models for Real-time PCR <span class="hlt">Absolute</span> Quantification</span></a></p> <p><a target="_blank" href="http://oaspub.epa.gov/eims/query.page">EPA Science Inventory</a></p> <p></p> <p></p> <p>Real-time PCR <span class="hlt">absolute</span> quantification applications rely on the use of standard curves to make estimates of DNA target <span class="hlt">concentrations</span> in unknown samples. Traditional <span class="hlt">absolute</span> quantification approaches dictate that a standard curve must accompany each experimental run. However, t...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26101619','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26101619"><span id="translatedtitle">Relevance of dietary <span class="hlt">protein</span> <span class="hlt">concentration</span> and quality as risk factors for the formation of calcium oxalate stones in cats.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Paßlack, Nadine; Burmeier, Hannes; Brenten, Thomas; Neumann, Konrad; Zentek, Jürgen</p> <p>2014-01-01</p> <p>The role of dietary <span class="hlt">protein</span> for the development of feline calcium oxalate (CaOx) uroliths has not been conclusively clarified. The present study evaluated the effects of a varying dietary <span class="hlt">protein</span> <span class="hlt">concentration</span> and quality on critical indices for the formation of CaOx uroliths. Three diets with a high <span class="hlt">protein</span> quality (10-11 % greaves meal/diet) and a varying crude <span class="hlt">protein</span> (CP) <span class="hlt">concentration</span> (35, 44 and 57 % in DM) were compared. Additionally, the 57 % CP diet was compared with a fourth diet that had a similar CP <span class="hlt">concentration</span> (55 % in DM), but a lower <span class="hlt">protein</span> quality (34 % greaves meal/diet). The Ca and oxalate (Ox) <span class="hlt">concentrations</span> were similar in all diets. A group of eight cats received the same diet at the same time. Each feeding period was divided into a 21 d adaptation period and a 7 d sampling period to collect urine. There were increases in urinary volume, urinary Ca <span class="hlt">concentrations</span>, renal Ca and Ox excretion and urinary relative supersaturation (RSS) with CaOx with increasing dietary <span class="hlt">protein</span> <span class="hlt">concentrations</span>. Urinary pH ranged between 6·34 and 6·66 among all groups, with no unidirectional effect of dietary <span class="hlt">protein</span>. Lower renal Ca excretion was observed when feeding the diet with the lower <span class="hlt">protein</span> quality, however, the underlying mechanism needs further evaluation. In conclusion, although the observed higher urinary volume is beneficial, the increase in urinary Ca <span class="hlt">concentrations</span>, renal Ca and Ox excretion and urinary RSS CaOx associated with a high-<span class="hlt">protein</span> diet may be critical for the development of CaOx uroliths in cats.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/14740818','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/14740818"><span id="translatedtitle">Use of dry milk <span class="hlt">protein</span> <span class="hlt">concentrate</span> in pizza cheese manufactured by culture or direct acidification.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Shakeel-Ur-Rehman; Farkye, N Y; Yim, B</p> <p>2003-12-01</p> <p>Milk <span class="hlt">protein</span> <span class="hlt">concentrate</span> (MPC) contains high <span class="hlt">concentrations</span> of casein and calcium and low <span class="hlt">concentrations</span> of lactose. Enrichment of cheese milk with MPC should, therefore, enhance yields and improve quality. The objectives of this study were: 1) to compare pizza cheese made by culture acidification using standardized whole milk (WM) plus skim milk (SM) versus WM plus MPC; and 2) compare cheese made using WM + MPC by culture acidification to that made by direct acidification. The experimental design is as follows: vat 1 = WM + SM + culture (commercial thermophilic lactic acid bacteria), vat 2 = WM + MPC + culture, and vat 3 = WM + MPC + direct acid (2% citric acid). Each cheese milk was standardized to a <span class="hlt">protein</span>-to-fat ratio of approximately 1.4. The experiment was repeated three times. Yield and composition of cheeses were determined by standard methods, whereas the proteolysis was assessed by urea polyacrylamide gel electrophoresis (PAGE) and water-soluble N contents. Meltability of the cheeses was determined during 1 mo of storage, in addition to pizza making. The addition of MPC improved the yields from 10.34 +/- 0.57% in vat 1 cheese to 14.50 +/- 0.84% and 16.65 +/- 2.23%, respectively, in vats 2 and 3 and cheeses. The percentage of fat and <span class="hlt">protein</span> recoveries showed insignificant differences between the treatments, but TS recoveries were in the order, vat 2 > vat 3 > vat 1. Most of the compositional parameters were significantly affected by the different treatments. Vat 2 cheese had the highest calcium and lowest lactose contencentrations. Vat 3 cheese had the best meltability. Vat 1 cheese initially had better meltability than vat 2 cheese; however, the difference became insignificant after 28 d of storage at 4 degrees C. Vat 3 cheese had the softest texture and produced large-sized blisters when baked on pizza. The lowest and highest levels of proteolysis were found in vats 2 and 3 cheeses, respectively. The study demonstrates the use of MPC in pizza cheese</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/biblio/22212535','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/biblio/22212535"><span id="translatedtitle">Effects of sub-lethal neurite outgrowth inhibitory <span class="hlt">concentrations</span> of chlorpyrifos oxon on cytoskeletal <span class="hlt">proteins</span> and acetylcholinesterase in differentiating N2a cells</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>Flaskos, J.; Nikolaidis, E.; Harris, W.; Sachana, M.; Hargreaves, A.J.</p> <p>2011-11-15</p> <p>Previous work in our laboratory has shown that sub-lethal <span class="hlt">concentrations</span> (1-10 {mu}M) of chlorpyrifos (CPF), diazinon (DZ) and diazinon oxon (DZO) inhibit the outgrowth of axon-like neurites in differentiating mouse N2a neuroblastoma cells concomitant with altered levels and/or phosphorylation state of axonal cytoskeleton and growth-associated <span class="hlt">proteins</span>. The aim of the present work was to determine whether chlorpyrifos oxon (CPO) was capable of inhibiting N2a cell differentiation in a similar manner. Using experimental conditions similar to our previous work, sub-lethal <span class="hlt">concentrations</span> (1-10 {mu}M) of CPO were found to inhibit N2a cell differentiation. However, unlike previous studies with DZ and DZO, there was a high level of sustained inhibition of acetylcholinesterase (AChE) in CPO treated cells. Impairment of neurite outgrowth was also associated with reduced levels of growth associated <span class="hlt">protein</span>-43 and neurofilament heavy chain (NFH), and the distribution of NFH in cells stained by indirect immunofluorescence was disrupted. However, in contrast to previous findings for DZO, the <span class="hlt">absolute</span> level of phosphorylated NFH was unaffected by CPO exposure. Taken together, the findings suggest that sub-lethal <span class="hlt">concentrations</span> of CPO inhibit axon outgrowth in differentiating N2a cells and that this effect involves reduced levels of two <span class="hlt">proteins</span> that play key roles in axon outgrowth and maintenance. Although the inhibition of neurite outgrowth is unlikely to involve AChE inhibition directly, further work will help to determine whether the persistent inhibition of AChE by CPO can account for the different effects induced by CPO and DZO on the levels of total and phosphorylated NFH. -- Highlights: Black-Right-Pointing-Pointer Sub-lethal levels of chlorpyrifos oxon inhibit neurite outgrowth in N2a cells Black-Right-Pointing-Pointer Acetylcholinesterase exhibits sustained inhibition throughout exposure Black-Right-Pointing-Pointer The levels of neurofilament heavy chain and GAP-43</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=5021069','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=5021069"><span id="translatedtitle">VITAMIN D–BINDING <span class="hlt">PROTEIN</span> IN HEALTHY PRE- AND POSTMENOPAUSAL WOMEN: RELATIONSHIP WITH ESTRADIOL <span class="hlt">CONCENTRATIONS</span></span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Pop, L. Claudia; Shapses, Sue A.; Chang, Brian; Sun, Wei; Wang, Xiangbing</p> <p>2016-01-01</p> <p>Objective To examine the relationship between endogenous serum estradiol and vitamin D–binding <span class="hlt">protein</span> (DBP) and total, free, and bioavailable 25-hydroxyvitamin D (25OHD) <span class="hlt">concentrations</span> in pre- and postmenopausal women. Methods In 165 healthy women (ages, 26 to 75 years) not taking any form of exogenous estrogen, the serum <span class="hlt">concentrations</span> of estradiol, 25OHD, DBP, parathyroid hormone, and albumin were measured. Free and bioavailable 25OHD (free + albumin-bound) levels were calculated from total 25OHD, DBP, and serum albumin levels. Results Premenopausal women had higher serum 25OHD (31.5 ± 7.9 ng/mL), DBP (45.3 ± 6.2 mg/dL), and estradiol (52.8 ± 35.0 pg/mL) levels than postmenopausal women (26.5 ± 4.9 ng/mL, 41.7 ± 5.7 mg/dL, and 12.9 ± 4.9 pg/mL), respectively. In addition, the calculated free and bioavailable 25OHD levels were higher in pre- than postmenopausal women (P<.05). Serum estradiol correlated with DBP (r = 0.22; P<.01) and total 25OHD (r = 0.27; P<.01). In multivariate regression models (with or without serum 25OHD), estradiol was independently associated with DBP (P<.05). Conclusion Lower estradiol level is one of the factors that contribute to lower DBP levels in older women. Our data indicate that besides well-known factors such as age, gender, and race, serum estradiol <span class="hlt">concentrations</span> are also a physiologic predictor of DBP <span class="hlt">concentration</span>. PMID:26121448</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/23927918','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/23927918"><span id="translatedtitle">Scale-up of the process to obtain functional ingredients based in plasma <span class="hlt">protein</span> <span class="hlt">concentrates</span> from porcine blood.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Parés, Dolors; Toldrà, Mònica; Saguer, Elena; Carretero, Carmen</p> <p>2014-01-01</p> <p>The feasibility of a scaled-up process to obtain two <span class="hlt">protein</span> <span class="hlt">concentrates</span> from porcine blood plasma, i.e. serum and albumin, for use as functional food ingredients was assessed. The process consisted of fractionating plasma <span class="hlt">proteins</span> by salting out, <span class="hlt">concentrating</span> and purifying fractions by means of membrane technology, and subsequently dehydrating through spray-drying. The fractionation process allowed a good isolation of the desired <span class="hlt">proteins</span>, which were then <span class="hlt">concentrated</span> and desalted in a tangential flow filtration (TFF) process combining ultra and diafiltration. Purification, pre-<span class="hlt">concentration</span> and dehydration were successfully achieved. The functional properties of dehydrated serum and albumin were determined. As compared to the same hemoderivatives obtained by a lab-scale production system, serum maintained the gelling properties; albumin exhibited similar foaming properties; and both serum and albumin <span class="hlt">concentrates</span> showed slightly improved emulsifying properties. PMID:23927918</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=246274','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=246274"><span id="translatedtitle">The Effect of Diet on <span class="hlt">Protein</span> <span class="hlt">Concentration</span>, Hypopharyngeal Gland Development and Virus Load in Worker Honey ees (Apis mellifera L.)</span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>Elucidating the mechanisms by which honey bees process pollen vs. <span class="hlt">protein</span> supplements are important in the generation of artificial diets needed to sustain managed honey bees. We measured the effects of diet on <span class="hlt">protein</span> <span class="hlt">concentration</span>, hypopharyngeal gland development and virus titers in worker honey...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=371431','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=371431"><span id="translatedtitle">Sex Steroid Modulation of Fatty Acid Utilization and Fatty Acid Binding <span class="hlt">Protein</span> <span class="hlt">Concentration</span> in Rat Liver</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Ockner, Robert K.; Lysenko, Nina; Manning, Joan A.; Monroe, Scott E.; Burnett, David A.</p> <p>1980-01-01</p> <p>The mechanism by which sex steroids influence very low density hepatic lipoprotein triglyceride production has not been fully elucidated. In previous studies we showed that [14C]oleate utilization and incorporation into triglycerides were greater in hepatocyte suspensions from adult female rats than from males. The sex differences were not related to activities of the enzymes of triglyceride biosynthesis, whereas fatty acid binding <span class="hlt">protein</span> (FABP) <span class="hlt">concentration</span> in liver cytosol was greater in females. These findings suggested that sex differences in lipoprotein could reflect a sex steroid influence on the availability of fatty acids for hepatocellular triglyceride biosynthesis. In the present studies, sex steroid effects on hepatocyte [14C]oleate utilization and FABP <span class="hlt">concentration</span> were investigated directly. Hepatocytes from immature (30-d-old) rats exhibited no sex differences in [14C]oleate utilization. With maturation, total [14C]oleate utilization and triglyceride biosynthesis increased moderately in female cells and decreased markedly in male cells; the profound sex differences in adults were maximal by age 60 d. Fatty acid oxidation was little affected. Rats were castrated at age 30 d, and received estradiol, testosterone, or no hormone until age 60 d, when hepatocyte [14C]oleate utilization was studied. Castration virtually eliminated maturational changes and blunted the sex differences in adults. Estradiol or testosterone largely reproduced the appropriate adult pattern of [14C]oleate utilization regardless of the genotypic sex of the treated animal. In immature females and males, total cytosolic FABP <span class="hlt">concentrations</span> were similar. In 60-d-old animals, there was a striking correlation among all groups (females, males, castrates, and hormone-treated) between mean cytosolic FABP <span class="hlt">concentration</span> on the one hand, and mean total [14C]oleate utilization (r = 0.91) and incorporation into triglycerides (r = 0.94) on the other. In 30-d-old animals rates of [14C</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3122448','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3122448"><span id="translatedtitle">Posaconazole in Human Serum: a Greater Pharmacodynamic Effect than Predicted by the Non-<span class="hlt">Protein</span>-Bound Serum <span class="hlt">Concentration</span> ▿</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Lignell, Anders; Löwdin, Elisabeth; Cars, Otto; Chryssanthou, Erja; Sjölin, Jan</p> <p>2011-01-01</p> <p>It is generally accepted that only the unbound fraction of a drug is pharmacologically active. Posaconazole is an antifungal agent with a <span class="hlt">protein</span> binding of 98 to 99%. Taking into account the degree of <span class="hlt">protein</span> binding, plasma levels in patients, and MIC levels of susceptible strains, it can be assumed that the free <span class="hlt">concentration</span> of posaconazole sometimes will be too low to exert the expected antifungal effect. The aim was therefore to test the activity of posaconazole in serum in comparison with that of the calculated unbound <span class="hlt">concentrations</span> in <span class="hlt">protein</span>-free media. Significant differences (P < 0.05) from the serum control were found at serum <span class="hlt">concentrations</span> of posaconazole of 1.0 and 0.10 mg/liter, with calculated free <span class="hlt">concentrations</span> corresponding to 1× MIC and 0.1× MIC, respectively, against one Candida lusitaniae strain selected for proof of principle. In RPMI 1640, the corresponding calculated unbound <span class="hlt">concentration</span> of 0.015 mg/liter resulted in a significant effect, whereas that of 0.0015 mg/liter did not. Also, against seven additional Candida strains tested, there was an effect of the low posaconazole <span class="hlt">concentration</span> in serum, in contrast to the results in RPMI 1640. Fluconazole, a low-grade-<span class="hlt">protein</span>-bound antifungal, was used for comparison at corresponding <span class="hlt">concentrations</span> in serum and RPMI 1640. No effect was observed at the serum <span class="hlt">concentration</span>, resulting in a calculated unbound <span class="hlt">concentration</span> of 0.1× MIC. In summary, there was a substantially greater pharmacodynamic effect of posaconazole in human serum than could be predicted by the non-<span class="hlt">protein</span>-bound serum <span class="hlt">concentration</span>. A flux from serum <span class="hlt">protein</span>-bound to fungal lanosterol 14α-demethylase-bound posaconazole is suggested. PMID:21502622</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26814439','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26814439"><span id="translatedtitle">Preparation and Characterization of Nanocomposites from Whey <span class="hlt">Protein</span> <span class="hlt">Concentrate</span> Activated with Lycopene.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Pereira, Rafaela Corrêa; de Deus Souza Carneiro, João; Borges, Soraia Vilela; Assis, Odílio Benedito Garrido; Alvarenga, Gabriela Lara</p> <p>2016-03-01</p> <p>The production and characterization of nanocomposites based on whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) and montmorilonite (MMT) incorporated with lycopene as a functional substance is presented and discussed as an alternative biomaterial for potential uses in foodstuff applications. A full factorial design with varying levels of MMT (0% and 2% in w/w) and lycopene (0%, 6%, and 12% in w/w) was used. Color, light transmission, film transparency, moisture, density, solubility, water vapor permeability, and antioxidant activity of the resulting materials were evaluated. Results indicated that lycopene and MMT nanoparticles were successfully included in WPC films using the casting/evaporation method. Inclusion of 2% w/w of MMT in the polymeric matrix significantly improved barrier property against water vapor. Lycopene, besides its good red coloring ability, provided to the films antioxidant activity and UV-vis light protection. These findings open a new perspective for the use of materials for bioactive packaging applications. PMID:26814439</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26505877','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26505877"><span id="translatedtitle">Unusual dynamics of <span class="hlt">concentration</span> fluctuations in solutions of weakly attractive globular <span class="hlt">proteins</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Bucciarelli, Saskia; Casal-Dujat, Lucía; De Michele, Cristiano; Sciortino, Francesco; Dhont, Jan; Bergenholtz, Johan; Farago, Bela; Schurtenberger, Peter; Stradner, Anna</p> <p>2015-11-19</p> <p>The globular <span class="hlt">protein</span> γB-crystallin exhibits a complex phase behavior, where liquid-liquid phase separation characterized by a critical volume fraction ϕc = 0.154 and a critical temperature Tc = 291.8 K coexists with dynamical arrest on all length scales at volume fractions around ϕ ≈ 0.3-0.35, and an arrest line that extends well into the unstable region below the spinodal. However, although the static properties such as the osmotic compressibility and the static correlation length are in quantitative agreement with predictions for binary liquid mixtures, this is not the case for the dynamics of <span class="hlt">concentration</span> fluctuations described by the dynamic structure factor S(q,t). Using a combination of dynamic light scattering and neutron spin echo measurements, we demonstrate that the competition between critical slowing down and dynamical arrest results in a much more complex wave vector dependence of S(q,t) than previously anticipated.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26814439','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26814439"><span id="translatedtitle">Preparation and Characterization of Nanocomposites from Whey <span class="hlt">Protein</span> <span class="hlt">Concentrate</span> Activated with Lycopene.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Pereira, Rafaela Corrêa; de Deus Souza Carneiro, João; Borges, Soraia Vilela; Assis, Odílio Benedito Garrido; Alvarenga, Gabriela Lara</p> <p>2016-03-01</p> <p>The production and characterization of nanocomposites based on whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) and montmorilonite (MMT) incorporated with lycopene as a functional substance is presented and discussed as an alternative biomaterial for potential uses in foodstuff applications. A full factorial design with varying levels of MMT (0% and 2% in w/w) and lycopene (0%, 6%, and 12% in w/w) was used. Color, light transmission, film transparency, moisture, density, solubility, water vapor permeability, and antioxidant activity of the resulting materials were evaluated. Results indicated that lycopene and MMT nanoparticles were successfully included in WPC films using the casting/evaporation method. Inclusion of 2% w/w of MMT in the polymeric matrix significantly improved barrier property against water vapor. Lycopene, besides its good red coloring ability, provided to the films antioxidant activity and UV-vis light protection. These findings open a new perspective for the use of materials for bioactive packaging applications.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/biblio/6010102','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/biblio/6010102"><span id="translatedtitle">Alcohol and single-cell <span class="hlt">protein</span> production by Kluyveromyces in <span class="hlt">concentrated</span> whey permeates with reduced ash</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>Mahmoud, M.M.; Kosikowski, F.V.</p> <p>1982-01-01</p> <p>Five Kluyveromyces yeasts were grown in <span class="hlt">concentrated</span> whey permeates under aerobic and anaerobic conditions to produce single-cell <span class="hlt">protein</span> and ethanol. K. fragilis NRRL Y2415 produced the highest yield of alcohol, 9.1%, and K. bulgaricus ATCC 1605 gave the highest yield of biomass, 13.5 mg/mL. High ash, apparently through Na and K effects, inhibited production of biomass and alcohol. A 0.77% ash was optimum. Lactose utilization was more rapid under aerobic than anaerobic conditions. (NH/sub 4/)/sub 2/SO/sub 4/ and urea supplementation were without effect on yeast growth or were slightly inhibitory. A 1% peptone inclusion gave the highest biomass yield with minimum alcohol production.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26505877','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26505877"><span id="translatedtitle">Unusual dynamics of <span class="hlt">concentration</span> fluctuations in solutions of weakly attractive globular <span class="hlt">proteins</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Bucciarelli, Saskia; Casal-Dujat, Lucía; De Michele, Cristiano; Sciortino, Francesco; Dhont, Jan; Bergenholtz, Johan; Farago, Bela; Schurtenberger, Peter; Stradner, Anna</p> <p>2015-11-19</p> <p>The globular <span class="hlt">protein</span> γB-crystallin exhibits a complex phase behavior, where liquid-liquid phase separation characterized by a critical volume fraction ϕc = 0.154 and a critical temperature Tc = 291.8 K coexists with dynamical arrest on all length scales at volume fractions around ϕ ≈ 0.3-0.35, and an arrest line that extends well into the unstable region below the spinodal. However, although the static properties such as the osmotic compressibility and the static correlation length are in quantitative agreement with predictions for binary liquid mixtures, this is not the case for the dynamics of <span class="hlt">concentration</span> fluctuations described by the dynamic structure factor S(q,t). Using a combination of dynamic light scattering and neutron spin echo measurements, we demonstrate that the competition between critical slowing down and dynamical arrest results in a much more complex wave vector dependence of S(q,t) than previously anticipated. PMID:26505877</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/22314906','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/22314906"><span id="translatedtitle">Effect of diet of varying <span class="hlt">protein</span> <span class="hlt">concentrations</span> on the activity of erythrocyte membrane Ca2+Mg2+ ATPase in dogs.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Adewoye, E O; Ige, A O; Adeyanju, O; Bekibele, E B</p> <p>2010-11-25</p> <p>Alterations in <span class="hlt">protein</span> diet have been reported to result in alterations in calcium homeostasis in the body. Ca2+Mg2+ATPase is an ubiquitous enzyme important in calcium homeostasis in the body. The effect of varying <span class="hlt">protein</span> diet on the activities of Ca2+ pump across cell membranes is however yet to be fully elucidated. In this study, the activity of erythrocyte membrane calcium pump in response to varying <span class="hlt">protein</span> <span class="hlt">concentration</span> in diet was therefore studied in the dog. The study was carried out in 24 dogs, randomly divided into 4 groups. The groups were fed with diets containing 30%, 26%, 16% and 0% <span class="hlt">proteins</span> (high, medium, low and zero) for six weeks respectively. Blood samples were collected from each animal to determine packed cell volumes, hematocrit, blood urea, electrolyte studies and erythrocyte ghost membrane studies. The effects of Ca2+ and ATP on the activity of Ca2+Mg2+ ATPase were determined in the isolated ghost membrane. The result of the study shows that there was a <span class="hlt">protein</span> diet dependent increase in the activity of Ca2+Mg2+ ATPase in the presence and absence of ATP in all the groups with the highest activity recorded in the high <span class="hlt">protein</span> diet group and the lowest activity observed in the zero <span class="hlt">protein</span> group. There was also a <span class="hlt">protein</span> diet dependent increase in the <span class="hlt">protein</span> <span class="hlt">concentration</span> of the membranes in all groups observed with the highest <span class="hlt">protein</span> <span class="hlt">concentration</span> recorded in the high <span class="hlt">protein</span> diet group and the lowest activity observed in the zero <span class="hlt">protein</span> group. There was a significant decrease in K+ <span class="hlt">concentration</span> (P <0.05) and a significant increase in urea <span class="hlt">concentration</span> of animals fed with high <span class="hlt">protein</span> diet (P <0.05). There was also a significant increase (P <0.05) in HCO3- <span class="hlt">concentration</span> in the animals fed with medium <span class="hlt">protein</span> diet and no significant difference in the PCV and heamatocrit values in all groups. This study has shown that high <span class="hlt">protein</span> diets increase the activity of the Ca2+Mg2+ ATPase in the presence and absence of ATP.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3837907','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3837907"><span id="translatedtitle"><span class="hlt">Protein</span> Binding of β-Lactam Antibiotics in Critically Ill Patients: Can We Successfully Predict Unbound <span class="hlt">Concentrations</span>?</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Wong, Gloria; Briscoe, Scott; Adnan, Syamhanin; McWhinney, Brett; Ungerer, Jacobus; Lipman, Jeffrey</p> <p>2013-01-01</p> <p>The use of therapeutic drug monitoring (TDM) to optimize beta-lactam dosing in critically ill patients is growing in popularity, although there are limited data describing the potential impact of altered <span class="hlt">protein</span> binding on achievement of target <span class="hlt">concentrations</span>. The aim of this study was to compare the measured unbound <span class="hlt">concentration</span> to the unbound <span class="hlt">concentration</span> predicted from published <span class="hlt">protein</span> binding values for seven beta-lactams using data from blood samples obtained from critically ill patients. From 161 eligible patients, we obtained 228 and 220 plasma samples at the midpoint of the dosing interval and trough, respectively, for ceftriaxone, cefazolin, meropenem, piperacillin, ampicillin, benzylpenicillin, and flucloxacillin. The total and unbound beta-lactam <span class="hlt">concentrations</span> were measured using validated methods. Variabilities in both unbound and total <span class="hlt">concentrations</span> were marked for all antibiotics, with significant differences being present between measured and predicted unbound <span class="hlt">concentrations</span> for ceftriaxone and for flucloxacillin at the mid-dosing interval (P < 0.05). The predictive performance for calculating unbound <span class="hlt">concentrations</span> using published <span class="hlt">protein</span> binding values was poor, with bias for overprediction of unbound <span class="hlt">concentrations</span> for ceftriaxone (83.3%), flucloxacillin (56.8%), and benzylpenicillin (25%) and underprediction for meropenem (12.1%). Linear correlations between the measured total and unbound <span class="hlt">concentrations</span> were observed for all beta-lactams (R2 = 0.81 to 1.00; P < 0.05) except ceftriaxone and flucloxacillin. The percent <span class="hlt">protein</span> binding of flucloxacillin and the plasma albumin <span class="hlt">concentration</span> were also found to be linearly correlated (R2 = 0.776; P < 0.01). In conclusion, significant differences between measured and predicted unbound drug <span class="hlt">concentrations</span> were found only for the highly <span class="hlt">protein</span>-bound beta-lactams ceftriaxone and flucloxacillin. However, direct measurement of unbound drug in research and clinical practice is suggested for selected</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/15298756','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/15298756"><span id="translatedtitle">Effect of chickpea aqueous extracts, organic extracts, and <span class="hlt">protein</span> <span class="hlt">concentrates</span> on cell proliferation.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Girón-Calle, Julio; Vioque, Javier; del Mar Yust, María; Pedroche, Justo; Alaiz, Manuel; Millán, Francisco</p> <p>2004-01-01</p> <p>Pulses should be part of a healthy diet, and it is also becoming clear that they have health-promoting effects. Nevertheless, most studies on the bioactive or health-promoting properties of pulses have been carried out using soybeans. We have studied cell growth-regulating properties, which may be responsible for anti-cancer properties, in chickpea seeds. Chickpea seeds are a staple in the traditional diet of many Mediterranean, Asian, and South and Central American countries. In addition, chickpea seeds have industrial applications since they can be used for the preparation of <span class="hlt">protein</span> <span class="hlt">concentrates</span> and isolates. The cell lines Caco-2 (epithelial intestinal) and J774 (macrophages) have been exposed to chickpea seed extracts and <span class="hlt">protein</span> preparations in order to screen the different chickpea fractions for effects on cell growth. Both cell growth-promoting and cell growth-inhibiting effects were found. Most interestingly, a fraction soluble in ethanol and acetone specifically and almost completely inhibited the growth of Caco-2 cells exhibiting a cancerous phenotype. It is concluded that chickpea seeds are a source of bioactive components and deserve further study for their possible anti-cancer effect.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27022878','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27022878"><span id="translatedtitle">Whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> doped electrospun poly(epsilon-caprolactone) fibers for antibiotic release improvement.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Ahmed, Said Mahmoud; Ahmed, Hanaa; Tian, Chang; Tu, Qin; Guo, Yadan; Wang, Jinyi</p> <p>2016-07-01</p> <p>Design and fabrication of scaffolds using appropriate biomaterials are a key step for the creation of functionally engineered tissues and their clinical applications. Poly(epsilon-caprolactone) (PCL), a biodegradable and biocompatible material with negligible cytotoxicity, is widely used to fabricate nanofiber scaffolds by electrospinning for the applications of pharmaceutical products and wound dressings. However, the use of PCL as such in tissue engineering is limited due to its poor bioregulatory activity, high hydrophobicity, lack of functional groups and neutral charge. With the attempt to found nanofiber scaffolds with antibacterial activity for skin tissue engineering, in this study, whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) was used to modify the PCL nanofibers by doping it in the PCL electrospun solution. By adding <span class="hlt">proteins</span> into PCL nanofibers, the degradability of the fibers may be increased, and this further allows an antibiotic incorporated in the fibers to be efficiently released. The morphology, wettability and degradation of the as-prepared PCL/WPC nanofibers were carefully characterized. The results showed that the PCL/WPC nanofibers possessed good morphology and wettability, as well as high degradation ability to compare with the pristine PCL fibers. Afterwords, tetracycline hydrochloride as a model antibiotic drug was doped in the PCL/WPC nanofibers. In vitro drug release assays demonstrated that PCL/WPC nanofibers had higher antibiotic release capability than the PCL nanofibers. Also, antibacterial activity evaluation against various bacteria showed that the drug-doped PCL/WPC fibers possessed more efficient antibacterial activity than the PCL nanofibers. PMID:27022878</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/24804041','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/24804041"><span id="translatedtitle">Sensorial evolution of cassava flour (Manihot esculenta crantz) added to <span class="hlt">protein</span> <span class="hlt">concentrate</span> cassava leaves.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Lima, Elaine C S; Feijo, Márcia B S; Freitas, Maria C J; Dos Santos, Edna R; Sabaa-Srur, Armando U O; Moura, Luciana S M</p> <p>2013-09-01</p> <p>Cassava is regarded as the nutritional base of populations in developing countries, and flour, product made of cassava, is the most consumed in the world. The cassava leaves are very rich in vegetable <span class="hlt">proteins</span>, but a big amount is lost in processing the crop. The objective of this study was to do a sensory evaluation of cassava flour to which a <span class="hlt">protein</span> <span class="hlt">concentrate</span> obtained from cassava leaves (CPML) was added. The CPML was obtained from cassava leaves by isoelectric precipitation and added to cassava paste for preparation of flour in three parts 2.5, 5, and 10%. The acceptance test was done by 93 consumers of flour, using hedonic scale of 7 points to evaluate characteristics like color, scent, flavor, bitterness, texture, and overall score. By the method of quantitative descriptive analysis (QDA), eight trained tasters evaluated the following characteristics: whitish color, greenish color, cassava flavor, bitter flavor, characteristic flavor, lumpiness, raw texture, leaf scent, and cassava scent. The acceptability test indicated that flour cassava with 2.5 was preferred. Whitish color, greenish color, cassava flavor, bitter flavor, salty flavor, characteristic flavor, lumpiness texture, raw texture, and the smell of the leaves and cassava flour were the main descriptors defined for flour cassava with CPML has better characteristics.</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_13");'>13</a></li> <li><a href="#" onclick='return showDiv("page_14");'>14</a></li> <li class="active"><span>15</span></li> <li><a href="#" onclick='return showDiv("page_16");'>16</a></li> <li><a href="#" onclick='return showDiv("page_17");'>17</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_15 --> <div id="page_16" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_14");'>14</a></li> <li><a href="#" onclick='return showDiv("page_15");'>15</a></li> <li class="active"><span>16</span></li> <li><a href="#" onclick='return showDiv("page_17");'>17</a></li> <li><a href="#" onclick='return showDiv("page_18");'>18</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="301"> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4470098','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4470098"><span id="translatedtitle">Circulating resistin <span class="hlt">protein</span> and mRNA <span class="hlt">concentrations</span> and clinical severity of coronary artery disease</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Sopic, Miron; Spasojevic-Kalimanovska, Vesna; Kalimanovska-Ostric, Dimitra; Andjelkovic, Kristina; Jelic-Ivanovic, Zorana</p> <p>2015-01-01</p> <p>Introduction Previous studies have implicated a strong link between circulating plasma resistin and coronary artery disease (CAD). The aim of this study was to evaluate the differences in peripheral blood mononuclear cells (PBMC) resistin mRNA and its plasma <span class="hlt">protein</span> <span class="hlt">concentrations</span> between the patients with CAD of different clinical severity. Material and methods This study included 33 healthy subjects as the control group (CG) and 77 patients requiring coronary angiography. Of the latter 30 was CAD negative whereas 47 were CAD positive [18 with stable angina pectoris (SAP) and 29 with acute coronary syndrome (ACS)]. Circulating resistin was measured by ELISA; PBMC resistin mRNA was determined by real-time PCR. Results Resistin <span class="hlt">protein</span> was significantly higher in the ACS group compared to the CG (P = 0.001) and the CAD negative group (P = 0.018). Resistin mRNA expression did not vary across the study groups, despite the positive correlation seen with plasma resistin (ρ = 0.305, P = 0.008). In patients, plasma resistin and PBMC resistin mRNA negatively correlated with HDL-C (ρ = -0.404, P < 0.001 and ρ = -0.257, P = 0.032, respectively). Furthermore, the highest plasma resistin tertile showed the lowest HDL-C (P = 0.006). Plasma resistin was positively associated with serum creatinine (ρ = 0.353, P = 0.002). Conclusion Significant increase of plasma resistin in patients with ACS compared to CG and CAD negative patients was observed. Despite no change in PBMC resistin mRNA in different disease conditions a positive association between resistin mRNA and resistin plasma <span class="hlt">protein</span> was evident. Both plasma resistin and PBMC resistin mRNA were negatively associated with plasma HDL-C, and plasma resistin positively with serum creatinine. PMID:26110037</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26188582','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26188582"><span id="translatedtitle">The effect of microfiltration on color, flavor, and functionality of 80% whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Qiu, Y; Smith, T J; Foegeding, E A; Drake, M A</p> <p>2015-09-01</p> <p>The residual annatto colorant in fluid Cheddar cheese whey is bleached to provide a neutral-colored final product. Currently, hydrogen peroxide (HP) and benzoyl peroxide are used for bleaching liquid whey. However, previous studies have shown that chemical bleaching causes off-flavor formation, mainly due to lipid oxidation and <span class="hlt">protein</span> degradation. The objective of this study was to evaluate the efficacy of microfiltration (MF) on norbixin removal and to compare flavor and functionality of 80% whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC80) from MF whey to WPC80 from whey bleached with HP or lactoperoxidase (LP). Cheddar cheese whey was manufactured from colored, pasteurized milk. The fluid whey was pasteurized and fat separated. Liquid whey was subjected to 4 different treatments: control (no bleaching; 50°C, 1 h), HP (250 mg of HP/kg; 50°C, 1 h), and LP (20 mg of HP/kg; 50°C, 1 h), or MF (microfiltration; 50°C, 1 h). The treated whey was then ultrafiltered, diafiltered, and spray-dried to 80% <span class="hlt">concentrate</span>. The entire experiment was replicated 3 times. Proximate analyses, color, functionality, descriptive sensory and instrumental volatile analysis were conducted on WPC80. The MF and HP- and LP-bleached WPC80 displayed a 39.5, 40.9, and 92.8% norbixin decrease, respectively. The HP and LP WPC80 had higher cardboard flavors and distinct cabbage flavor compared with the unbleached and MF WPC80. Volatile compound results were consistent with sensory results. The HP and LP WPC80 were higher in lipid oxidation compounds (especially heptanal, hexanal, pentanal, 1-hexen-3-one, 2-pentylfuran, and octanal) compared with unbleached and MF WPC80. All WPC80 had >85% solubility across the pH range of 3 to 7. The microstructure of MF gels determined by confocal laser scanning showed an increased <span class="hlt">protein</span> particle size in the gel network. MF WPC80 also had larger storage modulus values, indicating higher gel firmness. Based on bleaching efficacy comparable to chemical bleaching with HP</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26454287','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26454287"><span id="translatedtitle">Partial calcium depletion during membrane filtration affects gelation of reconstituted milk <span class="hlt">protein</span> <span class="hlt">concentrates</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Eshpari, H; Jimenez-Flores, R; Tong, P S; Corredig, M</p> <p>2015-12-01</p> <p>Milk <span class="hlt">protein</span> <span class="hlt">concentrate</span> powders (MPC) with improved rehydration properties are often manufactured using processing steps, such as acidification and high-pressure processing, and with addition of other ingredients, such as sodium chloride, during their production. These steps are known to increase the amount of serum caseins or modify the mineral equilibrium, hence improving solubility of the retentates. The processing functionality of the micelles may be affected. The aim of this study was to investigate the effects of partial acidification by adding glucono-δ-lactone (GDL) to skim milk during membrane filtration on the structural changes of the casein micelles by observing their chymosin-induced coagulation behavior, as such coagulation is affected by both the supramolecular structure of the caseins and calcium equilibrium. Milk <span class="hlt">protein</span> <span class="hlt">concentrates</span> were prepared by preacidification with GDL to pH 6 using ultrafiltration (UF) and diafiltration (DF) followed by spray-drying. Reconstituted UF and DF samples (3.2% <span class="hlt">protein</span>) treated with GDL showed significantly increased amounts of soluble calcium and nonsedimentable caseins compared with their respective controls, as measured by ion chromatography and sodium dodecyl sulfate-PAGE electrophoresis, respectively. The primary phase of chymosin-induced gelation was not significantly different between treatments as measured by the amount of caseino-macropeptide released. The rheological properties of the reconstituted MPC powders were determined immediately after addition of chymosin, both before and after dialysis against skim milk, to ensure similar serum composition for all samples. Reconstituted samples before dialysis showed no gelation (defined as tan δ=1), and after re-equilibration only control UF and DF samples showed gelation. The gelation properties of reconstituted MPC powders were negatively affected by the presence of soluble casein, and positively affected by the amount of both soluble and insoluble</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26188582','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26188582"><span id="translatedtitle">The effect of microfiltration on color, flavor, and functionality of 80% whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Qiu, Y; Smith, T J; Foegeding, E A; Drake, M A</p> <p>2015-09-01</p> <p>The residual annatto colorant in fluid Cheddar cheese whey is bleached to provide a neutral-colored final product. Currently, hydrogen peroxide (HP) and benzoyl peroxide are used for bleaching liquid whey. However, previous studies have shown that chemical bleaching causes off-flavor formation, mainly due to lipid oxidation and <span class="hlt">protein</span> degradation. The objective of this study was to evaluate the efficacy of microfiltration (MF) on norbixin removal and to compare flavor and functionality of 80% whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC80) from MF whey to WPC80 from whey bleached with HP or lactoperoxidase (LP). Cheddar cheese whey was manufactured from colored, pasteurized milk. The fluid whey was pasteurized and fat separated. Liquid whey was subjected to 4 different treatments: control (no bleaching; 50°C, 1 h), HP (250 mg of HP/kg; 50°C, 1 h), and LP (20 mg of HP/kg; 50°C, 1 h), or MF (microfiltration; 50°C, 1 h). The treated whey was then ultrafiltered, diafiltered, and spray-dried to 80% <span class="hlt">concentrate</span>. The entire experiment was replicated 3 times. Proximate analyses, color, functionality, descriptive sensory and instrumental volatile analysis were conducted on WPC80. The MF and HP- and LP-bleached WPC80 displayed a 39.5, 40.9, and 92.8% norbixin decrease, respectively. The HP and LP WPC80 had higher cardboard flavors and distinct cabbage flavor compared with the unbleached and MF WPC80. Volatile compound results were consistent with sensory results. The HP and LP WPC80 were higher in lipid oxidation compounds (especially heptanal, hexanal, pentanal, 1-hexen-3-one, 2-pentylfuran, and octanal) compared with unbleached and MF WPC80. All WPC80 had >85% solubility across the pH range of 3 to 7. The microstructure of MF gels determined by confocal laser scanning showed an increased <span class="hlt">protein</span> particle size in the gel network. MF WPC80 also had larger storage modulus values, indicating higher gel firmness. Based on bleaching efficacy comparable to chemical bleaching with HP</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/22612922','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/22612922"><span id="translatedtitle">Effect of bleaching whey on sensory and functional properties of 80% whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Jervis, S; Campbell, R; Wojciechowski, K L; Foegeding, E A; Drake, M A; Barbano, D M</p> <p>2012-06-01</p> <p>Whey is a highly functional food that has found widespread use in a variety of food and beverage applications. A large amount of the whey <span class="hlt">proteins</span> produced in the United States is derived from annatto-colored Cheddar cheese. Color from annatto is undesirable in whey and must be bleached. The objective of this study was to compare 2 commercially approved bleaching agents, benzoyl peroxide (BP) and hydrogen peroxide (HP), and their effects on the flavor and functionality of 80% whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC80). Colored and uncolored liquid wheys were bleached with BP or HP, and then ultrafiltered, diafiltered, and spray-dried; WPC80 from unbleached colored and uncolored Cheddar whey were manufactured as controls. All treatments were manufactured in triplicate. The WPC80 were then assessed by sensory, instrumental, functionality, color, and proximate analysis techniques. The HP-bleached WPC80 were higher in lipid oxidation compounds (specifically hexanal, heptanal, octanal, nonanal, decanal, dimethyl disulfide, and 1-octen-3-one) and had higher fatty and cardboard flavors compared with the other unbleached and BP-bleached WPC80. The WPC80 bleached with BP had lower norbixin <span class="hlt">concentrations</span> compared with WPC80 bleached with HP. The WPC powders differed in Hunter color values (L, a, b), with bleached powders being more white, less red, and less yellow than unbleached powders. Bleaching with BP under the conditions used in this study resulted in larger reductions in yellowness of the powders made from whey with annatto color than did bleaching with HP. Functionality testing demonstrated that whey bleached with HP treatments had more soluble <span class="hlt">protein</span> after 10 min of heating at 90°C at pH 4.6 and pH 7 than the no-bleach and BP treatments, regardless of additional color. Overall, HP bleaching caused more lipid oxidation products and subsequent off-flavors compared with BP bleaching. However, heat stability of WPC80 was enhanced by HP bleaching compared with control or BP</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2453621','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2453621"><span id="translatedtitle">Circulating Retinol-Binding <span class="hlt">Protein</span>-4 <span class="hlt">Concentration</span> Might Reflect Insulin Resistance–Associated Iron Overload</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Fernández-Real, José Manuel; Moreno, José María; Ricart, Wifredo</p> <p>2008-01-01</p> <p>OBJECTIVES—The mechanisms behind the association between retinol-binding <span class="hlt">protein</span>-4 (RBP4) and insulin resistance are not well understood. An interaction between iron and vitamin A status, of which RBP4 is a surrogate, has long been recognized. We hypothesized that iron-associated insulin resistance could be behind the impaired insulin action caused by RBP4. RESEARCH DESIGN AND METHODS—Serum ferritin and RBP4 <span class="hlt">concentration</span> and insulin resistance were evaluated in a sample of middle-aged men (n = 132) and in a replication independent study. Serum RBP4 was also studied before and after iron depletion in patients with type 2 diabetes. Finally, the effect of iron on RBP4 release was evaluated in vitro in adipose tissue. RESULTS—A positive correlation between circulating RBP4 and log serum ferritin (r = 0.35 and r = 0.61, respectively; P < 0.0001) was observed in both independent studies. Serum RBP4 <span class="hlt">concentration</span> was higher in men than women in parallel to increased ferritin levels. On multiple regression analyses to predict serum RBP4, log serum ferritin contributed significantly to RBP4 variance after controlling for BMI, age, and homeostasis model assessment value. Serum RBP4 <span class="hlt">concentration</span> decreased after iron depletion in type 2 diabetic patients (percent mean difference −13.7 [95% CI −25.4 to −2.04]; P = 0.024). The iron donor lactoferrin led to increased dose-dependent adipose tissue release of RBP4 (2.4-fold, P = 0.005) and increased RBP4 expression, while apotransferrin and deferoxamine led to decreased RBP4 release. CONCLUSIONS—The relationship between circulating RBP4 and iron stores, both cross-sectional and after iron depletion, and in vitro findings suggest that iron could play a role in the RBP4–insulin resistance relationship. PMID:18426863</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://ntrs.nasa.gov/search.jsp?R=19720059878&hterms=rights+author&qs=Ntx%3Dmode%2Bmatchall%26Ntk%3DAll%26N%3D0%26No%3D80%26Ntt%3Drights%2Bauthor','NASA-TRS'); return false;" href="http://ntrs.nasa.gov/search.jsp?R=19720059878&hterms=rights+author&qs=Ntx%3Dmode%2Bmatchall%26Ntk%3DAll%26N%3D0%26No%3D80%26Ntt%3Drights%2Bauthor"><span id="translatedtitle">Singular perturbation of <span class="hlt">absolute</span> stability.</span></a></p> <p><a target="_blank" href="http://ntrs.nasa.gov/search.jsp">NASA Technical Reports Server (NTRS)</a></p> <p>Siljak, D. D.</p> <p>1972-01-01</p> <p>It was previously shown (author, 1969) that the regions of <span class="hlt">absolute</span> stability in the parameter space can be determined when the parameters appear on the right-hand side of the system equations, i.e., the regular case. Here, the effect on <span class="hlt">absolute</span> stability of a small parameter attached to higher derivatives in the equations (the singular case) is studied. The Lur'e-Postnikov class of nonlinear systems is considered.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26235579','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26235579"><span id="translatedtitle">Increased Milk <span class="hlt">Protein</span> <span class="hlt">Concentration</span> in a Rehydration Drink Enhances Fluid Retention Caused by Water Reabsorption in Rats.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Ito, Kentaro; Saito, Yuri; Ashida, Kinya; Yamaji, Taketo; Itoh, Hiroyuki; Oda, Munehiro</p> <p>2015-01-01</p> <p>A fluid-retention effect is required for beverages that are designed to prevent dehydration. That is, fluid absorbed from the intestines should not be excreted quickly; long-term retention is desirable. Here, we focused on the effect of milk <span class="hlt">protein</span> on fluid retention, and propose a new effective oral rehydration method that can be used daily for preventing dehydration. We first evaluated the effects of different <span class="hlt">concentrations</span> of milk <span class="hlt">protein</span> on fluid retention by measuring the urinary volumes of rats fed fluid containing milk <span class="hlt">protein</span> at <span class="hlt">concentrations</span> of 1, 5, and 10%. We next compared the fluid-retention effect of milk <span class="hlt">protein</span>-enriched drink (MPD) with those of distilled water (DW) and a sports drink (SD) by the same method. Third, to investigate the mechanism of fluid retention, we measured plasma insulin changes in rats after ingesting these three drinks. We found that the addition of milk <span class="hlt">protein</span> at 5 or 10% reduced urinary volume in a dose-dependent manner. Ingestion of the MPD containing 4.6% milk <span class="hlt">protein</span> resulted in lower urinary volumes than DW and SD. MPD also showed a higher water reabsorption rate in the kidneys and higher <span class="hlt">concentrations</span> of plasma insulin than DW and SD. These results suggest that increasing milk <span class="hlt">protein</span> <span class="hlt">concentration</span> in a beverage enhances fluid retention, which may allow the possibility to develop rehydration beverages that are more effective than SDs. In addition, insulin-modifying renal water reabsorption may contribute to the fluid-retention effect of MPD.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26235579','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26235579"><span id="translatedtitle">Increased Milk <span class="hlt">Protein</span> <span class="hlt">Concentration</span> in a Rehydration Drink Enhances Fluid Retention Caused by Water Reabsorption in Rats.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Ito, Kentaro; Saito, Yuri; Ashida, Kinya; Yamaji, Taketo; Itoh, Hiroyuki; Oda, Munehiro</p> <p>2015-01-01</p> <p>A fluid-retention effect is required for beverages that are designed to prevent dehydration. That is, fluid absorbed from the intestines should not be excreted quickly; long-term retention is desirable. Here, we focused on the effect of milk <span class="hlt">protein</span> on fluid retention, and propose a new effective oral rehydration method that can be used daily for preventing dehydration. We first evaluated the effects of different <span class="hlt">concentrations</span> of milk <span class="hlt">protein</span> on fluid retention by measuring the urinary volumes of rats fed fluid containing milk <span class="hlt">protein</span> at <span class="hlt">concentrations</span> of 1, 5, and 10%. We next compared the fluid-retention effect of milk <span class="hlt">protein</span>-enriched drink (MPD) with those of distilled water (DW) and a sports drink (SD) by the same method. Third, to investigate the mechanism of fluid retention, we measured plasma insulin changes in rats after ingesting these three drinks. We found that the addition of milk <span class="hlt">protein</span> at 5 or 10% reduced urinary volume in a dose-dependent manner. Ingestion of the MPD containing 4.6% milk <span class="hlt">protein</span> resulted in lower urinary volumes than DW and SD. MPD also showed a higher water reabsorption rate in the kidneys and higher <span class="hlt">concentrations</span> of plasma insulin than DW and SD. These results suggest that increasing milk <span class="hlt">protein</span> <span class="hlt">concentration</span> in a beverage enhances fluid retention, which may allow the possibility to develop rehydration beverages that are more effective than SDs. In addition, insulin-modifying renal water reabsorption may contribute to the fluid-retention effect of MPD. PMID:26235579</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/servlets/purl/10124599','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/servlets/purl/10124599"><span id="translatedtitle">Hydrogen-ion titrations of amino acids and <span class="hlt">proteins</span> in solutions containing <span class="hlt">concentrated</span> electrolyte</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>Fergg, F.; Kuehner, D.E.; Blanch, H.W.; Prausnitz, J.M.</p> <p>1994-12-01</p> <p>This report describes a first attempt to quantify the net charge as a function of solution pH for lysozyme and {alpha}-chymotrypsin at 0.1 M, 1.0 M and 3.0 M ionic strength, (IS). The calculations are based on the residue (titratable group) pK{sub a}`s in the amino-acid sequence of the <span class="hlt">protein</span>. To determine these pK{sub a}`s, a simple theory was used which assumes that the pK{sub a}`s are independent from each other in the <span class="hlt">protein</span> and are equal to their pK{sub a} values in free amino-acid solution (Independent-Site Theory, IST). Residue pK{sub a}`s were obtained from amino-acid hydrogen-ion titrations at three different KCl <span class="hlt">concentrations</span> corresponding to 0.1M, 1.0M and 3.0M ionic strength. After construction of a suitable apparatus, the experimental procedure and data reduction were computerized to perform a large number of titrations. Most measured pK{sub a}`s showed high reproducibility (the difference of pK{sub a} values observed between two experiments was less than 0.05). For IS = 0.1M, observed pK{sub a}`s agreed with literature values to within a few hundredths of a pH unit. Furthermore, the ionic-strength dependence of the pK{sub a}`s followed the trends reported in the literature, viz. pK{sub a} values decrease with increasing ionic strength until they reach a minimum at about IS = 0.5M. At still higher IS, pK{sub a}`s increase as the ionic strength rises to 3M. The known pK{sub a}`s of all titratable groups in a <span class="hlt">protein</span> were used with the IST to give a first approximation of how the <span class="hlt">protein</span> net charge varies with pH at high ionic strength. A comparison of the titration curves based on the IST with experimental lysozyme and {alpha}-chymotrypsin titration data indicates acceptable agreement at IS = 0.1M. However, comparison of measured and calculated titration curves at IS = 1M and IS = 3M indicates only quantitative agreement.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26455339','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26455339"><span id="translatedtitle">Stability of buffer-free freeze-dried formulations: A feasibility study of a monoclonal antibody at high <span class="hlt">protein</span> <span class="hlt">concentrations</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Garidel, Patrick; Pevestorf, Benjamin; Bahrenburg, Sven</p> <p>2015-11-01</p> <p>We studied the stability of freeze-dried therapeutic <span class="hlt">protein</span> formulations over a range of initial <span class="hlt">concentrations</span> (from 40 to 160 mg/mL) and employed a variety of formulation strategies (including buffer-free freeze dried formulations, or BF-FDF). Highly <span class="hlt">concentrated</span>, buffer-free liquid formulations of therapeutic monoclonal antibodies (mAbs) have been shown to be a viable alternative to conventionally buffered preparations. We considered whether it is feasible to use the buffer-free strategy in freeze-dried formulations, as an answer to some of the known drawbacks of conventional buffers. We therefore conducted an accelerated stability study (24 weeks at 40 °C) to assess the feasibility of stabilizing freeze-dried formulations without "classical" buffer components. Factors monitored included pH stability, <span class="hlt">protein</span> integrity, and <span class="hlt">protein</span> aggregation. Because the <span class="hlt">protein</span> solutions are inherently self-buffering, and the system's buffer capacity scales with <span class="hlt">protein</span> <span class="hlt">concentration</span>, we included highly <span class="hlt">concentrated</span> buffer-free freeze-dried formulations in the study. The tested formulations ranged from "fully formulated" (containing both conventional buffer and disaccharide stabilizers) to "buffer-free" (including formulations with only disaccharide lyoprotectant stabilizers) to "excipient-free" (with neither added buffers nor stabilizers). We evaluated the impacts of varying <span class="hlt">concentrations</span>, buffering schemes, pHs, and lyoprotectant additives. At the end of 24 weeks, no change in pH was observed in any of the buffer-free formulations. Unbuffered formulations were found to have shorter reconstitution times and lower opalescence than buffered formulations. <span class="hlt">Protein</span> stability was assessed by visual inspection, sub-visible particle analysis, <span class="hlt">protein</span> monomer content, charge variants analysis, and hydrophobic interaction chromatography. All of these measures found the stability of buffer-free formulations that included a disaccharide stabilizer comparable to buffer</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26029973','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26029973"><span id="translatedtitle">Insight into the Interaction of Graphene Oxide with Serum <span class="hlt">Proteins</span> and the Impact of the Degree of Reduction and <span class="hlt">Concentration</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Wei, Xue-Qin; Hao, Li-Ying; Shao, Xiao-Ru; Zhang, Quan; Jia, Xiao-Qin; Zhang, Zhi-Rong; Lin, Yun-Feng; Peng, Qiang</p> <p>2015-06-24</p> <p>As novel applied nanomaterials, both graphene oxide (GO) and its reduced form (rGO) have attracted global attention, because of their excellent properties. However, the lack of comprehensive understanding of their interactions with biomacromolecules highly limits their biomedical applications. This work aims to initiate a systematic study on the property changes of GO/rGO upon interaction with serum <span class="hlt">proteins</span> and on how their degree of reduction and exposure <span class="hlt">concentration</span> affect this interaction, as well as to analyze the possible biomedical impacts of the interaction. We found that the adsorption of <span class="hlt">proteins</span> on GO/rGO occurred spontaneously and rapidly, leading to significant changes in size, zeta potential, and morphology. Compared to rGO, GO showed a higher ability in quenching intrinsic fluorescence of serum <span class="hlt">proteins</span> in a <span class="hlt">concentration</span>-dependent manner. The <span class="hlt">protein</span> adsorption efficiency and the types of associated <span class="hlt">proteins</span> varied, depending on the degree of reduction and <span class="hlt">concentration</span> of graphene. Our findings indicate the importance of evaluating the potential <span class="hlt">protein</span> adsorption before making use of GO/rGO in drug delivery, because the changed physicochemical properties after <span class="hlt">protein</span> adsorption will have significant impacts on safety and effectiveness of these delivery systems. On the other hand, this interaction can also be used for the separation, purification, or delivery of certain <span class="hlt">proteins</span>. PMID:26029973</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/22771841','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/22771841"><span id="translatedtitle">Comparison and applications of label-free <span class="hlt">absolute</span> proteome quantification methods on Escherichia coli.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Arike, L; Valgepea, K; Peil, L; Nahku, R; Adamberg, K; Vilu, R</p> <p>2012-09-18</p> <p>Three different label-free proteome quantification methods--APEX, emPAI and iBAQ--were evaluated to measure proteome-wide <span class="hlt">protein</span> <span class="hlt">concentrations</span> in the cell. All the methods were applied to a sample from Escherichia coli chemostat culture. A Pearson squared correlation of approximately 0.6 among the three quantification methods was demonstrated. Importantly, the sum of quantified <span class="hlt">proteins</span> by iBAQ and emPAI corresponded with the Lowry total <span class="hlt">protein</span> quantification, demonstrating applicability of label-free methods for an accurate calculation of <span class="hlt">protein</span> <span class="hlt">concentrations</span> at the proteome level. The iBAQ method showed the best correlation between biological replicates, a normal distribution among all <span class="hlt">protein</span> abundances, and the lowest variation among ribosomal <span class="hlt">protein</span> abundances, which are expected to have equal amounts. <span class="hlt">Absolute</span> quantitative proteome data enabled us to evaluate metabolic cost for <span class="hlt">protein</span> synthesis and apparent catalytic activities of enzymes by integration with flux analysis. All the methods demonstrated similar ATP costs for <span class="hlt">protein</span> synthesis for different cellular processes and that costs for expressing biomass synthesis related <span class="hlt">proteins</span> were higher than those for energy generation. Importantly, catalytic activities of energy metabolism enzymes were an order or two higher than those of monomer synthesis. Interestingly, a staircase-like <span class="hlt">protein</span> expression was demonstrated for most of the transcription units. PMID:22771841</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4416786','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4416786"><span id="translatedtitle">Validation of a P-Glycoprotein (P-gp) Humanized Mouse Model by Integrating Selective <span class="hlt">Absolute</span> Quantification of Human MDR1, Mouse Mdr1a and Mdr1b <span class="hlt">Protein</span> Expressions with In Vivo Functional Analysis for Blood-Brain Barrier Transport</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Sadiq, Muhammad Waqas; Uchida, Yasuo; Hoshi, Yutaro; Tachikawa, Masanori; Terasaki, Tetsuya; Hammarlund-Udenaes, Margareta</p> <p>2015-01-01</p> <p>It is essential to establish a useful validation method for newly generated humanized mouse models. The novel approach of combining our established species-specific <span class="hlt">protein</span> quantification method combined with in vivo functional studies is evaluated to validate a humanized mouse model of P-gp/MDR1 efflux transporter. The P-gp substrates digoxin, verapamil and docetaxel were administered to male FVB Mdr1a/1b(+/+) (FVB WT), FVB Mdr1a/1b(-/-) (Mdr1a/1b(-/-)), C57BL/6 Mdr1a/1b(+/+) (C57BL/6 WT) and humanized C57BL (hMDR1) mice. Brain-to-plasma total <span class="hlt">concentration</span> ratios (Kp) were measured. Quantitative targeted <span class="hlt">absolute</span> proteomic (QTAP) analysis was used to selectively quantify the <span class="hlt">protein</span> expression levels of hMDR1, Mdr1a and Mdr1b in the isolated brain capillaries. The <span class="hlt">protein</span> expressions of other transporters, receptors and claudin-5 were also quantified. The Kp for digoxin, verapamil, and docetaxel were 20, 30 and 4 times higher in the Mdr1a/1b(-/-) mice than in the FVB WT controls, as expected. The Kp for digoxin, verapamil and docetaxel were 2, 16 and 2-times higher in the hMDR1 compared to the C57BL/6 WT mice. The hMDR1 mice had 63- and 9.1-fold lower expressions of the hMDR1 and Mdr1a <span class="hlt">proteins</span> than the corresponding expression of Mdr1a in C57BL/6 WT mice, respectively. The <span class="hlt">protein</span> expression levels of other molecules were almost consistent between C57BL/6 WT and hMDR1 mice. The P-gp function at the BBB in the hMDR1 mice was smaller than that in WT mice due to lower <span class="hlt">protein</span> expression levels of hMDR1 and Mdr1a. The combination of QTAP and in vivo functional analyses was successfully applied to validate the humanized animal model and evaluates its suitability for further studies. PMID:25932627</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/10909989','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/10909989"><span id="translatedtitle">Serum leptin <span class="hlt">concentrations</span> during severe <span class="hlt">protein</span>-energy malnutrition: correlation with growth parameters and endocrine function.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Soliman, A T; ElZalabany, M M; Salama, M; Ansari, B M</p> <p>2000-07-01</p> <p>Circulating leptin, insulin, insulin-like growth factor-I (IGF-I), cortisol, and albumin <span class="hlt">concentrations</span> and the growth hormone (GH) response to provocation were measured in 30 children with severe <span class="hlt">protein</span>-energy malnutrition (PEM), 20 with marasmus and 10 with kwashiorkor, as well as 10 age-matched normal children (body mass index [BMI] >50th and <90th percentile for age and sex) and 10 prepubertal obese children (BMI >95th percentile for age and sex). Patients with PEM had a significantly lower BMI, midarm circumference (MAC), and skinfold thickness (SFT) compared with the age-matched control group. Basal cortisol and GH <span class="hlt">concentrations</span> were significantly higher in the malnourished groups versus controls. Leptin and IGF-I were significantly lower in the marasmic and kwashiorkor groups versus normal children. Fasting insulin levels were significantly decreased in the kwashiorkor group compared with marasmic and normal children. The BMI correlated significantly with leptin (r = .77, P < .001), basal insulin (r = .61, P < .001), and IGF-I (r = .77, P < .001) and negatively with basal GH (r = -.52, P < .001). These findings suggest that during prolonged nutritional deprivation, the decreased energy intake, diminished subcutaneous fat mass, and declining insulin (and possibly IGF-I) <span class="hlt">concentration</span> suppress leptin production. In support of this view, serum leptin levels were positively correlated with triceps, scapular, and abdominal SFT (r = .763, .75, and .744, respectively, P < .0001) in all of the children. Moreover, basal insulin and circulating IGF-I were correlated significantly with leptin <span class="hlt">concentrations</span> (r = .47 and .62, respectively, P < .001). Basal levels of cortisol and GH were significantly elevated in the 2 groups with severe PEM. It is suggested that low leptin levels can stimulate the hypothalamic-pituitary-adrenal (HPA) axis and possibly the hypothalamic-pituitary-GH axis to maintain the high cortisol and GH levels necessary for effective lipolysis to</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4550234','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4550234"><span id="translatedtitle">Baseline Plasma C-Reactive <span class="hlt">Protein</span> <span class="hlt">Concentrations</span> and Motor Prognosis in Parkinson Disease</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Umemura, Atsushi; Oeda, Tomoko; Yamamoto, Kenji; Tomita, Satoshi; Kohsaka, Masayuki; Park, Kwiyoung; Sugiyama, Hiroshi; Sawada, Hideyuki</p> <p>2015-01-01</p> <p>Background C-reactive <span class="hlt">protein</span> (CRP), a blood inflammatory biomarker, is associated with the development of Alzheimer disease. In animal models of Parkinson disease (PD), systemic inflammatory stimuli can promote neuroinflammation and accelerate dopaminergic neurodegeneration. However, the association between long-term systemic inflammations and neurodegeneration has not been assessed in PD patients. Objective To investigate the longitudinal effects of baseline CRP <span class="hlt">concentrations</span> on motor prognosis in PD. Design, Setting, and Participants Retrospective analysis of 375 patients (mean age, 69.3 years; mean PD duration, 6.6 years). Plasma <span class="hlt">concentrations</span> of high-sensitivity CRP were measured in the absence of infections, and the Unified Parkinson’s Disease Rating Scale Part III (UPDRS-III) scores were measured at five follow-up intervals (Days 1–90, 91–270, 271–450, 451–630, and 631–900). Main Outcome Measure Change of UPDRS-III scores from baseline to each of the five follow-up periods. Results Change in UPDRS-III scores was significantly greater in PD patients with CRP <span class="hlt">concentrations</span> ≥0.7 mg/L than in those with CRP <span class="hlt">concentrations</span> <0.7 mg/L, as determined by a generalized estimation equation model (P = 0.021) for the entire follow-up period and by a generalized regression model (P = 0.030) for the last follow-up interval (Days 631–900). The regression coefficients of baseline CRP for the two periods were 1.41 (95% confidence interval [CI] 0.21–2.61) and 2.62 (95% CI 0.25–4.98), respectively, after adjusting for sex, age, baseline UPDRS-III score, dementia, and incremental L-dopa equivalent dose. Conclusion Baseline plasma CRP levels were associated with motor deterioration and predicted motor prognosis in patients with PD. These associations were independent of sex, age, PD severity, dementia, and anti-Parkinsonian agents, suggesting that subclinical systemic inflammations could accelerate neurodegeneration in PD. PMID:26308525</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2517420','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2517420"><span id="translatedtitle">AMNIOTIC FLUID HEAT SHOCK <span class="hlt">PROTEIN</span> 70 <span class="hlt">CONCENTRATION</span> IN HISTOLOGIC CHORIOAMNIONITIS, TERM AND PRETERM PARTURITION</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Chaiworapongsa, Tinnakorn; Erez, Offer; Kusanovic, Juan Pedro; Vaisbuch, Edi; Mazaki-Tovi, Shali; Gotsch, Francesca; Than, Nandor Gabor; Mittal, Pooja; Kim, Yeon Mee; Camacho, Natalia; Edwin, Samuel; Gomez, Ricardo; Hassan, Sonia S.; Romero, Roberto</p> <p>2008-01-01</p> <p>Objective Heat shock <span class="hlt">protein</span> (HSP) 70, a conserved member of the stress <span class="hlt">protein</span> family, is produced in almost all cell types in response to a wide range of stressful stimuli and their production has a survival value. Evidence suggests that extra-cellular HSP70 is involved in the activation of the innate and adaptive immune response. Furthermore, increased mRNA expression of HSP 70 was observed in human fetal membranes following endotoxin stimulation. This study was conducted to determine the changes in amniotic fluid HSP70 <span class="hlt">concentrations</span> during pregnancy, term and preterm parturition, intra-amniotic infection (IAI), and histologic chorioamnionitis. Study design A cross-sectional study was conducted in 376 pregnant women in the following groups: 1) women with a normal pregnancy that were classified in the following categories: a) women in the mid-trimester (14–18 weeks) who underwent amniocentesis for genetic indications and delivered normal infants at term (n=72); b) women at term not in labor (n=23); and c) those at term in labor (n=48); 2) women with spontaneous preterm labor and intact membranes that were subdivided into the following categories: a) preterm labor who delivered at term without IAI (n=42), b) preterm labor who delivered preterm without IAI (n=57), and c) preterm labor and delivery with IAI (n=30); and 3) women with preterm prelabor rupture of membranes (PROM) with (n=50) and without (n=54) IAI. Among patients with preterm labor with intact membranes and preterm PROM who delivered within 72 hours of amniocentesis, placenta, umbilical cord and chorioamniotic membranes were collected and assessed for the presence or absence of acute inflammatory lesions in the extra-placental membranes (histologic chorioamnionitis) and/or umbilical cords (funisitis). HSP70 <span class="hlt">concentrations</span> in amniotic fluid were determined using a sensitive and specific immunoassay. Non-parametric statistics were used for analysis. A p value <0.05 was considered statistically</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4680326','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4680326"><span id="translatedtitle">Changes of urinary angiotensinogen <span class="hlt">concentration</span> and its association with urinary <span class="hlt">proteins</span> in diabetic rats</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Zhuang, Zhen; Bai, Qiong; A, Lata; Liang, Yaoxian; Zheng, Danxia; Wang, Yue</p> <p>2015-01-01</p> <p>Objective: It had been reported that angiotensinogen might be a marker for activation of renin-angiotensin system, which was associated with the development of diabetic nephropathy. The purpose of this study was to investigate the functional roles of AGT in DN in vitro. Methods: Diabetic rat models were built by single intraperitoneal injection of streptozotocin. The diabetic rats were divided into three groups, two of the three groups were treated with different doses of losartan, the other diabetic group was as control and normal rats acted as healthy control. In a 12-week investigation, we detected the changes of AGT in all rats’ blood and urine and the association between AGT <span class="hlt">concentration</span> and RAS activation and urinary <span class="hlt">proteins</span> were analyzed in this study. Results: The serum AGT of rats had no significant differences (P>0.05 for all). The urinary AGT of the diabetic rats was significantly different from the control group, moreover, the urinary AGT of the diabetic rats under different treatments was also obviously different (P<0.05 for all). Besides, the results of immunohistochemical assay indicated that AGT expression level was correlated with renal tissues damage. The level of AGT was positively associated with urinary <span class="hlt">protein</span> (r=0.493, P<0.01) and negatively correlated with CCr (r=-0.474, P=0.007) and the dose of ARB (r=-0.575, P=0.001). Moreover, the dose of ARB was independently associated with urinary AGT (B=-2.963, P=0.024) in diabetic rats. Conclusion: Urinary AGT may be a marker for the activation of local RAS in kidney and independently associated with ARB. PMID:26722381</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27085401','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27085401"><span id="translatedtitle">Short communication: The effect of liquid storage on the flavor of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Park, Curtis W; Parker, Megan; Drake, MaryAnne</p> <p>2016-06-01</p> <p>Unit operations in dried dairy ingredient manufacture significantly influence sensory properties and, consequently, their use and consumer acceptance in a variety of ingredient applications. In whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) manufacture, liquid can be stored as whey or WPC before spray drying. The objective of this study was to determine the effect of storage, composition, and bleaching on the flavor of spray-dried WPC80. Liquid whey was manufactured and subjected to the following treatments: bleached or unbleached and liquid whey or liquid WPC storage. The experiment was replicated 3 times and included a no-storage control. All liquid storage was performed at 4°C for 24h. Flavor of the final spray-dried WPC80 was evaluated by a trained panel and volatile compound analyses. Storage of liquids increased cardboard flavor, decreased sweet aromatic flavor, and resulted in increased volatile lipid oxidation products. Bleaching altered the effect of liquid storage. Storage of unbleached liquid whey decreased sweet aromatic flavor and increased cardboard flavor and volatile lipid oxidation products compared with liquid WPC80 and no storage. In contrast, storage of bleached liquid WPC decreased sweet aromatic flavor and increased cardboard flavor and associated volatile lipid oxidation products compared with bleached liquid whey or no storage. These results confirm that liquid storage increases off-flavors in spray-dried <span class="hlt">protein</span> but to a variable degree, depending on whether bleaching has been applied. If liquid storage is necessary, bleached WPC80 should be stored as liquid whey and unbleached WPC80 should be stored as liquid WPC to mitigate off-flavors.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26556312','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26556312"><span id="translatedtitle">Intentional formation of a <span class="hlt">protein</span> corona on nanoparticles: Serum <span class="hlt">concentration</span> affects <span class="hlt">protein</span> corona mass, surface charge, and nanoparticle-cell interaction.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Gräfe, Christine; Weidner, Andreas; Lühe, Moritz V D; Bergemann, Christian; Schacher, Felix H; Clement, Joachim H; Dutz, Silvio</p> <p>2016-06-01</p> <p>The <span class="hlt">protein</span> corona, which immediately is formed after contact of nanoparticles and biological systems, plays a crucial role for the biological fate of nanoparticles. In the here presented study we describe a strategy to control the amount of corona <span class="hlt">proteins</span> which bind on particle surface and the impact of such a <span class="hlt">protein</span> corona on particle-cell interactions. For corona formation, polyethyleneimine (PEI) coated magnetic nanoparticles (MNP) were incubated in a medium consisting of fetal calf serum (FCS) and cell culture medium. To modulate the amount of <span class="hlt">proteins</span> bind to particles, the composition of the incubation medium was varied with regard to the FCS content. The <span class="hlt">protein</span> corona mass was estimated and the size distribution of the participating <span class="hlt">proteins</span> was determined by means of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Additionally, the zeta potential of incubated particles was measured. Human blood-brain barrier-representing cell line HBMEC was used for in vitro incubation experiments. To investigate the consequences of the FCS dependent <span class="hlt">protein</span> corona formation on the interaction of MNP and cells flow cytometry and laser scanning microscopy were used. Zeta potential as well as SDS-PAGE clearly reveal an increase in the amount of corona <span class="hlt">proteins</span> on MNP with increasing amount of FCS in incubation medium. For MNP incubated with lower FCS <span class="hlt">concentrations</span> especially medium-sized <span class="hlt">proteins</span> of molecular weights between 30kDa and 100kDa could be found within the <span class="hlt">protein</span> corona, whereas for MNP incubated within higher FCS <span class="hlt">concentrations</span> the fraction of corona <span class="hlt">proteins</span> of 30kDa and less increased. The presence of the <span class="hlt">protein</span> corona reduces the interaction of PEI-coated MNP with HBMEC cells within a 30min-incubation.</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_14");'>14</a></li> <li><a href="#" onclick='return showDiv("page_15");'>15</a></li> <li class="active"><span>16</span></li> <li><a href="#" onclick='return showDiv("page_17");'>17</a></li> <li><a href="#" onclick='return showDiv("page_18");'>18</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_16 --> <div id="page_17" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_15");'>15</a></li> <li><a href="#" onclick='return showDiv("page_16");'>16</a></li> <li class="active"><span>17</span></li> <li><a href="#" onclick='return showDiv("page_18");'>18</a></li> <li><a href="#" onclick='return showDiv("page_19");'>19</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="321"> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2016JASMS..27..669H','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2016JASMS..27..669H"><span id="translatedtitle">Conformational Analysis of <span class="hlt">Proteins</span> in Highly <span class="hlt">Concentrated</span> Solutions by Dialysis-Coupled Hydrogen/Deuterium Exchange Mass Spectrometry</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Houde, Damian; Nazari, Zeinab E.; Bou-Assaf, George M.; Weiskopf, Andrew S.; Rand, Kasper D.</p> <p>2016-04-01</p> <p>When highly <span class="hlt">concentrated</span>, an antibody solution can exhibit unusual behaviors, which can lead to unwanted properties, such as increased levels of <span class="hlt">protein</span> aggregation and unusually high viscosity. Molecular modeling, along with many indirect biophysical measurements, has suggested that the cause for these phenomena can be due to short range electrostatic and/or hydrophobic <span class="hlt">protein-protein</span> interactions. Hydrogen/deuterium exchange mass spectrometry (HDX-MS) is a useful tool for investigating <span class="hlt">protein</span> conformation, dynamics, and interactions. However, "traditional" continuous dilution labeling HDX-MS experiments have limited utility for the direct analysis of solutions with high <span class="hlt">concentrations</span> of <span class="hlt">protein</span>. Here, we present a dialysis-based HDX-MS (di-HDX-MS) method as an alternative HDX-MS labeling format, which takes advantage of passive dialysis rather than the classic dilution workflow. We applied this approach to a highly <span class="hlt">concentrated</span> antibody solution without dilution or significant sample manipulation, prior to analysis. Such a method could pave the way for a deeper understanding of the unusual behavior of <span class="hlt">proteins</span> at high <span class="hlt">concentrations</span>, which is highly relevant for development of biopharmaceuticals in industry.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4701966','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4701966"><span id="translatedtitle">Smoking-Relevant Nicotine <span class="hlt">Concentration</span> Attenuates the Unfolded <span class="hlt">Protein</span> Response in Dopaminergic Neurons</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Srinivasan, Rahul; Henley, Beverley M.; Henderson, Brandon J.; Indersmitten, Tim; Cohen, Bruce N.; Kim, Charlene H.; McKinney, Sheri; Deshpande, Purnima; Xiao, Cheng</p> <p>2016-01-01</p> <p>Retrospective epidemiological studies show an inverse correlation between susceptibility to Parkinson's disease and a person's history of tobacco use. Animal model studies suggest nicotine as a neuroprotective agent and nicotinic acetylcholine (ACh) receptors (nAChRs) as targets for neuroprotection, but the underlying neuroprotective mechanism(s) are unknown. We cultured mouse ventral midbrain neurons for 3 weeks. Ten to 20% of neurons were dopaminergic (DA), revealed by tyrosine hydroxylase (TH) immunoreactivity. We evoked mild endoplasmic reticulum (ER) stress with tunicamycin (Tu), producing modest increases in the level of nuclear ATF6, phosphorylated eukaryotic initiation factor 2α, nuclear XBP1, and the downstream proapoptotic effector nuclear C/EBP homologous <span class="hlt">protein</span>. We incubated cultures for 2 weeks with 200 nm nicotine, the approximate steady-state <span class="hlt">concentration</span> between cigarette smoking or vaping, or during nicotine patch use. Nicotine incubation suppressed Tu-induced ER stress and the unfolded <span class="hlt">protein</span> response (UPR). Study of mice with fluorescent nAChR subunits showed that the cultured TH+ neurons displayed α4, α6, and β3 nAChR subunit expression and ACh-evoked currents. Gene expression profile in cultures from TH-eGFP mice showed that the TH+ neurons also express several other genes associated with DA release. Nicotine also upregulated ACh-induced currents in DA neurons by ∼2.5-fold. Thus, nicotine, at a <span class="hlt">concentration</span> too low to activate an appreciable fraction of plasma membrane nAChRs, induces two sequelae of pharmacological chaperoning in the ER: UPR suppression and nAChR upregulation. Therefore, one mechanism of neuroprotection by nicotine is pharmacological chaperoning, leading to UPR suppression. Measuring this pathway may help in assessing neuroprotection. SIGNIFICANCE STATEMENT Parkinson's disease (PD) cannot yet be cured or prevented. However, many retrospective epidemiological studies reveal that PD is diagnosed less frequently in</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/17264236','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/17264236"><span id="translatedtitle">The influence of oscillating dietary <span class="hlt">protein</span> <span class="hlt">concentrations</span> on finishing cattle. II. Nutrient retention and ammonia emissions.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Archibeque, S L; Freetly, H C; Cole, N A; Ferrell, C L</p> <p>2007-06-01</p> <p>We hypothesized that oscillation of the dietary CP <span class="hlt">concentrations</span> would improve efficiency of N use and reduce N loss to the environment. Charolais-cross steers (n = 8; 315 +/- 21 kg of BW) were used in a replicated 4 x 4 Latin square design. The steers were allowed ad libitum access to the following diets: 1) 9.1% CP (low), 2) 11.8% CP (medium), 3) 13.9% CP (high), or 4) low and high oscillated on a 48-h interval on each diet (oscillating). Dry matter intake did not differ among treatments (P = 0.46), but N intake differed (P < 0.01) from 94 (low) to 131 (medium), 142 (high), and 133 g/d (oscillating), as designed. Dry matter digestibility increased (P < 0.01) from 71.8% (low) to 75.8% (medium), 77.7% (high), and 77.5% (oscillating). Nitrogen digestibility increased (P < 0.01) from 62.2% (low) to 67.2% (medium) to 70.1% (high) and 70.9% (oscillating). Nitrogen retention was greater (P < 0.01) in steers fed oscillating (55.0 g/d) than in the steers fed low (34.8 g/ d) or high (40.2 g/d), but N retention of steers fed medium (49.8 g/d) differed (P = 0.02) only from that of steers fed low. Urinary urea N did not differ between steers fed medium (19.5 g/d) or oscillating (21.3 g/d) but was lowest (P < 0.01) for those fed low (8.2 g/d) and greatest for those fed high (39.2 g/d). Daily heat production (kcal/BW(0.75)) tended (P = 0.09) to be less for the steers fed low (177) than those fed medium (189), high (188), or oscillating (182). Cumulative in vitro ammonia volatilization from the manure of steers fed oscillating was lower (P < 0.01) for the initial 5 d of incubation than from manure of those fed medium, but there was no difference after 11 d of incubation. Additionally, there was a decrease (P < 0.01) in in vitro ammonia volatilization as <span class="hlt">protein</span> <span class="hlt">concentration</span> in the diet decreased from high to medium to low. These data indicate that oscillation of the dietary <span class="hlt">protein</span> improved N retention of finishing steers compared with those in high and low N diets and that</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26049243','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26049243"><span id="translatedtitle">Production and functional evaluation of a <span class="hlt">protein</span> <span class="hlt">concentrate</span> from giant squid (Dosidicus gigas) by acid dissolution and isoelectric precipitation.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Cortés-Ruiz, Juan A; Pacheco-Aguilar, Ramón; Elena Lugo-Sánchez, M; Gisela Carvallo-Ruiz, M; García-Sánchez, Guillermina</p> <p>2008-09-15</p> <p>A <span class="hlt">protein</span> <span class="hlt">concentrate</span> from giant squid (Dosidicus gigas) was produced under acidic conditions and its functional-technological capability evaluated in terms of its gel-forming ability, water holding capacity and colour attributes. Technological functionality of the <span class="hlt">concentrate</span> was compared with that of squid muscle and a neutral <span class="hlt">concentrate</span>. <span class="hlt">Protein-protein</span> aggregates insoluble at high ionic strength (I=0.5M), were detected in the acidic <span class="hlt">concentrate</span> as result of processing with no preclusion of its gel-forming ability during the sol-to-gel thermal transition. Even though washing under acidic condition promoted autolysis of the myosin heavy chain, the acidic <span class="hlt">concentrate</span> displayed an outstanding ability to gel giving samples with a gel strength of 455 and 1160gcm at 75% and 90% compression respectively, and an AA folding test grade indicative of high gel strength, elasticity, and cohesiveness. The process proved to be a good alternative for obtaining a functional <span class="hlt">protein</span> <span class="hlt">concentrate</span> from giant squid muscle. PMID:26049243</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/24081467','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/24081467"><span id="translatedtitle">Effect of freezing rate and dendritic ice formation on <span class="hlt">concentration</span> profiles of <span class="hlt">proteins</span> frozen in cylindrical vessels.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Rodrigues, Miguel A; Miller, Maria A; Glass, Matt A; Singh, Satish K; Johnston, Keith P</p> <p>2011-04-01</p> <p>The process of freezing <span class="hlt">protein</span> solutions can perturb the conformation of the <span class="hlt">protein</span> and potentially lead to aggregate formation during long-term storage in the frozen state. Radial macroscopic freeze <span class="hlt">concentration</span> and temperature profiles for bovine serum albumin (BSA) solutions in small cylindrical stainless steel vessels were determined for various freezing rates. The measured <span class="hlt">concentrations</span> of both BSA and immunoglobulin G2, as well as trehalose in sampled ice sections, increased by up to twofold to threefold toward the bottom and radial center for slow freezing rates produced in stagnant air freezers. The <span class="hlt">concentration</span> and temperature profiles result in density gradients that transport solutes by convective flow. For faster external cooling by either forced convection of air or a liquid coolant, the increased freezing rate raised the ice front velocity resulting in enhanced dendritic ice growth. The ice trapped the solutes more effectively before they were removed from the ice front by diffusion and convection, resulting in more uniform solute <span class="hlt">concentration</span> profiles. The dynamic temperature profiles from multiple radial thermocouples were consistent with the independently measured freeze <span class="hlt">concentration</span> profiles. The ability to control the <span class="hlt">protein</span> <span class="hlt">concentration</span> profile in the frozen state offers the potential to improve stability of <span class="hlt">protein</span> in long-term frozen storage.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/18374361','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/18374361"><span id="translatedtitle">Are extracellular osmolality and sodium <span class="hlt">concentration</span> determined by Donnan effects of intracellular <span class="hlt">protein</span> charges and of pumped sodium?</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Kurbel, Sven</p> <p>2008-06-21</p> <p>Although we are used to attribute almost identical extracellular fluid (ECF) sodium <span class="hlt">concentrations</span> in birds, amphibians, reptiles, and mammals to the composition of the primordial oceans in which, presumably, all life originated, this interpretation is not supported by geological data suggesting that the ocean salinity was never much lower than the present-day values, still four times higher than our plasma sodium. Here presented interpretation is that the similar ECF salt <span class="hlt">concentrations</span> are dictated by the opposed Donnan effects on the cell membrane. The only way for the cell to reach the osmotic equilibrium is to alter cell volume, until <span class="hlt">concentration</span> of nondiffusible intracellular ions (mainly charges on intracellular <span class="hlt">proteins</span>) is equal to the ECF restricted ions (mainly Na+ ions, restricted by pumping out of cells). The achievement of electroneutrality requires that the sum of all anions equals <span class="hlt">concentration</span> of positive ions in the cell (mainly K+). Negative charges on cytoplasmic <span class="hlt">proteins</span> are the most stable component among ionized particles and other ions have to adapt to their <span class="hlt">concentration</span>. Positive and negative soluble intracellular ions are all osmotically active and to achieve balance of osmotic forces on the cell membrane, the sum of their intracellular <span class="hlt">concentrations</span> must equal the <span class="hlt">concentration</span> of osmotically active extracellular particles. Since almost half the osmotically active ECF particles are sodium ions, the ECF sodium <span class="hlt">concentration</span> seems related to <span class="hlt">concentration</span> of charges on cytoplasmic <span class="hlt">proteins</span> and <span class="hlt">concentration</span> of intracellular phosphates. Our ancestors could not leave the salty ocean and move to brackish, or even fresh waters, without adequate regulation of their ECF sodium <span class="hlt">concentration</span> and osmolality. <span class="hlt">Concentration</span> of charges on cytoplasmic <span class="hlt">proteins</span> or of intracellular phosphate buffers could not be altered, since this would compromise cell functioning. The remaining solution was to maintain the lowest ECF Na+ <span class="hlt">concentration</span> effective in</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26394157','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26394157"><span id="translatedtitle">Signaling Pathways Related to <span class="hlt">Protein</span> Synthesis and Amino Acid <span class="hlt">Concentration</span> in Pig Skeletal Muscles Depend on the Dietary <span class="hlt">Protein</span> Level, Genotype and Developmental Stages.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Liu, Yingying; Li, Fengna; Kong, Xiangfeng; Tan, Bie; Li, Yinghui; Duan, Yehui; Blachier, François; Hu, Chien-An A; Yin, Yulong</p> <p>2015-01-01</p> <p>Muscle growth is regulated by the homeostatic balance of the biosynthesis and degradation of muscle <span class="hlt">proteins</span>. To elucidate the molecular interactions among diet, pig genotype, and physiological stage, we examined the effect of dietary <span class="hlt">protein</span> <span class="hlt">concentration</span>, pig genotype, and physiological stages on amino acid (AA) pools, <span class="hlt">protein</span> deposition, and related signaling pathways in different types of skeletal muscles. The study used 48 Landrace pigs and 48 pure-bred Bama mini-pigs assigned to each of 2 dietary treatments: lower/GB (Chinese conventional diet)- or higher/NRC (National Research Council)-<span class="hlt">protein</span> diet. Diets were fed from 5 weeks of age to respective market weights of each genotype. Samples of biceps femoris muscle (BFM, type I) and longissimus dorsi muscle (LDM, type II) were collected at nursery, growing, and finishing phases according to the physiological stage of each genotype, to determine the AA <span class="hlt">concentrations</span>, mRNA levels for growth-related genes in muscles, and <span class="hlt">protein</span> abundances of mechanistic target of rapamycin (mTOR) signaling pathway. Our data showed that the <span class="hlt">concentrations</span> of most AAs in LDM and BFM of pigs increased (P<0.05) gradually with increasing age. Bama mini-pigs had generally higher (P<0.05) muscle <span class="hlt">concentrations</span> of flavor-related AA, including Met, Phe, Tyr, Pro, and Ser, compared with Landrace pigs. The mRNA levels for myogenic determining factor, myogenin, myocyte-specific enhancer binding factor 2 A, and myostatin of Bama mini-pigs were higher (P<0.05) than those of Landrace pigs, while total and phosphorylated <span class="hlt">protein</span> levels for <span class="hlt">protein</span> kinase B, mTOR, and p70 ribosomal <span class="hlt">protein</span> S6 kinases (p70S6K), and ratios of p-mTOR/mTOR, p-AKT/AKT, and p-p70S6K/p70S6K were lower (P<0.05). There was a significant pig genotype-dependent effect of dietary <span class="hlt">protein</span> on the levels for mTOR and p70S6K. When compared with the higher <span class="hlt">protein</span>-NRC diet, the lower <span class="hlt">protein</span>-GB diet increased (P<0.05) the levels for mTOR and p70S6K in Bama mini-pigs, but</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25175722','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25175722"><span id="translatedtitle">Relationship between cortisol and acute phase <span class="hlt">protein</span> <span class="hlt">concentrations</span> in female rabbits.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Argente, María-José; García, María de la Luz; Birlanga, Virginia; Muelas, Raquel</p> <p>2014-10-01</p> <p>Rabbit meat production in Europe is usually based on a semi-intensive system, in which lactation and gestation overlap. The demands of lactation and pregnancy are likely to be relatively stressful for female rabbits and may compromise the immune system and reproductive performance. The present study was designed to characterise circulating levels of cortisol, haptoglobin (Hp), C-reactive <span class="hlt">protein</span> (CRP), and serum amyloid A (SAA) in non-lactating and lactating female rabbits at first and second mating, and to determine whether any relationship exists between these biomarkers and litter size. Serum cortisol <span class="hlt">concentrations</span> were at their greatest (mean ± SEM = 39.5 ± 3.9 nmol/L) in animals at the end of lactation. However, after weaning, cortisol <span class="hlt">concentrations</span> were not significantly different compared to nulliparous females (19.9 ± 3.6 vs. 16.3 ± 2.2 nmol/L, respectively). The highest <span class="hlt">concentrations</span> of circulating Hp (0.14 ± 0.01 g/L) were seen in early lactating primiparous females, and lower in nulliparous females and in rabbits after weaning. In contrast, nulliparous female rabbits showed the highest plasma CRP values (13.1 ± 1.1 mg/L). No significant differences were found for SAA. Nulliparous females had smaller litter sizes than early lactating and non-lactating primiparous female rabbits. CRP and SAA showed a positive correlation (r = +0.24, P = 0.011) and were negatively related to litter size (r = -0.23, P = 0.017 and P = 0.032, respectively). Cortisol and Hp were not related to CRP, SAA, nor to litter size. These results suggest a closer association between the mechanisms that regulate release of CRP and SAA, compared to those that regulate Hp production. Thus, lactation is associated with changes in several stress biomarkers. CRP and SAA might be more useful for evaluating animal welfare and for predicting subsequent reproductive performance of female rabbits.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26188301','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26188301"><span id="translatedtitle">Hydrophobicity, thermal and micro-structural properties of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>-pullulan-beeswax films.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Jafari, Seid Mahdi; Khanzadi, Mehrdad; Mirzaei, Habibollah; Dehnad, Danial; Chegini, Faramarz Khodaian; Maghsoudlou, Yayha</p> <p>2015-09-01</p> <p>In this research, effects of beeswax (BW) on functional properties of whey <span class="hlt">protein</span> <span class="hlt">concentrates</span> (WPC):pullulan (PUL) films were investigated. For this purpose, 0, 10, 20 and 30w/w(glycerol)% BW rates and 30:70, 50:50 and 70:30w/w% WPC:PUL ratios were applied. Films containing 70% WPC:30% PUL (WPC70) and 30% BW (BW30) justified the highest contact angle (92.4°) among all films; SEM micrographs indicated that BW could come toward the surface of films during drying stage and resulted in a higher hydrophobic behavior of bilayer films compared with blend films. WPC70 supplied the lowest T(g) values (36-48 °C) among different proportions of WPC-PUL; the highest melting points were just assured in the absence of BW regardless of combination ratio for WPI:PUL. BW30 films deserved lower roughness rates than BW20 (and even BW10) films, indicating more advantageous microstructure and higher hydrogen connections in BW30 films and justifying similar melting points attained for BW30 films to BW20 or 10 ones. Overall, application of WPC70 and BW30 was recommended to obtain optimum combination of final properties for WPC-PUL-BW bilayer films as SEM exhibited flexible and elastic structures of such films.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27344387','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27344387"><span id="translatedtitle">Whey <span class="hlt">protein</span> phospholipid <span class="hlt">concentrate</span> and delactosed permeate: Applications in caramel, ice cream, and cake.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Levin, M A; Burrington, K J; Hartel, R W</p> <p>2016-09-01</p> <p>Whey <span class="hlt">protein</span> phospholipid <span class="hlt">concentrate</span> (WPPC) and delactosed permeate (DLP) are 2 coproducts of cheese whey processing that are currently underutilized. Past research has shown that WPPC and DLP can be used together as a functional dairy ingredient in foods such as ice cream, soup, and caramel. However, the scope of the research has been limited to a single WPPC supplier. The variability of the composition and functionality of WPPC was previously studied. The objective of this research was to expand on the previous study and examine the potential applications of WPPC and DLP blends in foods. In ice cream, WPPC was added as a natural emulsifier to replace synthetic emulsifiers. The WPPC decreased the amount of partially coalesced fat and increased the drip-through rate. In caramel, DLP and WPPC replaced sweetened condensed skim milk and lecithin. Cold flow increased significantly, and hardness and stickiness decreased. In cake, DLP and WPPC were added as a total replacement of eggs, with no change in yield, color, or texture. Overall, WPPC and DLP can be utilized as functional dairy ingredients at a lower cost in ice cream and cake but not in chewy caramel.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/24804055','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/24804055"><span id="translatedtitle">Low-fat frankfurters from <span class="hlt">protein</span> <span class="hlt">concentrates</span> of tilapia viscera and mechanically separated tilapia meat.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Cavenaghi-Altemio, Angela D; Alcade, Lígia B; Fonseca, Gustavo G</p> <p>2013-11-01</p> <p>In order to develop a healthy low-fat frankfurter-type sausage, different formulations were developed with tilapia viscera surimi (T1) and two with mechanically separated tilapia meat (MSTM) surimi (T2 and T3), all without pig lard addition. Due to technological problems observed for T1 sausage during cooking, it was not further investigated. The functionality of the other two formulations was evaluated based on proximate composition, pH, water activity, and texture. Finally, microbiological and sensory analyses based on acceptance tests were performed. Listeria monocytogenes and Salmonella spp. were found to be absent. T2 showed higher frequencies for the attributes color (90.0%) and overall acceptability (86.7%), while T3 showed higher frequencies for taste (86.7%) and texture (96.7%). The surimi <span class="hlt">concentration</span> was reflected in the physical properties of the sausages. It was found that the addition of MSTM surimi to sausage favored greater cutting strength (3.9 N for T2 and 4.9 N for T3). Beyond the surimi utilization, the total replacement of pig lard by cassava starch and soybean <span class="hlt">protein</span> had also contributed with the texture properties. PMID:24804055</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3951541','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3951541"><span id="translatedtitle">Low-fat frankfurters from <span class="hlt">protein</span> <span class="hlt">concentrates</span> of tilapia viscera and mechanically separated tilapia meat</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Cavenaghi-Altemio, Angela D; Alcade, Lígia B; Fonseca, Gustavo G</p> <p>2013-01-01</p> <p>In order to develop a healthy low-fat frankfurter-type sausage, different formulations were developed with tilapia viscera surimi (T1) and two with mechanically separated tilapia meat (MSTM) surimi (T2 and T3), all without pig lard addition. Due to technological problems observed for T1 sausage during cooking, it was not further investigated. The functionality of the other two formulations was evaluated based on proximate composition, pH, water activity, and texture. Finally, microbiological and sensory analyses based on acceptance tests were performed. Listeria monocytogenes and Salmonella spp. were found to be absent. T2 showed higher frequencies for the attributes color (90.0%) and overall acceptability (86.7%), while T3 showed higher frequencies for taste (86.7%) and texture (96.7%). The surimi <span class="hlt">concentration</span> was reflected in the physical properties of the sausages. It was found that the addition of MSTM surimi to sausage favored greater cutting strength (3.9 N for T2 and 4.9 N for T3). Beyond the surimi utilization, the total replacement of pig lard by cassava starch and soybean <span class="hlt">protein</span> had also contributed with the texture properties. PMID:24804055</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/7152949','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/7152949"><span id="translatedtitle">Activated charcoal filter counting for radioiodine effluent <span class="hlt">concentration</span> determination in <span class="hlt">protein</span> iodinations.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Button, T M; Hamilton, R G</p> <p>1982-12-01</p> <p>Regulatory agencies have recently placed emphasis upon quantification of 125I released to the environment during <span class="hlt">protein</span> iodinations at radioiodination facilities. This necessitates air sampling in order to determine the <span class="hlt">concentration</span> of 125I in the effluent. Air sample trapping mechanisms generally employed are activated charcoal filters. Difficulty arises in quantifying the activity of 125I trapped because of the attenuation of the 125I decay photons by the charcoal. Evaluation of the activity incident upon commercially available filters using a scintillation detector and large detector source separation is considered here. It is demonstrated that the activity in the filter may be treated as an exponential distribution within an attentuating matrix. This treatment essentially adds a constant correction factor to the counting efficiency of a given geometry for a filter-affluent flow rate combination. Finally, it is shown that an approximation assuming a uniform distribution of activity produces a large error in correction factor to the counting efficiency for the filters examined. PMID:7152949</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=2005PNAS..10218926W&link_type=ABSTRACT','NASAADS'); return false;" href="http://adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=2005PNAS..10218926W&link_type=ABSTRACT"><span id="translatedtitle"><span class="hlt">Absolute</span> rate theories of epigenetic stability</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Walczak, Aleksandra M.; Onuchic, José N.; Wolynes, Peter G.</p> <p>2005-12-01</p> <p>Spontaneous switching events in most characterized genetic switches are rare, resulting in extremely stable epigenetic properties. We show how simple arguments lead to theories of the rate of such events much like the <span class="hlt">absolute</span> rate theory of chemical reactions corrected by a transmission factor. Both the probability of the rare cellular states that allow epigenetic escape and the transmission factor depend on the rates of DNA binding and unbinding events and on the rates of <span class="hlt">protein</span> synthesis and degradation. Different mechanisms of escape from the stable attractors occur in the nonadiabatic, weakly adiabatic, and strictly adiabatic regimes, characterized by the relative values of those input rates. rate theory | stochastic gene expression | gene switches</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26028761','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26028761"><span id="translatedtitle">Effect of <span class="hlt">protein</span> <span class="hlt">concentrates</span>, emulsifiers on textural and sensory characteristics of gluten free cookies and its immunochemical validation.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Sarabhai, Swati; Indrani, D; Vijaykrishnaraj, M; Milind; Arun Kumar, V; Prabhasankar, P</p> <p>2015-06-01</p> <p>The effect of 5, 7.5 and 10 % <span class="hlt">protein</span> <span class="hlt">concentrates</span> namely soya <span class="hlt">protein</span> isolate (SPI), whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) and addition of 0.5 % emulsifiers such as glycerol monostearate (GMS), sodium stearoyl- 2- lactylate (SSL) and lecithin (LEC) on the rheological, sensory and textural characteristics of cookies with rice flour and its immunochemical validation was studied. The results showed that the use of 7.5 % SPI/WPC along with GMS significantly improved the quality characteristics of cookies with rice flour. Dot-Blot and Western-blot studies of cookies with 7.5 % of SPI or WPC confirmed that the anti-gliadin did not recognize these <span class="hlt">proteins</span>. Carry- through process using ELISA kit confirmed that gluten was within the permissible limit in all the stages of processing and hence these cookies can be consumed by people suffering from celiac disease.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/biblio/7023362','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/biblio/7023362"><span id="translatedtitle"><span class="hlt">Absolute</span> flux scale for radioastronomy</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>Ivanov, V.P.; Stankevich, K.S.</p> <p>1986-07-01</p> <p>The authors propose and provide support for a new <span class="hlt">absolute</span> flux scale for radio astronomy, which is not encumbered with the inadequacies of the previous scales. In constructing it the method of relative spectra was used (a powerful tool for choosing reference spectra). A review is given of previous flux scales. The authors compare the AIS scale with the scale they propose. Both scales are based on <span class="hlt">absolute</span> measurements by the ''artificial moon'' method, and they are practically coincident in the range from 0.96 to 6 GHz. At frequencies above 6 GHz, 0.96 GHz, the AIS scale is overestimated because of incorrect extrapolation of the spectra of the primary and secondary standards. The major results which have emerged from this review of <span class="hlt">absolute</span> scales in radio astronomy are summarized.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/18363977','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/18363977"><span id="translatedtitle">Effect of beta-casein, kappa-casein and beta-lactoglobulin genotypes on <span class="hlt">concentration</span> of milk <span class="hlt">protein</span> variants.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Hallén, E; Wedholm, A; Andrén, A; Lundén, A</p> <p>2008-04-01</p> <p>Individual mid-lactation milk samples were collected from 116 cows of the Swedish Red and Swedish Holstein breeds with known genotypes of beta-casein, kappa-casein and beta-lactoglobulin. Detailed milk <span class="hlt">protein</span> composition and allele-specific expression of beta-casein, kappa-casein and beta-lactoglobulin <span class="hlt">proteins</span> in milk were analysed using reversed-phase high-performance liquid chromatography. Aggregate beta-/kappa-casein genotype was significantly associated with the kappa-casein <span class="hlt">concentration</span> in milk. The lowest kappa-casein <span class="hlt">concentration</span> was found in milk of cows with genotypes including kappa-casein E (A(1)A(2)/AE, A(1)A(1)/AE) and also A(2)A(2)/AA milk, whereas highest levels were associated with genotypes including kappa-casein B. Casein number was positively and <span class="hlt">concentration</span> of beta-lactoglobulin negatively associated with the beta-lactoglobulin BB genotype. In heterozygote cows, beta-casein A(1) and beta-lactoglobulin A <span class="hlt">proteins</span> were found at higher <span class="hlt">concentrations</span> in milk compared with the <span class="hlt">protein</span> variant encoded by the alternative allele at these loci, whereas kappa-casein A and B variants were found at similar <span class="hlt">concentrations</span> in heterozygote AB cows.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25767825','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25767825"><span id="translatedtitle">Effects of storage time on total <span class="hlt">protein</span> and globulin <span class="hlt">concentrations</span> in bovine fresh frozen plasma obtained for transfusion.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Proverbio, D; Spada, E; Baggiani, L; Bagnagatti De Giorgi, G; Roggero, N; Belloli, A; Pravettoni, D; Perego, R</p> <p>2015-01-01</p> <p>To evaluate the effects of storage conditions on total <span class="hlt">protein</span> (TP) and globulin fractions in fresh frozen bovine plasma units prepared and stored for transfusion, TP and globulin fractions were evaluated in fresh plasma and at 1 month and 6 and 12 months after blood collection in plasma stored at -20°C. Significant differences in <span class="hlt">concentrations</span> were found in the median <span class="hlt">concentration</span> of total <span class="hlt">protein</span> (P=0.0336), between 0 months and 1 month (P=0.0108), 0 and 6 months (P=0.0023), and 0 and 12 months (P=0.0027), in mean <span class="hlt">concentration</span> (g/dL) of albumin (P=0.0394), between 0 months and 1 month (P=0.0131), 0 and 6 months (P=0.0035), and 0 and 12 months (P=0.0038), and beta-2 fraction (P=0.0401), between 0 and 6 months (P=0.0401) and 0 and 12 months (P=0.0230). This study suggests that total gamma globulin <span class="hlt">concentration</span> in bovine frozen plasma is stable for 12 months at -20°C. Total <span class="hlt">protein</span>, ALB, and beta-2 fraction have significantly different <span class="hlt">concentrations</span> (g/dL) when compared to prestorage. This study has shown IgG <span class="hlt">protein</span> fraction stability in bovine fresh frozen plasma collected for transfusion; therefore, bovine fresh frozen plasma seems to be suitable for the treatment of hypogammaglobulinemia (failure of passive transfer) in calves when stored for 12 months at -20°C.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/24324733','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/24324733"><span id="translatedtitle">Predicting the activity coefficients of free-solvent for <span class="hlt">concentrated</span> globular <span class="hlt">protein</span> solutions using independently determined physical parameters.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>McBride, Devin W; Rodgers, Victor G J</p> <p>2013-01-01</p> <p>The activity coefficient is largely considered an empirical parameter that was traditionally introduced to correct the non-ideality observed in thermodynamic systems such as osmotic pressure. Here, the activity coefficient of free-solvent is related to physically realistic parameters and a mathematical expression is developed to directly predict the activity coefficients of free-solvent, for aqueous <span class="hlt">protein</span> solutions up to near-saturation <span class="hlt">concentrations</span>. The model is based on the free-solvent model, which has previously been shown to provide excellent prediction of the osmotic pressure of <span class="hlt">concentrated</span> and crowded globular <span class="hlt">proteins</span> in aqueous solutions up to near-saturation <span class="hlt">concentrations</span>. Thus, this model uses only the independently determined, physically realizable quantities: mole fraction, solvent accessible surface area, and ion binding, in its prediction. Predictions are presented for the activity coefficients of free-solvent for near-saturated <span class="hlt">protein</span> solutions containing either bovine serum albumin or hemoglobin. As a verification step, the predictability of the model for the activity coefficient of sucrose solutions was evaluated. The predicted activity coefficients of free-solvent are compared to the calculated activity coefficients of free-solvent based on osmotic pressure data. It is observed that the predicted activity coefficients are increasingly dependent on the solute-solvent parameters as the <span class="hlt">protein</span> <span class="hlt">concentration</span> increases to near-saturation <span class="hlt">concentrations</span>.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/11681582','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/11681582"><span id="translatedtitle"><span class="hlt">Protein</span> adsorption on novel acrylamido-based polymeric ion-exchangers. III. Salt <span class="hlt">concentration</span> effects and elution behavior.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Hunter, A K; Carta, G</p> <p>2001-09-28</p> <p>The effect of salt <span class="hlt">concentration</span> on the adsorption and desorption of BSA has been determined for a polymeric anion-exchanger based on acrylamido monomers. The material investigated possesses a high adsorption capacity at low salt <span class="hlt">concentration</span> and the bound <span class="hlt">protein</span> can be recovered quantitatively at high salt <span class="hlt">concentrations</span>. The effects of salt on adsorption and desorption rates were evaluated from batch and shallow-bed experiments, and a model was developed to describe the data quantitatively. The adsorption capacity decreases as the salt <span class="hlt">concentration</span> is increased, but both adsorption and desorption rates increase at higher salt <span class="hlt">concentrations</span>. The predictability of the behavior of columns packed with this material was examined by comparing model predictions and experimental results obtained in laboratory columns. In general, a good agreement was obtained between predicted and experimental breakthrough and elution profiles, especially in shorter columns. Thus, the model allows a prediction of the effects of column length, mobile phase flow-rate, <span class="hlt">protein</span> feed <span class="hlt">concentration</span>, and salt <span class="hlt">concentration</span> on dynamic capacity, productivity, and on the <span class="hlt">concentration</span> of product fractions. PMID:11681582</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_15");'>15</a></li> <li><a href="#" onclick='return showDiv("page_16");'>16</a></li> <li class="active"><span>17</span></li> <li><a href="#" onclick='return showDiv("page_18");'>18</a></li> <li><a href="#" onclick='return showDiv("page_19");'>19</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_17 --> <div id="page_18" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_16");'>16</a></li> <li><a href="#" onclick='return showDiv("page_17");'>17</a></li> <li class="active"><span>18</span></li> <li><a href="#" onclick='return showDiv("page_19");'>19</a></li> <li><a href="#" onclick='return showDiv("page_20");'>20</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="341"> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=230599','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=230599"><span id="translatedtitle">A Common Missense Variant in the Glucokinase Regulatory <span class="hlt">Protein</span> Gene (GCKR) Is Associated with Increased Plasma Triglyceride and C-Reactive <span class="hlt">Protein</span> but Lower Fasting Glucose <span class="hlt">Concentrations</span></span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>OBJECTIVE-Using the genome-wide-association approach, we recently identified the glucokinase regulatory <span class="hlt">protein</span> gene (GCKR, rs780094) region as a novel quantitative trait locus for plasma triglyceride <span class="hlt">concentration</span> in Europeans. Here, we sought to study the association of GCKR variants with metaboli...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27166422','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27166422"><span id="translatedtitle">A repeat <span class="hlt">protein</span> links Rubisco to form the eukaryotic carbon-<span class="hlt">concentrating</span> organelle.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Mackinder, Luke C M; Meyer, Moritz T; Mettler-Altmann, Tabea; Chen, Vivian K; Mitchell, Madeline C; Caspari, Oliver; Freeman Rosenzweig, Elizabeth S; Pallesen, Leif; Reeves, Gregory; Itakura, Alan; Roth, Robyn; Sommer, Frederik; Geimer, Stefan; Mühlhaus, Timo; Schroda, Michael; Goodenough, Ursula; Stitt, Mark; Griffiths, Howard; Jonikas, Martin C</p> <p>2016-05-24</p> <p>Biological carbon fixation is a key step in the global carbon cycle that regulates the atmosphere's composition while producing the food we eat and the fuels we burn. Approximately one-third of global carbon fixation occurs in an overlooked algal organelle called the pyrenoid. The pyrenoid contains the CO2-fixing enzyme Rubisco and enhances carbon fixation by supplying Rubisco with a high <span class="hlt">concentration</span> of CO2 Since the discovery of the pyrenoid more that 130 y ago, the molecular structure and biogenesis of this ecologically fundamental organelle have remained enigmatic. Here we use the model green alga Chlamydomonas reinhardtii to discover that a low-complexity repeat <span class="hlt">protein</span>, Essential Pyrenoid Component 1 (EPYC1), links Rubisco to form the pyrenoid. We find that EPYC1 is of comparable abundance to Rubisco and colocalizes with Rubisco throughout the pyrenoid. We show that EPYC1 is essential for normal pyrenoid size, number, morphology, Rubisco content, and efficient carbon fixation at low CO2 We explain the central role of EPYC1 in pyrenoid biogenesis by the finding that EPYC1 binds Rubisco to form the pyrenoid matrix. We propose two models in which EPYC1's four repeats could produce the observed lattice arrangement of Rubisco in the Chlamydomonas pyrenoid. Our results suggest a surprisingly simple molecular mechanism for how Rubisco can be packaged to form the pyrenoid matrix, potentially explaining how Rubisco packaging into a pyrenoid could have evolved across a broad range of photosynthetic eukaryotes through convergent evolution. In addition, our findings represent a key step toward engineering a pyrenoid into crops to enhance their carbon fixation efficiency. PMID:27166422</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4889370','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4889370"><span id="translatedtitle">A repeat <span class="hlt">protein</span> links Rubisco to form the eukaryotic carbon-<span class="hlt">concentrating</span> organelle</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Mackinder, Luke C. M.; Meyer, Moritz T.; Mettler-Altmann, Tabea; Chen, Vivian K.; Mitchell, Madeline C.; Caspari, Oliver; Freeman Rosenzweig, Elizabeth S.; Pallesen, Leif; Reeves, Gregory; Itakura, Alan; Roth, Robyn; Sommer, Frederik; Geimer, Stefan; Mühlhaus, Timo; Schroda, Michael; Goodenough, Ursula; Stitt, Mark; Griffiths, Howard; Jonikas, Martin C.</p> <p>2016-01-01</p> <p>Biological carbon fixation is a key step in the global carbon cycle that regulates the atmosphere's composition while producing the food we eat and the fuels we burn. Approximately one-third of global carbon fixation occurs in an overlooked algal organelle called the pyrenoid. The pyrenoid contains the CO2-fixing enzyme Rubisco and enhances carbon fixation by supplying Rubisco with a high <span class="hlt">concentration</span> of CO2. Since the discovery of the pyrenoid more that 130 y ago, the molecular structure and biogenesis of this ecologically fundamental organelle have remained enigmatic. Here we use the model green alga Chlamydomonas reinhardtii to discover that a low-complexity repeat <span class="hlt">protein</span>, Essential Pyrenoid Component 1 (EPYC1), links Rubisco to form the pyrenoid. We find that EPYC1 is of comparable abundance to Rubisco and colocalizes with Rubisco throughout the pyrenoid. We show that EPYC1 is essential for normal pyrenoid size, number, morphology, Rubisco content, and efficient carbon fixation at low CO2. We explain the central role of EPYC1 in pyrenoid biogenesis by the finding that EPYC1 binds Rubisco to form the pyrenoid matrix. We propose two models in which EPYC1’s four repeats could produce the observed lattice arrangement of Rubisco in the Chlamydomonas pyrenoid. Our results suggest a surprisingly simple molecular mechanism for how Rubisco can be packaged to form the pyrenoid matrix, potentially explaining how Rubisco packaging into a pyrenoid could have evolved across a broad range of photosynthetic eukaryotes through convergent evolution. In addition, our findings represent a key step toward engineering a pyrenoid into crops to enhance their carbon fixation efficiency. PMID:27166422</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/23226133','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/23226133"><span id="translatedtitle">Heterogeneous kinetics of AKT signaling in individual cells are accounted for by variable <span class="hlt">protein</span> <span class="hlt">concentration</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Meyer, René; D'Alessandro, Lorenza A; Kar, Sandip; Kramer, Bernhard; She, Bin; Kaschek, Daniel; Hahn, Bettina; Wrangborg, David; Karlsson, Johan; Kvarnström, Mats; Jirstrand, Mats; Lehmann, Wolf-Dieter; Timmer, Jens; Höfer, Thomas; Klingmüller, Ursula</p> <p>2012-01-01</p> <p>In most solid cancers, cells harboring oncogenic mutations represent only a sub-fraction of the entire population. Within this sub-fraction the expression level of mutated <span class="hlt">proteins</span> can vary significantly due to cellular variability limiting the efficiency of targeted therapy. To address the causes of the heterogeneity, we performed a systematic analysis of one of the most frequently mutated pathways in cancer cells, the phosphatidylinositol 3 kinase (PI3K) signaling pathway. Among others PI3K signaling is activated by the hepatocyte growth factor (HGF) that regulates proliferation of hepatocytes during liver regeneration but also fosters tumor cell proliferation. HGF-mediated responses of PI3K signaling were monitored both at the single cell and cell population level in primary mouse hepatocytes and in the hepatoma cell line Hepa1_6. Interestingly, we observed that the HGF-mediated AKT responses at the level of individual cells is rather heterogeneous. However, the overall average behavior of the single cells strongly resembled the dynamics of AKT activation determined at the cell population level. To gain insights into the molecular cause for the observed heterogeneous behavior of individual cells, we employed dynamic mathematical modeling in a stochastic framework. Our analysis demonstrated that intrinsic noise was not sufficient to explain the observed kinetic behavior, but rather the importance of extrinsic noise has to be considered. Thus, distinct from gene expression in the examined signaling pathway fluctuations of the reaction rates has only a minor impact whereas variability in the <span class="hlt">concentration</span> of the various signaling components even in a clonal cell population is a key determinant for the kinetic behavior. PMID:23226133</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26547217','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26547217"><span id="translatedtitle">Vitamin D-binding <span class="hlt">protein</span> and free vitamin D <span class="hlt">concentrations</span> in acromegaly.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Altinova, Alev Eroglu; Ozkan, Cigdem; Akturk, Mujde; Gulbahar, Ozlem; Yalcin, Muhittin; Cakir, Nuri; Toruner, Fusun Balos</p> <p>2016-05-01</p> <p>Free 25-hydroxyvitamin D [25(OH)D] is suggested to be important in the determination of vitamin D deficiency, since vitamin D-binding <span class="hlt">protein</span> (VDBP) may affect total 25(OH)D levels. There are no data about free 25(OH)D <span class="hlt">concentrations</span> in acromegaly. We aimed to investigate serum VDBP and total and free 25(OH)D levels in patients with acromegaly in comparison with control subjects. We recruited 54 patients with acromegaly and 32 control subjects who were similar according to age, gender, and body mass index. Serum VDBP levels were found to be increased in patients with acromegaly compared to control subjects [90.35 (72.45-111.10) vs. 69.52 (63.89-80.13) mg/l, p = 0.001]. There was statistically no significant difference in serum total 25(OH)D levels between the patients with acromegaly and control subjects [18.63 (13.35-27.73) vs. 22.51 (19.20-28.96) ng/ml, p = 0.05]. Free 25(OH)D levels were significantly decreased in patients with acromegaly compared to control subjects [14.55 (10.45-21.45) vs. 17.75 (15.30-23.75) pg/ml, p = 0.03]. Free 25(OH)D levels correlated positively with total 25(OH)D (p = 0.0001) and HDL cholesterol (p = 0.04) and negatively with fasting blood glucose (p = 0.04). Our findings indicate that VDBP is increased and free 25(OH)D is decreased in acromegaly, while there is no significant alteration in total 25(OH)D.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/15905427','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/15905427"><span id="translatedtitle">Low-fat mozzarella as influenced by microbial exopolysaccharides, preacidification, and whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Zisu, B; Shah, N P</p> <p>2005-06-01</p> <p>Low-fat Mozzarella cheeses containing 6% fat were made by preacidification of milk, preacidification combined with exopolysaccharide- (EPS-) producing starter, used independently or as a coculture with non-EPS starter, and preacidification combined with whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) and EPS. The impact of these treatments on moisture retention, changes in texture profile analysis, cheese melt, stretch, and on pizza bake performance were investigated over 45 d of storage at 4 degrees C. Preacidified cheeses without EPS (control) had the lowest moisture content (53.75%). These cheeses were hardest and exhibited greatest springiness and chewiness. The meltability and stretchability of these cheeses increased most during the first 28 d of storage. The moisture content in cheeses increased to 55.08, 54.79, and 55.82% with EPS starter (containing 41.18 mg/g of EPS), coculturing (containing 28.61 mg/g of EPS), and WPC (containing 44.23 mg/g of EPS), respectively. Exopolysaccharide reduced hardness, springiness, and chewiness of low-fat cheeses made with preacidified milk in general and such cheeses exhibited an increase in cohesiveness and meltability. Although stretch distance was similar in all cheeses, those containing EPS were softer than the control. Cocultured cheeses exhibited the greatest meltability. Cheeses containing WPC were softest in general; however, hardness remained unchanged over 45 d. Cheeses made with WPC had the least increase in meltability over time. Incorporation of WPC did not reduce surface scorching or increase shred fusion of cheese shreds during pizza baking; however, there was an improvement in these properties between d 7 and 45. Coating of the cheese shreds with oil was necessary for adequate browning, melt, and flow characteristics in all cheese types.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27265171','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27265171"><span id="translatedtitle">Acid-responsive properties of fibrils from heat-induced whey <span class="hlt">protein</span> <span class="hlt">concentrate</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Xu, Hong-Hua; Wang, Jing; Dong, Shi-Rong; Cheng, Wen; Kong, Bao-Hua; Tan, Jun-Yan</p> <p>2016-08-01</p> <p>The heat-induced fibrils of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) have demonstrated an acid-responsive property; that is, the fibrils went through formation-depolymerization-reformation as pH was adjusted to 1.8, 6.5, and back to 1.8. We investigated the microstructure, driving force, and thermal stability of 3.0% (wt) WPC nanofibrils adjusted between pH 6.5 and 1.8 twice. The results showed that the nanofibrils had acid-responsive properties and good thermal stability after reheating for 10h at 90°C and adjusting pH from 1.8 to 6.5 to 1.8. The content of WPC fibril aggregates was not much different with the prolongation of heating times during pH variation. Although the nanofibrils' structure could be destroyed only by changing the pH, the essence of this destruction might only form fiber fragments, polymers that would restore a fibrous structure upon returning to pH 1.8. A described model for the acid-responsive assembly of fibrils of WPC was proposed. The fibrils went through formation-depolymerization-reformation by weaker noncovalent interactions (surface hydrophobicity) as pH changed from 1.8 to 6.5 back to 1.8. However, the fibrils lost the acid-responsive properties because much more S-S (disulfide) formation occurred when the solution was adjusted to pH 6.5 and reheated. Meanwhile, fibrils still possessed acid-responsive properties when reheated at pH 1.8, and the content of fibrils slightly increased with a further reduction of α-helix structure. PMID:27265171</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://eric.ed.gov/?q=Absolutism&pg=3&id=EJ265369','ERIC'); return false;" href="http://eric.ed.gov/?q=Absolutism&pg=3&id=EJ265369"><span id="translatedtitle">Relativistic <span class="hlt">Absolutism</span> in Moral Education.</span></a></p> <p><a target="_blank" href="http://www.eric.ed.gov/ERICWebPortal/search/extended.jsp?_pageLabel=advanced">ERIC Educational Resources Information Center</a></p> <p>Vogt, W. Paul</p> <p>1982-01-01</p> <p>Discusses Emile Durkheim's "Moral Education: A Study in the Theory and Application of the Sociology of Education," which holds that morally healthy societies may vary in culture and organization but must possess <span class="hlt">absolute</span> rules of moral behavior. Compares this moral theory with current theory and practice of American educators. (MJL)</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://ntrs.nasa.gov/search.jsp?R=19720027445&hterms=Phosphorus&qs=Ntx%3Dmode%2Bmatchall%26Ntk%3DAll%26N%3D0%26No%3D60%26Ntt%3DPhosphorus','NASA-TRS'); return false;" href="http://ntrs.nasa.gov/search.jsp?R=19720027445&hterms=Phosphorus&qs=Ntx%3Dmode%2Bmatchall%26Ntk%3DAll%26N%3D0%26No%3D60%26Ntt%3DPhosphorus"><span id="translatedtitle"><span class="hlt">Absolute</span> transition probabilities of phosphorus.</span></a></p> <p><a target="_blank" href="http://ntrs.nasa.gov/search.jsp">NASA Technical Reports Server (NTRS)</a></p> <p>Miller, M. H.; Roig, R. A.; Bengtson, R. D.</p> <p>1971-01-01</p> <p>Use of a gas-driven shock tube to measure the <span class="hlt">absolute</span> strengths of 21 P I lines and 126 P II lines (from 3300 to 6900 A). Accuracy for prominent, isolated neutral and ionic lines is estimated to be 28 to 40% and 18 to 30%, respectively. The data and the corresponding theoretical predictions are examined for conformity with the sum rules.-</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25114337','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25114337"><span id="translatedtitle">Chemical composition, molecular weight distribution, secondary structure and effect of NaCl on functional properties of walnut (Juglans regia L) <span class="hlt">protein</span> isolates and <span class="hlt">concentrates</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Mao, Xiao-Ying; Hua, Yu-Fei</p> <p>2014-08-01</p> <p>Chemical composition, molecular weight distribution, secondary structure and effect of sodium chloride <span class="hlt">concentration</span> on functional properties of walnut <span class="hlt">protein</span> isolates, <span class="hlt">concentrates</span> and defatted walnut flour were study. Compared with walnut <span class="hlt">protein</span> <span class="hlt">concentrates</span> (75.6%) and defatted walnut flour (52.5%), walnut <span class="hlt">protein</span> isolates contain a relatively high amount of <span class="hlt">protein</span> (90.5%). The yield of walnut <span class="hlt">protein</span> isolates and <span class="hlt">concentrates</span> was 43.2% and 76.6%, respectively. In molecular weight distribution study, Walnut <span class="hlt">protein</span> isolates showed one peak with molecular weight of 106.33 KDa (100%) and walnut <span class="hlt">protein</span> <span class="hlt">concentrates</span> showed four peaks with molecular weight of 16,725 KDa (0.8%),104.943 KDa(63.9%), 7.3 KDa (11.4%), 2.6 KDa (23.9%). The secondary structure of walnut <span class="hlt">protein</span> isolates was similar to that of walnut <span class="hlt">protein</span> <span class="hlt">concentrates</span>, but was differ from that of defatted walnut flour. The addition of sodium chloride (0 ~ 1 M) could improve the functionality of walnut <span class="hlt">protein</span> <span class="hlt">concentrates</span>, isolates and defatted walnut flour. The maximum solubility, water absorption capacity, emulsifying properties and foaming properties of walnut <span class="hlt">protein</span> isolates, <span class="hlt">concentrates</span> and defatted walnut flour were at sodium chloride solutions of 1.0 M, 0.6 M, 0.4 M, 0.6 M, respectively. The solubility of walnut <span class="hlt">protein</span> <span class="hlt">concentrates</span> (32.5%) in distilled water with 0 M sodium chloride was lower than that of walnut <span class="hlt">protein</span> isolates (35.2%). The maximum solubility of walnut <span class="hlt">protein</span> isolates, <span class="hlt">concentrates</span> and defatted walnut flour in solution were 36.8%, 33.7% and 9.6% at 1.0 M sodium chloride solutions, respectively. As compared with other vegetable <span class="hlt">proteins</span>, walnut <span class="hlt">protein</span> isolates and <span class="hlt">concentrates</span> exhibited better emulsifying properties and foam stability.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/25114337','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/25114337"><span id="translatedtitle">Chemical composition, molecular weight distribution, secondary structure and effect of NaCl on functional properties of walnut (Juglans regia L) <span class="hlt">protein</span> isolates and <span class="hlt">concentrates</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Mao, Xiao-Ying; Hua, Yu-Fei</p> <p>2014-08-01</p> <p>Chemical composition, molecular weight distribution, secondary structure and effect of sodium chloride <span class="hlt">concentration</span> on functional properties of walnut <span class="hlt">protein</span> isolates, <span class="hlt">concentrates</span> and defatted walnut flour were study. Compared with walnut <span class="hlt">protein</span> <span class="hlt">concentrates</span> (75.6%) and defatted walnut flour (52.5%), walnut <span class="hlt">protein</span> isolates contain a relatively high amount of <span class="hlt">protein</span> (90.5%). The yield of walnut <span class="hlt">protein</span> isolates and <span class="hlt">concentrates</span> was 43.2% and 76.6%, respectively. In molecular weight distribution study, Walnut <span class="hlt">protein</span> isolates showed one peak with molecular weight of 106.33 KDa (100%) and walnut <span class="hlt">protein</span> <span class="hlt">concentrates</span> showed four peaks with molecular weight of 16,725 KDa (0.8%),104.943 KDa(63.9%), 7.3 KDa (11.4%), 2.6 KDa (23.9%). The secondary structure of walnut <span class="hlt">protein</span> isolates was similar to that of walnut <span class="hlt">protein</span> <span class="hlt">concentrates</span>, but was differ from that of defatted walnut flour. The addition of sodium chloride (0 ~ 1 M) could improve the functionality of walnut <span class="hlt">protein</span> <span class="hlt">concentrates</span>, isolates and defatted walnut flour. The maximum solubility, water absorption capacity, emulsifying properties and foaming properties of walnut <span class="hlt">protein</span> isolates, <span class="hlt">concentrates</span> and defatted walnut flour were at sodium chloride solutions of 1.0 M, 0.6 M, 0.4 M, 0.6 M, respectively. The solubility of walnut <span class="hlt">protein</span> <span class="hlt">concentrates</span> (32.5%) in distilled water with 0 M sodium chloride was lower than that of walnut <span class="hlt">protein</span> isolates (35.2%). The maximum solubility of walnut <span class="hlt">protein</span> isolates, <span class="hlt">concentrates</span> and defatted walnut flour in solution were 36.8%, 33.7% and 9.6% at 1.0 M sodium chloride solutions, respectively. As compared with other vegetable <span class="hlt">proteins</span>, walnut <span class="hlt">protein</span> isolates and <span class="hlt">concentrates</span> exhibited better emulsifying properties and foam stability. PMID:25114337</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26124755','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26124755"><span id="translatedtitle">Cell age dependent <span class="hlt">concentration</span> of Escherichia coli divisome <span class="hlt">proteins</span> analyzed with ImageJ and ObjectJ.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Vischer, Norbert O E; Verheul, Jolanda; Postma, Marten; van den Berg van Saparoea, Bart; Galli, Elisa; Natale, Paolo; Gerdes, Kenn; Luirink, Joen; Vollmer, Waldemar; Vicente, Miguel; den Blaauwen, Tanneke</p> <p>2015-01-01</p> <p>The rod-shaped Gram-negative bacterium Escherichia coli multiplies by elongation followed by binary fission. Longitudinal growth of the cell envelope and synthesis of the new poles are organized by two <span class="hlt">protein</span> complexes called elongasome and divisome, respectively. We have analyzed the spatio-temporal localization patterns of many of these morphogenetic <span class="hlt">proteins</span> by immunolabeling the wild type strain MC4100 grown to steady state in minimal glucose medium at 28°C. This allowed the direct comparison of morphogenetic <span class="hlt">protein</span> localization patterns as a function of cell age as imaged by phase contrast and fluorescence wide field microscopy. Under steady state conditions the age distribution of the cells is constant and is directly correlated to cell length. To quantify cell size and <span class="hlt">protein</span> localization parameters in 1000s of labeled cells, we developed 'Coli-Inspector,' which is a project running under ImageJ with the plugin 'ObjectJ.' ObjectJ organizes image-analysis tasks using an integrated approach with the flexibility to produce different output formats from existing markers such as intensity data and geometrical parameters. ObjectJ supports the combination of automatic and interactive methods giving the user complete control over the method of image analysis and data collection, with visual inspection tools for quick elimination of artifacts. Coli-inspector was used to sort the cells according to division cycle cell age and to analyze the spatio-temporal localization pattern of each <span class="hlt">protein</span>. A unique dataset has been created on the <span class="hlt">concentration</span> and position of the <span class="hlt">proteins</span> during the cell cycle. We show for the first time that a subset of morphogenetic <span class="hlt">proteins</span> have a constant cellular <span class="hlt">concentration</span> during the cell division cycle whereas another set exhibits a cell division cycle dependent <span class="hlt">concentration</span> variation. Using the number of <span class="hlt">proteins</span> present at midcell, the stoichiometry of the divisome is discussed.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26124755','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26124755"><span id="translatedtitle">Cell age dependent <span class="hlt">concentration</span> of Escherichia coli divisome <span class="hlt">proteins</span> analyzed with ImageJ and ObjectJ.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Vischer, Norbert O E; Verheul, Jolanda; Postma, Marten; van den Berg van Saparoea, Bart; Galli, Elisa; Natale, Paolo; Gerdes, Kenn; Luirink, Joen; Vollmer, Waldemar; Vicente, Miguel; den Blaauwen, Tanneke</p> <p>2015-01-01</p> <p>The rod-shaped Gram-negative bacterium Escherichia coli multiplies by elongation followed by binary fission. Longitudinal growth of the cell envelope and synthesis of the new poles are organized by two <span class="hlt">protein</span> complexes called elongasome and divisome, respectively. We have analyzed the spatio-temporal localization patterns of many of these morphogenetic <span class="hlt">proteins</span> by immunolabeling the wild type strain MC4100 grown to steady state in minimal glucose medium at 28°C. This allowed the direct comparison of morphogenetic <span class="hlt">protein</span> localization patterns as a function of cell age as imaged by phase contrast and fluorescence wide field microscopy. Under steady state conditions the age distribution of the cells is constant and is directly correlated to cell length. To quantify cell size and <span class="hlt">protein</span> localization parameters in 1000s of labeled cells, we developed 'Coli-Inspector,' which is a project running under ImageJ with the plugin 'ObjectJ.' ObjectJ organizes image-analysis tasks using an integrated approach with the flexibility to produce different output formats from existing markers such as intensity data and geometrical parameters. ObjectJ supports the combination of automatic and interactive methods giving the user complete control over the method of image analysis and data collection, with visual inspection tools for quick elimination of artifacts. Coli-inspector was used to sort the cells according to division cycle cell age and to analyze the spatio-temporal localization pattern of each <span class="hlt">protein</span>. A unique dataset has been created on the <span class="hlt">concentration</span> and position of the <span class="hlt">proteins</span> during the cell cycle. We show for the first time that a subset of morphogenetic <span class="hlt">proteins</span> have a constant cellular <span class="hlt">concentration</span> during the cell division cycle whereas another set exhibits a cell division cycle dependent <span class="hlt">concentration</span> variation. Using the number of <span class="hlt">proteins</span> present at midcell, the stoichiometry of the divisome is discussed. PMID:26124755</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4462998','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4462998"><span id="translatedtitle">Cell age dependent <span class="hlt">concentration</span> of Escherichia coli divisome <span class="hlt">proteins</span> analyzed with ImageJ and ObjectJ</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Vischer, Norbert O. E.; Verheul, Jolanda; Postma, Marten; van den Berg van Saparoea, Bart; Galli, Elisa; Natale, Paolo; Gerdes, Kenn; Luirink, Joen; Vollmer, Waldemar; Vicente, Miguel; den Blaauwen, Tanneke</p> <p>2015-01-01</p> <p>The rod-shaped Gram-negative bacterium Escherichia coli multiplies by elongation followed by binary fission. Longitudinal growth of the cell envelope and synthesis of the new poles are organized by two <span class="hlt">protein</span> complexes called elongasome and divisome, respectively. We have analyzed the spatio-temporal localization patterns of many of these morphogenetic <span class="hlt">proteins</span> by immunolabeling the wild type strain MC4100 grown to steady state in minimal glucose medium at 28°C. This allowed the direct comparison of morphogenetic <span class="hlt">protein</span> localization patterns as a function of cell age as imaged by phase contrast and fluorescence wide field microscopy. Under steady state conditions the age distribution of the cells is constant and is directly correlated to cell length. To quantify cell size and <span class="hlt">protein</span> localization parameters in 1000s of labeled cells, we developed ‘Coli-Inspector,’ which is a project running under ImageJ with the plugin ‘ObjectJ.’ ObjectJ organizes image-analysis tasks using an integrated approach with the flexibility to produce different output formats from existing markers such as intensity data and geometrical parameters. ObjectJ supports the combination of automatic and interactive methods giving the user complete control over the method of image analysis and data collection, with visual inspection tools for quick elimination of artifacts. Coli-inspector was used to sort the cells according to division cycle cell age and to analyze the spatio-temporal localization pattern of each <span class="hlt">protein</span>. A unique dataset has been created on the <span class="hlt">concentration</span> and position of the <span class="hlt">proteins</span> during the cell cycle. We show for the first time that a subset of morphogenetic <span class="hlt">proteins</span> have a constant cellular <span class="hlt">concentration</span> during the cell division cycle whereas another set exhibits a cell division cycle dependent <span class="hlt">concentration</span> variation. Using the number of <span class="hlt">proteins</span> present at midcell, the stoichiometry of the divisome is discussed. PMID:26124755</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/biblio/1053357','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/biblio/1053357"><span id="translatedtitle">Atomic detail brownian dynamics simulations of <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions with a mean field treatment of hydrodynamic interactions.</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>Mereghetti, Paolo; Wade, Rebecca C.</p> <p>2012-07-26</p> <p>High macromolecular <span class="hlt">concentrations</span> are a distinguishing feature of living organisms. Understanding how the high <span class="hlt">concentration</span> of solutes affects the dynamic properties of biological macromolecules is fundamental for the comprehension of biological processes in living systems. In this paper, we describe the implementation of mean field models of translational and rotational hydrodynamic interactions into an atomically detailed many-<span class="hlt">protein</span> brownian dynamics simulation method. <span class="hlt">Concentrated</span> solutions (30-40% volume fraction) of myoglobin, hemoglobin A, and sickle cell hemoglobin S were simulated, and static structure factors, oligomer formation, and translational and rotational self-diffusion coefficients were computed. Good agreement of computed properties with available experimental data was obtained. The results show the importance of both solvent mediated interactions and weak <span class="hlt">protein-protein</span> interactions for accurately describing the dynamics and the association properties of <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions. Specifically, they show a qualitative difference in the translational and rotational dynamics of the systems studied. Although the translational diffusion coefficient is controlled by macromolecular shape and hydrodynamic interactions, the rotational diffusion coefficient is affected by macromolecular shape, direct intermolecular interactions, and both translational and rotational hydrodynamic interactions.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=292398','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=292398"><span id="translatedtitle">Effects of dietary <span class="hlt">protein</span> <span class="hlt">concentration</span> on ammonia volatilization, nitrate leaching, and plant nitrogen uptake from dairy manure applied to lysimeters</span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>This lysimeter experiment was designed to investigate the effects of dietary crude <span class="hlt">protein</span> (CP) <span class="hlt">concentration</span> on nitrate-N (NO3-N) and ammonia (NH3) losses from dairy manure applied to soil and manure N use for plant growth. Lactating dairy cows were fed diets with 16.7 (HighCP) or 14.8% (LowCP) cru...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=288933','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=288933"><span id="translatedtitle">Performance enhancement of poly(lactic acid)/soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> blends by promoting formation of network structure</span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>In this work, the effects of water content in preformulated soy <span class="hlt">protein</span> <span class="hlt">concentrate</span> (SPC) and of SPC content on the thermal, rheological and mechanical properties and morphology of poly(lactic acid) (PLA)/SPC blends were studied. The blends were prepared by twin screw compounding and the test specim...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/6506092','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/6506092"><span id="translatedtitle">Serum and tissue thiocyanate <span class="hlt">concentrations</span> in growing pigs fed cassava peel or corn based diets containing graded <span class="hlt">protein</span> levels.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Tewe, O O</p> <p>1984-11-01</p> <p>Thiocyanate <span class="hlt">concentrations</span> of serum, liver, kidney, spleen and longissimus dorsi were determined in 64 growing Large White x Landrace pigs offered 8 experimental isocaloric diets containing different levels of cassava peel and crude <span class="hlt">protein</span>. Cassava peel increased serum thiocyanate on day 60 (P less than 0.01) and day 90 (P less than 0.01) of the trial, while the crude <span class="hlt">protein</span> level increased it (P less than 0.05) on days 30 and 90, respectively. Interaction of the two factors was significant on day 30 (P less than 0.05) and day 90 (P less than 0.05). There was a correlation between cyanide intake and serum thiocyanate level. Coefficient of determination revealed that cyanide alone accounted for 28.5; 60.6 and 48.8% variation in serum thiocyanate on days 30, 60 and 90, respectively. Liver, spleen and longissimus dorsi thiocyanate were affected by dietary <span class="hlt">protein</span> intake (P less than 0.05). Thiocyanate <span class="hlt">concentration</span> was higher (P less than 0.05) on cassava peel diet. Generally, crude <span class="hlt">protein</span> at 5% reduced organ and muscle thiocyanate <span class="hlt">concentrations</span>. A diet containing 112.2-117.3 mg/kg hydrocyanic acid (HCN) affected serum but not organ and muscle thiocyanate in <span class="hlt">protein</span>-sufficient diets. PMID:6506092</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3945107','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3945107"><span id="translatedtitle">Temporal Dynamics of Microbial Rhodopsin Fluorescence Reports <span class="hlt">Absolute</span> Membrane Voltage</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Hou, Jennifer H.; Venkatachalam, Veena; Cohen, Adam E.</p> <p>2014-01-01</p> <p>Plasma membrane voltage is a fundamentally important property of a living cell; its value is tightly coupled to membrane transport, the dynamics of transmembrane <span class="hlt">proteins</span>, and to intercellular communication. Accurate measurement of the membrane voltage could elucidate subtle changes in cellular physiology, but existing genetically encoded fluorescent voltage reporters are better at reporting relative changes than <span class="hlt">absolute</span> numbers. We developed an Archaerhodopsin-based fluorescent voltage sensor whose time-domain response to a stepwise change in illumination encodes the <span class="hlt">absolute</span> membrane voltage. We validated this sensor in human embryonic kidney cells. Measurements were robust to variation in imaging parameters and in gene expression levels, and reported voltage with an <span class="hlt">absolute</span> accuracy of 10 mV. With further improvements in membrane trafficking and signal amplitude, time-domain encoding of <span class="hlt">absolute</span> voltage could be applied to investigate many important and previously intractable bioelectric phenomena. PMID:24507604</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/22062917','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/22062917"><span id="translatedtitle">Optimization of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> and sodium chloride <span class="hlt">concentrations</span> and cooking temperature of sous vide cooked whole-muscle beef from Argentina.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Szerman, N; Gonzalez, C B; Sancho, A M; Grigioni, G; Carduza, F; Vaudagna, S R</p> <p>2008-07-01</p> <p>Response surface methodology was used to optimize the effect of cooking temperature (CT: 65-75°C) and the incorporation of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC: 0-3.5%) and sodium chloride (NaCl: 0-2.5%) on technological, physical and sensory characteristics of cooked whole-muscle beef. Post-injection weight loss diminished when NaCl <span class="hlt">concentration</span> increased. Moreover, the increment of both additives produced a reduction of cooking loss. An opposite effect was observed with the increment of CT. As it was expected, a total yield improvement was achieved by increasing both ingredients and diminishing CT. Equivalent yields are achieved complementing both ingredients, meaning that if one ingredient <span class="hlt">concentration</span> is reduced the other has to be increased. Shear force values were not affected by the studied factors. Instead, lightness was reduced by their increment. At 65°C, injected muscles had lower flavour and odour scores than control. At all CT analyzed, the incorporated brines improved juiciness and tenderness-related attributes. Present results recommend the use of a CT of 70°C and maxima WPC and NaCl <span class="hlt">concentrations</span> of 2.6% and 1.9%, respectively. PMID:22062917</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_16");'>16</a></li> <li><a href="#" onclick='return showDiv("page_17");'>17</a></li> <li class="active"><span>18</span></li> <li><a href="#" onclick='return showDiv("page_19");'>19</a></li> <li><a href="#" onclick='return showDiv("page_20");'>20</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_18 --> <div id="page_19" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_17");'>17</a></li> <li><a href="#" onclick='return showDiv("page_18");'>18</a></li> <li class="active"><span>19</span></li> <li><a href="#" onclick='return showDiv("page_20");'>20</a></li> <li><a href="#" onclick='return showDiv("page_21");'>21</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="361"> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/22062917','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/22062917"><span id="translatedtitle">Optimization of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> and sodium chloride <span class="hlt">concentrations</span> and cooking temperature of sous vide cooked whole-muscle beef from Argentina.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Szerman, N; Gonzalez, C B; Sancho, A M; Grigioni, G; Carduza, F; Vaudagna, S R</p> <p>2008-07-01</p> <p>Response surface methodology was used to optimize the effect of cooking temperature (CT: 65-75°C) and the incorporation of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC: 0-3.5%) and sodium chloride (NaCl: 0-2.5%) on technological, physical and sensory characteristics of cooked whole-muscle beef. Post-injection weight loss diminished when NaCl <span class="hlt">concentration</span> increased. Moreover, the increment of both additives produced a reduction of cooking loss. An opposite effect was observed with the increment of CT. As it was expected, a total yield improvement was achieved by increasing both ingredients and diminishing CT. Equivalent yields are achieved complementing both ingredients, meaning that if one ingredient <span class="hlt">concentration</span> is reduced the other has to be increased. Shear force values were not affected by the studied factors. Instead, lightness was reduced by their increment. At 65°C, injected muscles had lower flavour and odour scores than control. At all CT analyzed, the incorporated brines improved juiciness and tenderness-related attributes. Present results recommend the use of a CT of 70°C and maxima WPC and NaCl <span class="hlt">concentrations</span> of 2.6% and 1.9%, respectively.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/25640969','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/25640969"><span id="translatedtitle"><span class="hlt">Protein</span> body formation in leaves of Nicotiana benthamiana: a <span class="hlt">concentration</span>-dependent mechanism influenced by the presence of fusion tags.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Saberianfar, Reza; Joensuu, Jussi J; Conley, Andrew J; Menassa, Rima</p> <p>2015-09-01</p> <p><span class="hlt">Protein</span> bodies (PBs) are endoplasmic reticulum (ER) derived organelles originally found in seeds whose function is to accumulate seed storage <span class="hlt">proteins</span>. It has been shown that PB formation is not limited to seeds and green fluorescent <span class="hlt">protein</span> (GFP) fused to either elastin-like polypeptide (ELP) or hydrophobin (HFBI) fusion tags induce the formation of PBs in leaves of N. benthamiana. In this study, we compared the ELP- and HFBI-induced PBs and showed that ELP-induced PBs are larger than HFBI-induced PBs. The size of ELP- and HFBI-induced PBs increased over time along with the accumulation levels of their fused <span class="hlt">protein</span>. Our results show that PB formation is a <span class="hlt">concentration</span>-dependent mechanism in which <span class="hlt">proteins</span> accumulating at levels higher than 0.2% of total soluble <span class="hlt">protein</span> are capable of inducing PBs in vivo. Our results show that the presence of fusion tags is not necessary for the formation of PBs, but affects the distribution pattern and size of PBs. This was confirmed by PBs induced by fluorescent <span class="hlt">proteins</span> as well as fungal xylanases. We noticed that in the process of PB formation, secretory and ER-resident molecules are passively sequestered into the lumen of PBs. We propose to use this property of PBs as a tool to increase the accumulation levels of erythropoietin and human interleukin-10 by co-expression with PB-inducing <span class="hlt">proteins</span>. PMID:25640969</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25859422','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25859422"><span id="translatedtitle">Comparison of cake compositions, pepsin digestibility and amino acids <span class="hlt">concentration</span> of <span class="hlt">proteins</span> isolated from black mustard and yellow mustard cakes.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Sarker, Ashish Kumar; Saha, Dipti; Begum, Hasina; Zaman, Asaduz; Rahman, Md Mashiar</p> <p>2015-01-01</p> <p>As a byproduct of oil production, black and yellow mustard cakes <span class="hlt">protein</span> are considered as potential source of plant <span class="hlt">protein</span> for feed applications to poultry, fish and swine industries. The <span class="hlt">protein</span> contents in black and yellow mustard cakes were 38.17% and 28.80% and their pepsin digestibility was 80.33% and 77.43%, respectively. The <span class="hlt">proteins</span> were extracted at different pH and maximum <span class="hlt">proteins</span> (89.13% of 38.17% and 87.76% of 28.80% respectively) isolated from black and yellow mustard cakes at pH 12. The purity of isolated <span class="hlt">proteins</span> of black and yellow mustard cakes was 89.83% and 91.12% respectively and their pepsin digestibility was 89.67% and 90.17% respectively which assigned the absence of antinutritional compounds. It was found that essential amino acids isoleucine, lysine, methionine, threonine and tryptophan and non essential amino acids arginine and tyrosine were present in greater <span class="hlt">concentration</span> in black mustard cake <span class="hlt">protein</span> whereas other amino acids were higher in yellow mustard cake <span class="hlt">protein</span>.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/10777248','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/10777248"><span id="translatedtitle">Toxic effects of zinc from trout farm sediments on ATP, <span class="hlt">protein</span>, and hemoglobin <span class="hlt">concentrations</span> of Limnodrilus hoffmeisteri.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Martinez-Tabche, L; Gutiérrez Cabrera, I; Gómez Oliván, L; Galar Martinez, M; Germán Faz, C</p> <p>2000-04-14</p> <p>Zinc (Zn) is a nutritionally essential metal, and deficiency results in severe health consequences to aquatic organisms. In this study toxicity data for Limnodrilus hoffmeisteri produced by Zn in systems using three natural sediments (trout farms: El Oyamel, El Truchón, and El Potrero) are presented. Hemoglobin, adenosine triphosphate (ATP), and <span class="hlt">protein</span> <span class="hlt">concentrations</span> were measured in L. hoffmeisteri exposed to spiked sediments, as indicators of exposure. Physicochemical characteristics of water and sediments were also considered. Zn <span class="hlt">concentrations</span> were measured in water and sediment. El Oyamel, El Truchón, and El Potrero pond sediments did not have similar physicochemical characteristics. Zn <span class="hlt">concentrations</span> of water obtained from the rustic ponds were near 0.4575 mg/L; however, this metal was always found to be higher in the sediments (0.0271-0.9754 mg/kg). The bioassay with worms demonstrated that pond sediments from El Oyamel, El Potrero, and El Truchón produced toxicity since ATP and <span class="hlt">protein</span> <span class="hlt">concentrations</span> were low compared to controls (organisms without metal). All spiked sediments had a significant reduction effect on ATP, <span class="hlt">protein</span>, and hemoglobin <span class="hlt">concentrations</span>. This investigation clearly shows that sediments of El Truchón, El Oyamel, and El Potrero possess toxicity potential. These results suggest the usefulness of these bioassays to evaluate the toxicity of sediments polluted with heavy metals. PMID:10777248</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2016NatSR...633556S','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2016NatSR...633556S"><span id="translatedtitle">External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of <span class="hlt">proteins</span> at low <span class="hlt">concentrations</span></span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Schwaighofer, Andreas; Alcaráz, Mirta R.; Araman, Can; Goicoechea, Héctor; Lendl, Bernhard</p> <p>2016-09-01</p> <p>Fourier transform infrared (FTIR) and circular dichroism (CD) spectroscopy are analytical techniques employed for the analysis of <span class="hlt">protein</span> secondary structure. The use of CD spectroscopy is limited to low <span class="hlt">protein</span> <span class="hlt">concentrations</span> (<2 mg ml‑1), while FTIR spectroscopy is commonly used in a higher <span class="hlt">concentration</span> range (>5 mg ml‑1). Here we introduce a quantum cascade laser (QCL)-based IR transmission setup for analysis of <span class="hlt">protein</span> and polypeptide secondary structure at <span class="hlt">concentrations</span> as low as 0.25 mg ml‑1 in deuterated buffer solution. We present dynamic QCL-IR spectra of the temperature-induced α-helix to β-sheet transition of poly-L-lysine. The <span class="hlt">concentration</span> dependence of the α-β transition temperature between 0.25 and 10 mg ml‑1 was investigated by QCL-IR, FTIR and CD spectroscopy. By using QCL-IR spectroscopy it is possible to perform IR spectroscopic analysis in the same <span class="hlt">concentration</span> range as CD spectroscopy, thus enabling a combined analysis of biomolecules secondary structure by CD and IR spectroscopy.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27633337','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27633337"><span id="translatedtitle">External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of <span class="hlt">proteins</span> at low <span class="hlt">concentrations</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Schwaighofer, Andreas; Alcaráz, Mirta R; Araman, Can; Goicoechea, Héctor; Lendl, Bernhard</p> <p>2016-09-16</p> <p>Fourier transform infrared (FTIR) and circular dichroism (CD) spectroscopy are analytical techniques employed for the analysis of <span class="hlt">protein</span> secondary structure. The use of CD spectroscopy is limited to low <span class="hlt">protein</span> <span class="hlt">concentrations</span> (<2 mg ml(-1)), while FTIR spectroscopy is commonly used in a higher <span class="hlt">concentration</span> range (>5 mg ml(-1)). Here we introduce a quantum cascade laser (QCL)-based IR transmission setup for analysis of <span class="hlt">protein</span> and polypeptide secondary structure at <span class="hlt">concentrations</span> as low as 0.25 mg ml(-1) in deuterated buffer solution. We present dynamic QCL-IR spectra of the temperature-induced α-helix to β-sheet transition of poly-L-lysine. The <span class="hlt">concentration</span> dependence of the α-β transition temperature between 0.25 and 10 mg ml(-1) was investigated by QCL-IR, FTIR and CD spectroscopy. By using QCL-IR spectroscopy it is possible to perform IR spectroscopic analysis in the same <span class="hlt">concentration</span> range as CD spectroscopy, thus enabling a combined analysis of biomolecules secondary structure by CD and IR spectroscopy.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27633337','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27633337"><span id="translatedtitle">External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of <span class="hlt">proteins</span> at low <span class="hlt">concentrations</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Schwaighofer, Andreas; Alcaráz, Mirta R; Araman, Can; Goicoechea, Héctor; Lendl, Bernhard</p> <p>2016-01-01</p> <p>Fourier transform infrared (FTIR) and circular dichroism (CD) spectroscopy are analytical techniques employed for the analysis of <span class="hlt">protein</span> secondary structure. The use of CD spectroscopy is limited to low <span class="hlt">protein</span> <span class="hlt">concentrations</span> (<2 mg ml(-1)), while FTIR spectroscopy is commonly used in a higher <span class="hlt">concentration</span> range (>5 mg ml(-1)). Here we introduce a quantum cascade laser (QCL)-based IR transmission setup for analysis of <span class="hlt">protein</span> and polypeptide secondary structure at <span class="hlt">concentrations</span> as low as 0.25 mg ml(-1) in deuterated buffer solution. We present dynamic QCL-IR spectra of the temperature-induced α-helix to β-sheet transition of poly-L-lysine. The <span class="hlt">concentration</span> dependence of the α-β transition temperature between 0.25 and 10 mg ml(-1) was investigated by QCL-IR, FTIR and CD spectroscopy. By using QCL-IR spectroscopy it is possible to perform IR spectroscopic analysis in the same <span class="hlt">concentration</span> range as CD spectroscopy, thus enabling a combined analysis of biomolecules secondary structure by CD and IR spectroscopy. PMID:27633337</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=5025714','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=5025714"><span id="translatedtitle">External cavity-quantum cascade laser infrared spectroscopy for secondary structure analysis of <span class="hlt">proteins</span> at low <span class="hlt">concentrations</span></span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Schwaighofer, Andreas; Alcaráz, Mirta R.; Araman, Can; Goicoechea, Héctor; Lendl, Bernhard</p> <p>2016-01-01</p> <p>Fourier transform infrared (FTIR) and circular dichroism (CD) spectroscopy are analytical techniques employed for the analysis of <span class="hlt">protein</span> secondary structure. The use of CD spectroscopy is limited to low <span class="hlt">protein</span> <span class="hlt">concentrations</span> (<2 mg ml−1), while FTIR spectroscopy is commonly used in a higher <span class="hlt">concentration</span> range (>5 mg ml−1). Here we introduce a quantum cascade laser (QCL)-based IR transmission setup for analysis of <span class="hlt">protein</span> and polypeptide secondary structure at <span class="hlt">concentrations</span> as low as 0.25 mg ml−1 in deuterated buffer solution. We present dynamic QCL-IR spectra of the temperature-induced α-helix to β-sheet transition of poly-L-lysine. The <span class="hlt">concentration</span> dependence of the α-β transition temperature between 0.25 and 10 mg ml−1 was investigated by QCL-IR, FTIR and CD spectroscopy. By using QCL-IR spectroscopy it is possible to perform IR spectroscopic analysis in the same <span class="hlt">concentration</span> range as CD spectroscopy, thus enabling a combined analysis of biomolecules secondary structure by CD and IR spectroscopy. PMID:27633337</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4109875','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4109875"><span id="translatedtitle">Identification of Differentially Expressed <span class="hlt">Proteins</span> in Liver in Response to Subacute Ruminal Acidosis (SARA) Induced by High-<span class="hlt">concentrate</span> Diet</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Jiang, X. Y.; Ni, Y. D.; Zhang, S. K.; Zhang, Y. S.; Shen, X. Z.</p> <p>2014-01-01</p> <p>The aim of this study was to evaluate <span class="hlt">protein</span> expression patterns of liver in response to subacute ruminal acidosis (SARA) induced by high-<span class="hlt">concentrate</span> diet. Sixteen healthy mid-lactating goats were randomly divided into 2 groups and fed either a high-forage (HF) diet or a high-<span class="hlt">concentrate</span> (HC) diet. The HC diet was expected to induce SARA. After ensuring the occurrence of SARA, liver samples were collected. Proteome analysis with differential in gel electrophoresis technology revealed that, 15 <span class="hlt">proteins</span> were significantly modulated in liver in a comparison between HF and HC-fed goats. These <span class="hlt">proteins</span> were found mainly associated with metabolism and energy transfer after identified by matrix-assisted laser desorption ionization/time of flight. The results indicated that glucose, lipid and <span class="hlt">protein</span> catabolism could be enhanced when SARA occurred. It prompted that glucose, lipid and amine acid in the liver mainly participated in oxidation and energy supply when SARA occurred, which possibly consumed more precursors involved in milk <span class="hlt">protein</span> and milk fat synthesis. These results suggest new candidate <span class="hlt">proteins</span> that may contribute to a better understanding of the mechanisms that mediate liver adaptation to SARA. PMID:25083113</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=362454','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=362454"><span id="translatedtitle">hsp82 is an essential <span class="hlt">protein</span> that is required in higher <span class="hlt">concentrations</span> for growth of cells at higher temperatures.</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Borkovich, K A; Farrelly, F W; Finkelstein, D B; Taulien, J; Lindquist, S</p> <p>1989-01-01</p> <p>hsp82 is one of the most highly conserved and abundantly synthesized heat shock <span class="hlt">proteins</span> of eucaryotic cells. The yeast Saccharomyces cerevisiae contains two closely related genes in the HSP82 gene family. HSC82 was expressed constitutively at a very high level and was moderately induced by high temperatures. HSP82 was expressed constitutively at a much lower level and was more strongly induced by heat. Site-directed disruption mutations were produced in both genes. Cells homozygous for both mutations did not grow at any temperature. Cells carrying other combinations of the HSP82 and HSC82 mutations grew well at 25 degrees C, but their ability to grow at higher temperatures varied with gene copy number. Thus, HSP82 and HSC82 constitute an essential gene family in yeast cells. Although the two <span class="hlt">proteins</span> had different patterns of expression, they appeared to have equivalent functions; growth at higher temperatures required higher <span class="hlt">concentrations</span> of either <span class="hlt">protein</span>. Biochemical analysis of hsp82 from vertebrate cells suggests that the <span class="hlt">protein</span> binds to a variety of other cellular <span class="hlt">proteins</span>, keeping them inactive until they have reached their proper intracellular location or have received the proper activation signal. We speculate that the reason cells require higher <span class="hlt">concentrations</span> of hsp82 or hsc82 for growth at higher temperatures is to maintain proper levels of complex formation with these other <span class="hlt">proteins</span>. Images PMID:2674684</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/24930024','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/24930024"><span id="translatedtitle">The degree of resistance of erythrocyte membrane cytoskeletal <span class="hlt">proteins</span> to supra-physiologic <span class="hlt">concentrations</span> of calcium: an in vitro study.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Mostafavi, Ebrahim; Nargesi, Arash Aghajani; Ghazizadeh, Zaniar; Larry, Mehrdad; Farahani, Roya Horabad; Morteza, Afsaneh; Esteghamati, Alireza; Vigneron, Claude; Nakhjavani, Manouchehr</p> <p>2014-08-01</p> <p>Calcium is a key regulator of cell dynamics. Dysregulation of its cytosolic <span class="hlt">concentration</span> is implicated in the pathophysiology of several diseases. This study aimed to assess the effects of calcium on the network of membrane cytoskeletal <span class="hlt">proteins</span>. Erythrocyte membranes were obtained from eight healthy donors and incubated with 250 µM and 1.25 mM calcium solutions. Membrane cytoskeletal <span class="hlt">proteins</span> were quantified using SDS-PAGE at baseline and after 3 and 5 days of incubation. Supra-physiologic <span class="hlt">concentrations</span> of calcium (1.25 mM) induced a significant proteolysis in membrane cytoskeletal <span class="hlt">proteins</span>, compared with magnesium (p < 0.001). Actin exhibited the highest sensitivity to calcium-induced proteolysis (6.8 ± 0.3 vs. 5.3 ± 0.6, p < 0.001), while spectrin (39.9 ± 1.0 vs. 40.3 ± 2.0, p = 0.393) and band-6 (6.3 ± 0.3 vs. 6.8 ± 0.8, p = 0.191) were more resistant to proteolysis after incubation with calcium in the range of endoplasmic reticulum <span class="hlt">concentrations</span> (250 µM). Aggregation of membrane cytoskeletal <span class="hlt">proteins</span> was determined after centrifugation and was significantly higher after incubation with calcium ions compared with control, EDTA and magnesium solutions (p < 0.001). In a supra-physiologic range of 1.25-10 mM of calcium ions, there was a nearly perfect linear relationship between calcium <span class="hlt">concentration</span> and aggregation of erythrocyte membrane cytoskeletal <span class="hlt">proteins</span> (R(2) = 0.971, p < 0.001). Our observation suggests a strong interaction between calcium ions and membrane cytoskeletal network. Cumulative effects of disrupted calcium homeostasis on cytoskeletal <span class="hlt">proteins</span> need to be further investigated at extended periods of time in disease states.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/24930024','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/24930024"><span id="translatedtitle">The degree of resistance of erythrocyte membrane cytoskeletal <span class="hlt">proteins</span> to supra-physiologic <span class="hlt">concentrations</span> of calcium: an in vitro study.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Mostafavi, Ebrahim; Nargesi, Arash Aghajani; Ghazizadeh, Zaniar; Larry, Mehrdad; Farahani, Roya Horabad; Morteza, Afsaneh; Esteghamati, Alireza; Vigneron, Claude; Nakhjavani, Manouchehr</p> <p>2014-08-01</p> <p>Calcium is a key regulator of cell dynamics. Dysregulation of its cytosolic <span class="hlt">concentration</span> is implicated in the pathophysiology of several diseases. This study aimed to assess the effects of calcium on the network of membrane cytoskeletal <span class="hlt">proteins</span>. Erythrocyte membranes were obtained from eight healthy donors and incubated with 250 µM and 1.25 mM calcium solutions. Membrane cytoskeletal <span class="hlt">proteins</span> were quantified using SDS-PAGE at baseline and after 3 and 5 days of incubation. Supra-physiologic <span class="hlt">concentrations</span> of calcium (1.25 mM) induced a significant proteolysis in membrane cytoskeletal <span class="hlt">proteins</span>, compared with magnesium (p < 0.001). Actin exhibited the highest sensitivity to calcium-induced proteolysis (6.8 ± 0.3 vs. 5.3 ± 0.6, p < 0.001), while spectrin (39.9 ± 1.0 vs. 40.3 ± 2.0, p = 0.393) and band-6 (6.3 ± 0.3 vs. 6.8 ± 0.8, p = 0.191) were more resistant to proteolysis after incubation with calcium in the range of endoplasmic reticulum <span class="hlt">concentrations</span> (250 µM). Aggregation of membrane cytoskeletal <span class="hlt">proteins</span> was determined after centrifugation and was significantly higher after incubation with calcium ions compared with control, EDTA and magnesium solutions (p < 0.001). In a supra-physiologic range of 1.25-10 mM of calcium ions, there was a nearly perfect linear relationship between calcium <span class="hlt">concentration</span> and aggregation of erythrocyte membrane cytoskeletal <span class="hlt">proteins</span> (R(2) = 0.971, p < 0.001). Our observation suggests a strong interaction between calcium ions and membrane cytoskeletal network. Cumulative effects of disrupted calcium homeostasis on cytoskeletal <span class="hlt">proteins</span> need to be further investigated at extended periods of time in disease states. PMID:24930024</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/19296233','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/19296233"><span id="translatedtitle"><span class="hlt">Protein</span> profile and alpha-lactalbumin <span class="hlt">concentration</span> in the milk of standard and transgenic goats expressing recombinant human butyrylcholinesterase.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Baldassarre, H; Schirm, M; Deslauriers, J; Turcotte, C; Bordignon, V</p> <p>2009-08-01</p> <p>The expression of recombinant <span class="hlt">proteins</span> of pharmaceutical interest in the milk of transgenic farm animals can result in phenotypes exhibiting compromised lactation performance, as a result of the extraordinary demand placed on the mammary gland. In this study, we investigated differences in the <span class="hlt">protein</span> composition of milk from control and transgenic goats expressing recombinant human butyrylcholinesterase. In Experiment 1, the milk was characterized by gel electrophoresis and liquid chromatography/mass spectrometry in order to identify <span class="hlt">protein</span> bands that were uniquely visible in the transgenic milk and/or at differing band densities compared with controls. Differences in <span class="hlt">protein</span> content were additionally evaluated by computer assisted band densitometry. <span class="hlt">Proteins</span> identified in the transgenic milk only included serum <span class="hlt">proteins</span> (i.e. complement component 3b, ceruloplasmin), a cytoskeleton <span class="hlt">protein</span> (i.e. actin) and a stress-induced <span class="hlt">protein</span> (94 kDA glucose-regulated <span class="hlt">protein</span>). <span class="hlt">Proteins</span> exhibiting evident differences in band density between the transgenic and control groups included immunoglobulins, serum albumin, beta-lactoglobulin and alpha-lactalbumin. These results were found to be indicative of compromised epithelial tight junctions, premature mammary cell death, and <span class="hlt">protein</span> synthesis stress resulting from transgene expression. In Experiment 2, the <span class="hlt">concentration</span> of alpha-lactalbumin was determined using the IDRing assay and was found to be significantly reduced on day 1 of lactation in transgenic goats (4.33 +/- 0.97 vs. 2.24 +/- 0.25 mg/ml, P < 0.01), but was not different from non-transgenic controls by day 30 (0.99 +/- 0.46 vs. 0.90 +/- 0.11 mg/ml, P > 0.05). We concluded that a decreased/delayed expression of the alpha-lactalbumin gene may be the cause for the delayed start of milk production observed in this herd of transgenic goats.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/15956470','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/15956470"><span id="translatedtitle">Changes in ruminal fermentation and <span class="hlt">protein</span> degradation in growing Holstein heifers from 80 to 250 kg fed high-<span class="hlt">concentrate</span> diets with different forage-to-<span class="hlt">concentrate</span> ratios.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Rotger, A; Ferret, A; Calsamiglia, S; Manteca, X</p> <p>2005-07-01</p> <p>Six Holstein heifers (initial BW = 65.2 +/- 1.8 kg) fitted with ruminal cannulas were used in a repeated measures trial to assess the effect of age and forage-to-<span class="hlt">concentrate</span> ratio on ruminal fermentation end products and in situ degradation kinetics of four plant <span class="hlt">protein</span> supplements (soybean meal, sunflower meal, peas, and lupin seeds). Alfalfa hay also was incubated in situ to estimate NDF degradation. Three experimental periods were conducted at 13, 27, and 41 wk of age. Heifers were fed one of two diets, 12:88 vs. 30:70 forage-to-<span class="hlt">concentrate</span> ratio (DM basis), offered as total mixed ration on an ad libitum basis. Intakes of DM, OM, CP, NDF, and ADG were not affected (P > or = 0.105) by diet. The 30:70 diet resulted in faster (P = 0.045) fluid passage rate and decreased (P = 0.015) ammonia N <span class="hlt">concentration</span> compared with the 12:88 diet, but no differences (P > or = 0.244) were detected in ruminal pH and total VFA <span class="hlt">concentration</span> between diets. The rate of degradation and the effective degradability of N in <span class="hlt">protein</span> supplements was greater with the 30:70 diet for peas (P < or = 0.008) and lupin seeds (P < or = 0.02), and in the 12:88 diet for sunflower meal (P < or = 0.06). Degradation of NDF of alfalfa hay was low with both diets (18.5 and 23.7 % for 12:88 and 30:70, respectively); however, the rate and extent of DM and NDF degradation were greater (P < or = 0.016) with the 30:70 diet, suggesting a higher cellulolytic activity. Total VFA <span class="hlt">concentration</span> and the proportion of propionate increased (P < or = 0.035), and the acetate proportion decreased (P = 0.021) with age. Average pH, ammonia N <span class="hlt">concentration</span>, and passage rates were not affected (P > or = 0.168) by age. Degradation rate and effective degradability of N of sunflower meal, peas, lupin seeds, and of DM of alfalfa hay increased (P < or = 0.08) with age, but degradation kinetics of NDF of alfalfa hay was not affected (P > or = 0.249). The increase in the rate and extent of N degradation with age would suggest an</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/22459840','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/22459840"><span id="translatedtitle">Effect of dietary <span class="hlt">protein</span> <span class="hlt">concentration</span> on ammonia and greenhouse gas emitting potential of dairy manure.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Lee, C; Hristov, A N; Dell, C J; Feyereisen, G W; Kaye, J; Beegle, D</p> <p>2012-04-01</p> <p>Two experiments were conducted to investigate the effect of dietary crude <span class="hlt">protein</span> <span class="hlt">concentration</span> on ammonia (NH(3)) and greenhouse gas (GHG; nitrous oxide, methane, and carbon dioxide) emissions from fresh dairy cow manure incubated in a controlled environment (experiment 1) and from manure-amended soil (experiment 2). Manure was prepared from feces and urine collected from lactating Holstein cows fed diets with 16.7% (DM basis; HCP) or 14.8% CP (LCP). High-CP manure had higher N content and proportion of NH(3)- and urea-N in total manure N than LCP manure (DM basis: 4.4 vs. 2.8% and 51.4 vs. 30.5%, respectively). In experiment 1, NH(3) emitting potential (EP) was greater for HCP compared with LCP manure (9.20 vs. 4.88 mg/m(2) per min, respectively). The 122-h cumulative NH(3) emission tended to be decreased 47% (P=0.09) using LCP compared with HCP manure. The EP and cumulative emissions of GHG were not different between HCP and LCP manure. In experiment 2, urine and feces from cows fed LCP or HCP diets were mixed and immediately applied to lysimeters (61×61×61 cm; Hagerstown silt loam; fine, mixed, mesic Typic Hapludalf) at 277 kg of N/ha application rate. The average NH(3) EP (1.53 vs. 1.03 mg/m(2) per min, respectively) and the area under the EP curve were greater for lysimeters amended with HCP than with LCP manure. The largest difference in the NH(3) EP occurred approximately 24 h after manure application (approximately 3.5 times greater for HCP than LCP manure). The 100-h cumulative NH(3) emission was 98% greater for HCP compared with LCP manure (7,415 vs. 3,745 mg/m(2), respectively). The EP of methane was increased and that of carbon dioxide tended to be increased by LCP compared with HCP manure. The cumulative methane emission was not different between treatments, whereas the cumulative carbon dioxide emission was increased with manure from the LCP diet. Nitrous oxide emissions were low in this experiment and did not differ between treatments. In the</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/23848445','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/23848445"><span id="translatedtitle">Adsorption of <span class="hlt">proteins</span> at physiological <span class="hlt">concentrations</span> on pegylated surfaces and the compatibilizing role of adsorbed albumin with respect to other <span class="hlt">proteins</span> according to optical waveguide lightmode spectroscopy (OWLS).</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Leclercq, Laurent; Modena, Enrico; Vert, Michel</p> <p>2013-01-01</p> <p>In literature, contacts between pegylated compounds and blood <span class="hlt">proteins</span> are generally discussed in terms of excluded volume-related repulsions although adsorption and compatibility have been reported for some of these <span class="hlt">proteins</span> occasionally. The major problem to investigate the behavior of blood in contact with pegylated surfaces is the complexity of the medium and especially the presence of albumin in large excess. In a model approach, optical waveguide lightmode spectroscopy (OWLS) was used to monitor the fate of albumin, fibrinogen, and γ-globulins at physiological <span class="hlt">concentrations</span> in pH = 7.4 isotonic HEPES buffer after contact with SiTiO2 chips coated with diblock poly(DL-lactic acid)-block-poly(ethylene oxide)s and triblock poly(DL-lactic acid)-block-poly(ethylene oxide)-block-poly(DL-lactic acid) copolymers. Corresponding homopolymers were used as controls. The three <span class="hlt">protein</span> systems were investigated separately, as a mixture and when added successively according to different orders of addition. OWLS gave access to the mass and the thickness of adhering <span class="hlt">protein</span> layers that resist washing with HEPES buffer. <span class="hlt">Protein</span> depositions were detected regardless of the presence of poly(ethylene glycol) segments on surfaces. Adsorption depended on the <span class="hlt">protein</span>, on the surface and also on the presence of the other <span class="hlt">proteins</span>. Unexpectedly any surface coated with a layer of adsorbed albumin prevented deposition of other <span class="hlt">proteins</span>, including albumin itself. This outstanding finding suggests that it was the presence of albumin adsorbed on a surface, pegylated or not, that made that surface compatible with other <span class="hlt">proteins</span>. As a consequence, dipping a device to be in contact with the blood of a patient in a solution of albumin could be a very simple means to avoid further <span class="hlt">protein</span> deposition and maybe platelets adhesion after in vivo implantation.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/23776273','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/23776273"><span id="translatedtitle">Ileal digestibility of amino acids of unheated and autoclaved pea <span class="hlt">protein</span> <span class="hlt">concentrate</span> in broilers.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Frikha, M; Valencia, D G; de Coca-Sinova, A; Lázaro, R; Mateos, G G</p> <p>2013-07-01</p> <p>The effects of autoclaving 2 varieties of micronized (fine grinding) pea <span class="hlt">protein</span> <span class="hlt">concentrate</span> (PPC) on the ileal digestibility (ID) of CP and amino acids (AA) were studied in broilers. There was a control diet based on fermented soybean meal (FSBM) and 4 extra diets in which the FSBM was substituted on a CP basis by PPC from 2 different pea cultivars (PPC-1 and PPC-2), either unheated or autoclaved. Chicks were fed a common diet from 1 to 17 d of age and, then, their respective experimental diets from 18 to 21 d of age. Each treatment was replicated 6 times. Autoclaving reduced trypsin inhibitor activity (TIA) but had little effect on the saponin content of the PPC. The apparent ID (AID) of CP was similar for the FSBM and the unheated PPC and lower for both than for the autoclaved PPC. Autoclaving improved (P < 0.001) the AID of CP (87.6 vs. 82.2%) and most indispensable AA (e.g., 92.1 vs. 88.8% for Lys and 83.6 vs. 76.5% for Thr) of the PPC. The improvement in CP and AA digestibility with autoclaving varied with the PPC used and was consistent with the reduction in TIA observed (9.4 to 2.8 mg/g for PPC-1 vs. 9.1 to 5.3 mg/g for PPC-2). The standardized ID (SID) of most indispensable AA was similar for the FSBM and the PPC-2 and higher for both than for the PPC-1 (P < 0.05). For Lys, the lowest SID value was observed for the FSBM and the highest for the PPC-2 either unheated or autoclaved. It is concluded that the ID of the AA of the PPC improved with heating and was in general higher for the autoclaved PPC than for the FSBM. Consequently, heat processed PPC is a good alternative to FSBM and unheated PPC in starter diets for broilers.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/23776273','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/23776273"><span id="translatedtitle">Ileal digestibility of amino acids of unheated and autoclaved pea <span class="hlt">protein</span> <span class="hlt">concentrate</span> in broilers.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Frikha, M; Valencia, D G; de Coca-Sinova, A; Lázaro, R; Mateos, G G</p> <p>2013-07-01</p> <p>The effects of autoclaving 2 varieties of micronized (fine grinding) pea <span class="hlt">protein</span> <span class="hlt">concentrate</span> (PPC) on the ileal digestibility (ID) of CP and amino acids (AA) were studied in broilers. There was a control diet based on fermented soybean meal (FSBM) and 4 extra diets in which the FSBM was substituted on a CP basis by PPC from 2 different pea cultivars (PPC-1 and PPC-2), either unheated or autoclaved. Chicks were fed a common diet from 1 to 17 d of age and, then, their respective experimental diets from 18 to 21 d of age. Each treatment was replicated 6 times. Autoclaving reduced trypsin inhibitor activity (TIA) but had little effect on the saponin content of the PPC. The apparent ID (AID) of CP was similar for the FSBM and the unheated PPC and lower for both than for the autoclaved PPC. Autoclaving improved (P < 0.001) the AID of CP (87.6 vs. 82.2%) and most indispensable AA (e.g., 92.1 vs. 88.8% for Lys and 83.6 vs. 76.5% for Thr) of the PPC. The improvement in CP and AA digestibility with autoclaving varied with the PPC used and was consistent with the reduction in TIA observed (9.4 to 2.8 mg/g for PPC-1 vs. 9.1 to 5.3 mg/g for PPC-2). The standardized ID (SID) of most indispensable AA was similar for the FSBM and the PPC-2 and higher for both than for the PPC-1 (P < 0.05). For Lys, the lowest SID value was observed for the FSBM and the highest for the PPC-2 either unheated or autoclaved. It is concluded that the ID of the AA of the PPC improved with heating and was in general higher for the autoclaved PPC than for the FSBM. Consequently, heat processed PPC is a good alternative to FSBM and unheated PPC in starter diets for broilers. PMID:23776273</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27459315','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27459315"><span id="translatedtitle">Leaf <span class="hlt">Protein</span> and Mineral <span class="hlt">Concentrations</span> across the "Miracle Tree" Genus Moringa.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Olson, Mark E; Sankaran, Renuka P; Fahey, Jed W; Grusak, Michael A; Odee, David; Nouman, Wasif</p> <p>2016-01-01</p> <p>The moringa tree Moringa oleifera is a fast-growing, drought-resistant tree cultivated across the lowland dry tropics worldwide for its nutritious leaves. Despite its nutritious reputation, there has been no systematic survey of the variation in leaf nutritional quality across M. oleifera grown worldwide, or of the other species of the genus. To guide informed use of moringa, we surveyed <span class="hlt">protein</span>, macro-, and micro- nutrients across 67 common garden samples of 12 Moringa taxa, including 23 samples of M. oleifera. Moringa oleifera, M. concanensis, M. stenopetala, an M. concanensis X oleifera hybrid, and M. longituba were highest in <span class="hlt">protein</span>, with M. ruspoliana having the highest calcium levels. A <span class="hlt">protein</span>-dry leaf mass tradeoff may preclude certain breeding possibilities, e.g. maximally high <span class="hlt">protein</span> with large leaflets. These findings identify clear priorities and limitations for improved moringa varieties with traits such as high <span class="hlt">protein</span>, calcium, or ease of preparation.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27459315','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27459315"><span id="translatedtitle">Leaf <span class="hlt">Protein</span> and Mineral <span class="hlt">Concentrations</span> across the "Miracle Tree" Genus Moringa.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Olson, Mark E; Sankaran, Renuka P; Fahey, Jed W; Grusak, Michael A; Odee, David; Nouman, Wasif</p> <p>2016-01-01</p> <p>The moringa tree Moringa oleifera is a fast-growing, drought-resistant tree cultivated across the lowland dry tropics worldwide for its nutritious leaves. Despite its nutritious reputation, there has been no systematic survey of the variation in leaf nutritional quality across M. oleifera grown worldwide, or of the other species of the genus. To guide informed use of moringa, we surveyed <span class="hlt">protein</span>, macro-, and micro- nutrients across 67 common garden samples of 12 Moringa taxa, including 23 samples of M. oleifera. Moringa oleifera, M. concanensis, M. stenopetala, an M. concanensis X oleifera hybrid, and M. longituba were highest in <span class="hlt">protein</span>, with M. ruspoliana having the highest calcium levels. A <span class="hlt">protein</span>-dry leaf mass tradeoff may preclude certain breeding possibilities, e.g. maximally high <span class="hlt">protein</span> with large leaflets. These findings identify clear priorities and limitations for improved moringa varieties with traits such as high <span class="hlt">protein</span>, calcium, or ease of preparation. PMID:27459315</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_17");'>17</a></li> <li><a href="#" onclick='return showDiv("page_18");'>18</a></li> <li class="active"><span>19</span></li> <li><a href="#" onclick='return showDiv("page_20");'>20</a></li> <li><a href="#" onclick='return showDiv("page_21");'>21</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_19 --> <div id="page_20" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_18");'>18</a></li> <li><a href="#" onclick='return showDiv("page_19");'>19</a></li> <li class="active"><span>20</span></li> <li><a href="#" onclick='return showDiv("page_21");'>21</a></li> <li><a href="#" onclick='return showDiv("page_22");'>22</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="381"> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4961408','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4961408"><span id="translatedtitle">Leaf <span class="hlt">Protein</span> and Mineral <span class="hlt">Concentrations</span> across the “Miracle Tree” Genus Moringa</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Sankaran, Renuka P.; Fahey, Jed W.; Grusak, Michael A.; Odee, David; Nouman, Wasif</p> <p>2016-01-01</p> <p>The moringa tree Moringa oleifera is a fast-growing, drought-resistant tree cultivated across the lowland dry tropics worldwide for its nutritious leaves. Despite its nutritious reputation, there has been no systematic survey of the variation in leaf nutritional quality across M. oleifera grown worldwide, or of the other species of the genus. To guide informed use of moringa, we surveyed <span class="hlt">protein</span>, macro-, and micro- nutrients across 67 common garden samples of 12 Moringa taxa, including 23 samples of M. oleifera. Moringa oleifera, M. concanensis, M. stenopetala, an M. concanensis X oleifera hybrid, and M. longituba were highest in <span class="hlt">protein</span>, with M. ruspoliana having the highest calcium levels. A <span class="hlt">protein</span>-dry leaf mass tradeoff may preclude certain breeding possibilities, e.g. maximally high <span class="hlt">protein</span> with large leaflets. These findings identify clear priorities and limitations for improved moringa varieties with traits such as high <span class="hlt">protein</span>, calcium, or ease of preparation. PMID:27459315</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2006HMR....60....7R','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2006HMR....60....7R"><span id="translatedtitle"><span class="hlt">Protein</span>, carbohydrate, lipid <span class="hlt">concentrations</span> and HSP 70-HSP 90 (stress <span class="hlt">protein</span>) expression over an annual cycle: useful tools to detect feeding constraints in a benthic suspension feeder</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Rossi, Sergio; Snyder, Mark J.; Gili, Josep-Marìa</p> <p>2006-03-01</p> <p>In the present paper we suggest an effect of seasonal variations in food availability on two ecophysiological parameters in a warm temperate benthic suspension feeder: the tissue <span class="hlt">concentrations</span> of <span class="hlt">proteins</span>, carbohydrates and lipids on the one hand, and the expression of stress <span class="hlt">proteins</span> (HSP 70 and 90, inducible and/or constitutive) on the other hand. The <span class="hlt">concentrations</span> of biomacromolecules have already been used to describe bentho-pelagic and reproductive processes, but this is the first time that stress <span class="hlt">protein</span> expression is suggested to be directly related with food constraints in marine organisms. Paramuricea clavata (Cnidaria: Gorgonacea) express HSP 70 and 90 (constitutive and/or inducible) throughout the seasonal cycle, and HSP 70 levels are twice as high as the levels of HSP 90. In summer and autumn, when seston availability to suspension feeders was low, P. clavata showed low levels of carbohydrates and lipids, but high levels of HSPs expression. The levels of HSP 70 and 90 expression fit with negative exponential functions of carbohydrate and lipid <span class="hlt">concentrations</span>. We suggest a direct effect of food availability on the studied ecophysiological parameters while the effect of temperature may be rather indirect. HSP expression as well as the tissue <span class="hlt">concentrations</span> of carbohydrate and lipids may be used as biomarkers of environmental changes and seston availability to benthic suspension feeders.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=2016PhRvA..94a3808D&link_type=ABSTRACT','NASAADS'); return false;" href="http://adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=2016PhRvA..94a3808D&link_type=ABSTRACT"><span id="translatedtitle">Optomechanics for <span class="hlt">absolute</span> rotation detection</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Davuluri, Sankar</p> <p>2016-07-01</p> <p>In this article, we present an application of optomechanical cavity for the <span class="hlt">absolute</span> rotation detection. The optomechanical cavity is arranged in a Michelson interferometer in such a way that the classical centrifugal force due to rotation changes the length of the optomechanical cavity. The change in the cavity length induces a shift in the frequency of the cavity mode. The phase shift corresponding to the frequency shift in the cavity mode is measured at the interferometer output to estimate the angular velocity of <span class="hlt">absolute</span> rotation. We derived an analytic expression to estimate the minimum detectable rotation rate in our scheme for a given optomechanical cavity. Temperature dependence of the rotation detection sensitivity is studied.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/11262641','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/11262641"><span id="translatedtitle">Moral <span class="hlt">absolutism</span> and ectopic pregnancy.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Kaczor, C</p> <p>2001-02-01</p> <p>If one accepts a version of <span class="hlt">absolutism</span> that excludes the intentional killing of any innocent human person from conception to natural death, ectopic pregnancy poses vexing difficulties. Given that the embryonic life almost certainly will die anyway, how can one retain one's moral principle and yet adequately respond to a situation that gravely threatens the life of the mother and her future fertility? The four options of treatment most often discussed in the literature are non-intervention, salpingectomy (removal of tube with embryo), salpingostomy (removal of embryo alone), and use of methotrexate (MXT). In this essay, I review these four options and introduce a fifth (the milking technique). In order to assess these options in terms of the <span class="hlt">absolutism</span> mentioned, it will also be necessary to discuss various accounts of the intention/foresight distinction. I conclude that salpingectomy, salpingostomy, and the milking technique are compatible with absolutist presuppositions, but not the use of methotrexate.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/11262641','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/11262641"><span id="translatedtitle">Moral <span class="hlt">absolutism</span> and ectopic pregnancy.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Kaczor, C</p> <p>2001-02-01</p> <p>If one accepts a version of <span class="hlt">absolutism</span> that excludes the intentional killing of any innocent human person from conception to natural death, ectopic pregnancy poses vexing difficulties. Given that the embryonic life almost certainly will die anyway, how can one retain one's moral principle and yet adequately respond to a situation that gravely threatens the life of the mother and her future fertility? The four options of treatment most often discussed in the literature are non-intervention, salpingectomy (removal of tube with embryo), salpingostomy (removal of embryo alone), and use of methotrexate (MXT). In this essay, I review these four options and introduce a fifth (the milking technique). In order to assess these options in terms of the <span class="hlt">absolutism</span> mentioned, it will also be necessary to discuss various accounts of the intention/foresight distinction. I conclude that salpingectomy, salpingostomy, and the milking technique are compatible with absolutist presuppositions, but not the use of methotrexate. PMID:11262641</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://ntrs.nasa.gov/search.jsp?R=20100014902&hterms=asp&qs=Ntx%3Dmode%2Bmatchall%26Ntk%3DAll%26N%3D0%26No%3D50%26Ntt%3Dasp','NASA-TRS'); return false;" href="http://ntrs.nasa.gov/search.jsp?R=20100014902&hterms=asp&qs=Ntx%3Dmode%2Bmatchall%26Ntk%3DAll%26N%3D0%26No%3D50%26Ntt%3Dasp"><span id="translatedtitle">The <span class="hlt">Absolute</span> Spectrum Polarimeter (ASP)</span></a></p> <p><a target="_blank" href="http://ntrs.nasa.gov/search.jsp">NASA Technical Reports Server (NTRS)</a></p> <p>Kogut, A. J.</p> <p>2010-01-01</p> <p>The <span class="hlt">Absolute</span> Spectrum Polarimeter (ASP) is an Explorer-class mission to map the <span class="hlt">absolute</span> intensity and linear polarization of the cosmic microwave background and diffuse astrophysical foregrounds over the full sky from 30 GHz to 5 THz. The principal science goal is the detection and characterization of linear polarization from an inflationary epoch in the early universe, with tensor-to-scalar ratio r much greater than 1O(raised to the power of { -3}) and Compton distortion y < 10 (raised to the power of{-6}). We describe the ASP instrument and mission architecture needed to detect the signature of an inflationary epoch in the early universe using only 4 semiconductor bolometers.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/15831074','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/15831074"><span id="translatedtitle">Classification images predict <span class="hlt">absolute</span> efficiency.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Murray, Richard F; Bennett, Patrick J; Sekuler, Allison B</p> <p>2005-02-24</p> <p>How well do classification images characterize human observers' strategies in perceptual tasks? We show mathematically that from the classification image of a noisy linear observer, it is possible to recover the observer's <span class="hlt">absolute</span> efficiency. If we could similarly predict human observers' performance from their classification images, this would suggest that the linear model that underlies use of the classification image method is adequate over the small range of stimuli typically encountered in a classification image experiment, and that a classification image captures most important aspects of human observers' performance over this range. In a contrast discrimination task and in a shape discrimination task, we found that observers' <span class="hlt">absolute</span> efficiencies were generally well predicted by their classification images, although consistently slightly (approximately 13%) higher than predicted. We consider whether a number of plausible nonlinearities can account for the slight under prediction, and of these we find that only a form of phase uncertainty can account for the discrepancy.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/servlets/purl/1175308','DOE-PATENT-XML'); return false;" href="http://www.osti.gov/scitech/servlets/purl/1175308"><span id="translatedtitle"><span class="hlt">Absolute</span> calibration of optical flats</span></a></p> <p><a target="_blank" href="http://www.osti.gov/doepatents">DOEpatents</a></p> <p>Sommargren, Gary E.</p> <p>2005-04-05</p> <p>The invention uses the phase shifting diffraction interferometer (PSDI) to provide a true point-by-point measurement of <span class="hlt">absolute</span> flatness over the surface of optical flats. Beams exiting the fiber optics in a PSDI have perfect spherical wavefronts. The measurement beam is reflected from the optical flat and passed through an auxiliary optic to then be combined with the reference beam on a CCD. The combined beams include phase errors due to both the optic under test and the auxiliary optic. Standard phase extraction algorithms are used to calculate this combined phase error. The optical flat is then removed from the system and the measurement fiber is moved to recombine the two beams. The newly combined beams include only the phase errors due to the auxiliary optic. When the second phase measurement is subtracted from the first phase measurement, the <span class="hlt">absolute</span> phase error of the optical flat is obtained.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26633475','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26633475"><span id="translatedtitle">Maternal Low Quality <span class="hlt">Protein</span> Diet Alters Plasma Amino Acid <span class="hlt">Concentrations</span> of Weaning Rats.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Kabasakal Cetin, Arzu; Dasgin, Halil; Gülec, Atila; Onbasilar, İlyas; Akyol, Asli</p> <p>2015-12-01</p> <p>Several studies have indicated the influence of a maternal low <span class="hlt">protein</span> diet on the fetus. However, the effect of a maternal low quality <span class="hlt">protein</span> diet on fetal growth and development is largely unknown. Wistar rats (11 weeks old) were mated and maintained on either a chow diet with 20% casein (n = 6) as the control group (C), or a low quality <span class="hlt">protein</span> diet with 20% wheat gluten (n = 7) as the experimental group (WG) through gestation and lactation. Maternal body weights were similar in both groups throughout the study. Birth weights were not influenced by maternal diet and offspring body weights during lactation were similar between the groups. Offspring's plasma amino acid profiles showed that plasma methionine, glutamine and lysine were significantly lower and aspartic acid, ornithine and glycine-proline were significantly higher in the WG. Plant based <span class="hlt">protein</span> comprises an important part of <span class="hlt">protein</span> intake in developing countries. It is well-known that these diets can be inadequate in terms of essential amino acids. The current study shows differential effects of a maternal low quality <span class="hlt">protein</span> diet on the offspring's plasma amino acids. Future studies will examine further aspects of the influence of maternal low quality <span class="hlt">protein</span> diets on fetal growth and development.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4690060','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4690060"><span id="translatedtitle">Maternal Low Quality <span class="hlt">Protein</span> Diet Alters Plasma Amino Acid <span class="hlt">Concentrations</span> of Weaning Rats</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Kabasakal Cetin, Arzu; Dasgin, Halil; Gülec, Atila; Onbasilar, İlyas; Akyol, Asli</p> <p>2015-01-01</p> <p>Several studies have indicated the influence of a maternal low <span class="hlt">protein</span> diet on the fetus. However, the effect of a maternal low quality <span class="hlt">protein</span> diet on fetal growth and development is largely unknown. Wistar rats (11 weeks old) were mated and maintained on either a chow diet with 20% casein (n = 6) as the control group (C), or a low quality <span class="hlt">protein</span> diet with 20% wheat gluten (n = 7) as the experimental group (WG) through gestation and lactation. Maternal body weights were similar in both groups throughout the study. Birth weights were not influenced by maternal diet and offspring body weights during lactation were similar between the groups. Offspring’s plasma amino acid profiles showed that plasma methionine, glutamine and lysine were significantly lower and aspartic acid, ornithine and glycine-proline were significantly higher in the WG. Plant based <span class="hlt">protein</span> comprises an important part of <span class="hlt">protein</span> intake in developing countries. It is well-known that these diets can be inadequate in terms of essential amino acids. The current study shows differential effects of a maternal low quality <span class="hlt">protein</span> diet on the offspring’s plasma amino acids. Future studies will examine further aspects of the influence of maternal low quality <span class="hlt">protein</span> diets on fetal growth and development. PMID:26633475</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/24560966','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/24560966"><span id="translatedtitle">Rheological characterization and injection forces of <span class="hlt">concentrated</span> <span class="hlt">protein</span> formulations: an alternative predictive model for non-Newtonian solutions.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Allmendinger, Andrea; Fischer, Stefan; Huwyler, Joerg; Mahler, Hanns-Christian; Schwarb, Edward; Zarraga, Isidro E; Mueller, Robert</p> <p>2014-07-01</p> <p>Development of injection devices for subcutaneous drug administration requires a detailed understanding of user capability and forces occurring during the drug administration process. Injection forces of <span class="hlt">concentrated</span> <span class="hlt">protein</span> therapeutics are influenced by syringe properties (e.g., needle diameter) and injection speed, and are driven by solution properties such as rheology. In the present study, it is demonstrated that <span class="hlt">concentrated</span> <span class="hlt">protein</span> therapeutics may show significantly reduced injection forces because of shear-thinning (non-Newtonian) behavior. A mathematical model was thus established to predict/correlate injection forces of Newtonian and non-Newtonian solutions with viscosity data from plate/cone rheometry. The model was verified experimentally by glide-force measurements of reference and surrogate solutions. Application of the suggested model was demonstrated for injection force measurements of <span class="hlt">concentrated</span> <span class="hlt">protein</span> solutions to determine viscosity data at high shear rates (3 × 10(4)-1.6 × 10(5)s(-1)). By combining these data with viscosity data obtained by different viscosity methods (plate/cone and capillary rheometry), a viscosity-shear rate profile of the <span class="hlt">protein</span> solution between 10(2) and 1.6 × 10(5)s(-1) was obtained, which was mathematically described by the Carreau model. Characterization of rheological properties allows to accurately predict injection forces for different syringe-needle combinations as well as injection rates, thus supporting the development of injection devices for combination products.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26621385','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26621385"><span id="translatedtitle">The spider hemolymph clot proteome reveals high <span class="hlt">concentrations</span> of hemocyanin and von Willebrand factor-like <span class="hlt">proteins</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Sanggaard, Kristian W; Dyrlund, Thomas F; Bechsgaard, Jesper S; Scavenius, Carsten; Wang, Tobias; Bilde, Trine; Enghild, Jan J</p> <p>2016-02-01</p> <p>Arthropods include chelicerates, crustaceans, and insects that all have open circulation systems and thus require different properties of their coagulation system than vertebrates. Although the clotting reaction in the chelicerate horseshoe crab (Family: Limulidae) has been described in details, the overall <span class="hlt">protein</span> composition of the resulting clot has not been analyzed for any of the chelicerates. The largest class among the chelicerates is the arachnids, which includes spiders, ticks, mites, and scorpions. Here, we use a mass spectrometry-based approach to characterize the spider hemolymph clot proteome from the Brazilian whiteknee tarantula, Acanthoscurria geniculata. We focused on the insoluble part of the clot and demonstrated high <span class="hlt">concentrations</span> of <span class="hlt">proteins</span> homologous to the hemostasis-related and multimerization-prone von Willebrand factor. These <span class="hlt">proteins</span>, which include hemolectins and vitellogenin homologous, were previously identified as essential components of the hemolymph clot in crustaceans and insects. Their presence in the spider hemolymph clot suggests that the origin of these <span class="hlt">proteins</span>' function in coagulation predates the split between chelicerates and mandibulata. The clot proteome reveals that the major proteinaceous component is the oxygen-transporting and phenoloxidase-displaying abundant hemolymph <span class="hlt">protein</span> hemocyanin, suggesting that this <span class="hlt">protein</span> also plays a role in clot biology. Furthermore, quantification of the peptidome after coagulation revealed the simultaneous activation of both the innate immune system and the coagulation system. In general, many of the identified clot-<span class="hlt">proteins</span> are related to the innate immune system, and our results support the previously suggested crosstalk between immunity and coagulation in arthropods. PMID:26621385</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26621385','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26621385"><span id="translatedtitle">The spider hemolymph clot proteome reveals high <span class="hlt">concentrations</span> of hemocyanin and von Willebrand factor-like <span class="hlt">proteins</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Sanggaard, Kristian W; Dyrlund, Thomas F; Bechsgaard, Jesper S; Scavenius, Carsten; Wang, Tobias; Bilde, Trine; Enghild, Jan J</p> <p>2016-02-01</p> <p>Arthropods include chelicerates, crustaceans, and insects that all have open circulation systems and thus require different properties of their coagulation system than vertebrates. Although the clotting reaction in the chelicerate horseshoe crab (Family: Limulidae) has been described in details, the overall <span class="hlt">protein</span> composition of the resulting clot has not been analyzed for any of the chelicerates. The largest class among the chelicerates is the arachnids, which includes spiders, ticks, mites, and scorpions. Here, we use a mass spectrometry-based approach to characterize the spider hemolymph clot proteome from the Brazilian whiteknee tarantula, Acanthoscurria geniculata. We focused on the insoluble part of the clot and demonstrated high <span class="hlt">concentrations</span> of <span class="hlt">proteins</span> homologous to the hemostasis-related and multimerization-prone von Willebrand factor. These <span class="hlt">proteins</span>, which include hemolectins and vitellogenin homologous, were previously identified as essential components of the hemolymph clot in crustaceans and insects. Their presence in the spider hemolymph clot suggests that the origin of these <span class="hlt">proteins</span>' function in coagulation predates the split between chelicerates and mandibulata. The clot proteome reveals that the major proteinaceous component is the oxygen-transporting and phenoloxidase-displaying abundant hemolymph <span class="hlt">protein</span> hemocyanin, suggesting that this <span class="hlt">protein</span> also plays a role in clot biology. Furthermore, quantification of the peptidome after coagulation revealed the simultaneous activation of both the innate immune system and the coagulation system. In general, many of the identified clot-<span class="hlt">proteins</span> are related to the innate immune system, and our results support the previously suggested crosstalk between immunity and coagulation in arthropods.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=238119','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=238119"><span id="translatedtitle">Association Between Preovulatory <span class="hlt">Concentrations</span> of Estradiol and Expression of Uterine Milk <span class="hlt">Protein</span> Precursor, Inhibin Beta A, Period 1, Proenkephalin, and Receptors for Oxytocin, Progesterone, and Estradiol</span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>Eliminating the preovulatory surge of estradiol decreased uterine weight, uterine <span class="hlt">protein</span>, RNA to DNA ratio, rate of <span class="hlt">protein</span> synthesis, and embryo survival following embryo transfer in sheep. Furthermore, cows that did not exhibit standing estrus (decreased preovulatory <span class="hlt">concentrations</span> of estradiol) ...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/21735287','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/21735287"><span id="translatedtitle">Maternal <span class="hlt">protein</span> and folic acid intake during gestation does not program leptin transcription or serum <span class="hlt">concentration</span> in rat progeny.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Chmurzynska, Agata; Stachowiak, Monika; Pruszynska-Oszmalek, Ewa</p> <p>2012-04-01</p> <p>Maternal nutrition during gestation influences the development of the fetus, thereby determining its phenotype, including nutrient metabolism, appetite, and feeding behavior. The control of appetite is a very complex process and can be modulated by orexigenic and anorexigenic mediators such as leptin, which is involved in the regulation of energy homeostasis by controlling food intake and energy expenditure. Leptin transcription and secretion are regulated by numerous factors, nutrition being one of them. The present study was designed to test whether maternal nutrition can permanently affect leptin gene transcription and leptin serum <span class="hlt">concentration</span> in rat progeny. Moreover, we analyzed whether leptin expression and secretion in response to high-fat postweaning feeding depends on the maternal diet during gestation. Pregnant rats were fed either a normal <span class="hlt">protein</span>, normal folic acid diet (the AIN-93 diet); a <span class="hlt">protein</span>-restricted, normal folic acid diet; a <span class="hlt">protein</span>-restricted, folic acid-supplemented diet; or a normal <span class="hlt">protein</span>, folic acid-supplemented diet. After weaning, the progeny was fed either the AIN-93 diet or a high-fat diet. Neither maternal nutrition nor the postweaning diet significantly affected Lep transcription. High-fat feeding after weaning was associated with higher serum leptin <span class="hlt">concentration</span>, but the reaction of an organism to the fat content of the diet was not determined by maternal nutrition during gestation. There was no correlation between Lep mRNA level and serum leptin <span class="hlt">concentration</span>. Global DNA methylation in adipose tissue was about 30% higher in rats fed postnatally the high-fat diet (P < 0.01). Our study showed that the <span class="hlt">protein</span> and folic acid content in the maternal diet had no significant programming effect on Lep transcription and serum leptin <span class="hlt">concentration</span> in the rats.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27075256','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27075256"><span id="translatedtitle">Rising atmospheric CO2 is reducing the <span class="hlt">protein</span> <span class="hlt">concentration</span> of a floral pollen source essential for North American bees.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Ziska, Lewis H; Pettis, Jeffery S; Edwards, Joan; Hancock, Jillian E; Tomecek, Martha B; Clark, Andrew; Dukes, Jeffrey S; Loladze, Irakli; Polley, H Wayne</p> <p>2016-04-13</p> <p>At present, there is substantive evidence that the nutritional content of agriculturally important food crops will decrease in response to rising levels of atmospheric carbon dioxide, Ca However, whether Ca-induced declines in nutritional quality are also occurring for pollinator food sources is unknown. Flowering late in the season, goldenrod (Solidago spp.) pollen is a widely available autumnal food source commonly acknowledged by apiarists to be essential to native bee (e.g. Bombus spp.) and honeybee (Apis mellifera) health and winter survival. Using floral collections obtained from the Smithsonian Natural History Museum, we quantified Ca-induced temporal changes in pollen <span class="hlt">protein</span> <span class="hlt">concentration</span> of Canada goldenrod (Solidago canadensis), the most wide spread Solidago taxon, from hundreds of samples collected throughout the USA and southern Canada over the period 1842-2014 (i.e. a Ca from approx. 280 to 398 ppm). In addition, we conducted a 2 year in situtrial of S. Canadensis populations grown along a continuous Ca gradient from approximately 280 to 500 ppm. The historical data indicated a strong significant correlation between recent increases in Ca and reductions in pollen <span class="hlt">protein</span> <span class="hlt">concentration</span> (r(2)= 0.81). Experimental data confirmed this decrease in pollen <span class="hlt">protein</span> <span class="hlt">concentration</span>, and indicated that it would be ongoing as Ca continues to rise in the near term, i.e. to 500 ppm (r(2)= 0.88). While additional data are needed to quantify the subsequent effects of reduced <span class="hlt">protein</span> <span class="hlt">concentration</span> for Canada goldenrod on bee health and population stability, these results are the first to indicate that increasing Ca can reduce <span class="hlt">protein</span> content of a floral pollen source widely used by North American bees.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27075256','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27075256"><span id="translatedtitle">Rising atmospheric CO2 is reducing the <span class="hlt">protein</span> <span class="hlt">concentration</span> of a floral pollen source essential for North American bees.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Ziska, Lewis H; Pettis, Jeffery S; Edwards, Joan; Hancock, Jillian E; Tomecek, Martha B; Clark, Andrew; Dukes, Jeffrey S; Loladze, Irakli; Polley, H Wayne</p> <p>2016-04-13</p> <p>At present, there is substantive evidence that the nutritional content of agriculturally important food crops will decrease in response to rising levels of atmospheric carbon dioxide, Ca However, whether Ca-induced declines in nutritional quality are also occurring for pollinator food sources is unknown. Flowering late in the season, goldenrod (Solidago spp.) pollen is a widely available autumnal food source commonly acknowledged by apiarists to be essential to native bee (e.g. Bombus spp.) and honeybee (Apis mellifera) health and winter survival. Using floral collections obtained from the Smithsonian Natural History Museum, we quantified Ca-induced temporal changes in pollen <span class="hlt">protein</span> <span class="hlt">concentration</span> of Canada goldenrod (Solidago canadensis), the most wide spread Solidago taxon, from hundreds of samples collected throughout the USA and southern Canada over the period 1842-2014 (i.e. a Ca from approx. 280 to 398 ppm). In addition, we conducted a 2 year in situtrial of S. Canadensis populations grown along a continuous Ca gradient from approximately 280 to 500 ppm. The historical data indicated a strong significant correlation between recent increases in Ca and reductions in pollen <span class="hlt">protein</span> <span class="hlt">concentration</span> (r(2)= 0.81). Experimental data confirmed this decrease in pollen <span class="hlt">protein</span> <span class="hlt">concentration</span>, and indicated that it would be ongoing as Ca continues to rise in the near term, i.e. to 500 ppm (r(2)= 0.88). While additional data are needed to quantify the subsequent effects of reduced <span class="hlt">protein</span> <span class="hlt">concentration</span> for Canada goldenrod on bee health and population stability, these results are the first to indicate that increasing Ca can reduce <span class="hlt">protein</span> content of a floral pollen source widely used by North American bees. PMID:27075256</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3561907','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3561907"><span id="translatedtitle"><span class="hlt">Concentration</span> dependent requirement for local <span class="hlt">protein</span> synthesis in motor neuron subtype specific response to axon guidance cues</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Nedelec, Stephane; Peljto, Mirza; Shi, Peng; Amoroso, Mackenzie W.; Kam, Lance C.; Wichterle, Hynek</p> <p>2012-01-01</p> <p>Formation of functional motor circuits relies on the ability of distinct spinal motor neuron subtypes to project their axons with high precision to appropriate muscle targets. While guidance cues contributing to motor axon pathfinding have been identified, the intracellular pathways underlying subtype specific responses to these cues remain poorly understood. In particular, it remains controversial whether responses to axon guidance cues depend on axonal <span class="hlt">protein</span> synthesis. Using a growth cone collapse assay, we demonstrate that mouse embryonic stem cell (ESC) derived spinal motor neurons (ES-MNs) respond to ephrin-A5, Sema3f and Sema3a in a <span class="hlt">concentration</span> dependent manner. At low doses, ES-MNs exhibit segmental or subtype specific responses, while this selectivity is lost at higher <span class="hlt">concentrations</span>. Response to high doses of semaphorins and to all doses of ephrin-A5 is <span class="hlt">protein</span> synthesis independent. In contrast, using microfluidic devices and stripe assays, we show that growth cone collapse and guidance at low <span class="hlt">concentrations</span> of semaphorins relies on local <span class="hlt">protein</span> synthesis in the axonal compartment. Similar bimodal response to low and high <span class="hlt">concentrations</span> of guidance cues is observed in human ES-MNs, pointing to a general mechanism by which neurons increase their repertoire of responses to the limited set of guidance cues involved in neural circuit formation. PMID:22279234</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4890585','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4890585"><span id="translatedtitle">RNA-Seq reveals 10 novel promising candidate genes affecting milk <span class="hlt">protein</span> <span class="hlt">concentration</span> in the Chinese Holstein population</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Li, Cong; Cai, Wentao; Zhou, Chenghao; Yin, Hongwei; Zhang, Ziqi; Loor, Juan J.; Sun, Dongxiao; Zhang, Qin; Liu, Jianfeng; Zhang, Shengli</p> <p>2016-01-01</p> <p>Paired-end RNA sequencing (RNA-Seq) was used to explore the bovine transcriptome from the mammary tissue of 12 Chinese Holstein cows with 6 extremely high and 6 low phenotypic values for milk <span class="hlt">protein</span> percentage. We defined the differentially expressed transcripts between the two comparison groups, extremely high and low milk <span class="hlt">protein</span> percentage during the peak lactation (HP vs LP) and during the non-lactating period (HD vs LD), respectively. Within the differentially expressed genes (DEGs), we detected 157 at peak lactation and 497 in the non-lactating period with a highly significant correlation with milk <span class="hlt">protein</span> <span class="hlt">concentration</span>. Integrated interpretation of differential gene expression indicated that SERPINA1, CLU, CNTFR, ERBB2, NEDD4L, ANG, GALE, HSPA8, LPAR6 and CD14 are the most promising candidate genes affecting milk <span class="hlt">protein</span> <span class="hlt">concentration</span>. Similarly, LTF, FCGR3A, MEGF10, RRM2 and UBE2C are the most promising candidates that in the non-lactating period could help the mammary tissue prevent issues with inflammation and udder disorders. Putative genes will be valuable resources for designing better breeding strategies to optimize the content of milk <span class="hlt">protein</span> and also to provide new insights into regulation of lactogenesis. PMID:27254118</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27254118','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27254118"><span id="translatedtitle">RNA-Seq reveals 10 novel promising candidate genes affecting milk <span class="hlt">protein</span> <span class="hlt">concentration</span> in the Chinese Holstein population.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Li, Cong; Cai, Wentao; Zhou, Chenghao; Yin, Hongwei; Zhang, Ziqi; Loor, Juan J; Sun, Dongxiao; Zhang, Qin; Liu, Jianfeng; Zhang, Shengli</p> <p>2016-06-02</p> <p>Paired-end RNA sequencing (RNA-Seq) was used to explore the bovine transcriptome from the mammary tissue of 12 Chinese Holstein cows with 6 extremely high and 6 low phenotypic values for milk <span class="hlt">protein</span> percentage. We defined the differentially expressed transcripts between the two comparison groups, extremely high and low milk <span class="hlt">protein</span> percentage during the peak lactation (HP vs LP) and during the non-lactating period (HD vs LD), respectively. Within the differentially expressed genes (DEGs), we detected 157 at peak lactation and 497 in the non-lactating period with a highly significant correlation with milk <span class="hlt">protein</span> <span class="hlt">concentration</span>. Integrated interpretation of differential gene expression indicated that SERPINA1, CLU, CNTFR, ERBB2, NEDD4L, ANG, GALE, HSPA8, LPAR6 and CD14 are the most promising candidate genes affecting milk <span class="hlt">protein</span> <span class="hlt">concentration</span>. Similarly, LTF, FCGR3A, MEGF10, RRM2 and UBE2C are the most promising candidates that in the non-lactating period could help the mammary tissue prevent issues with inflammation and udder disorders. Putative genes will be valuable resources for designing better breeding strategies to optimize the content of milk <span class="hlt">protein</span> and also to provide new insights into regulation of lactogenesis.</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_18");'>18</a></li> <li><a href="#" onclick='return showDiv("page_19");'>19</a></li> <li class="active"><span>20</span></li> <li><a href="#" onclick='return showDiv("page_21");'>21</a></li> <li><a href="#" onclick='return showDiv("page_22");'>22</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_20 --> <div id="page_21" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_19");'>19</a></li> <li><a href="#" onclick='return showDiv("page_20");'>20</a></li> <li class="active"><span>21</span></li> <li><a href="#" onclick='return showDiv("page_22");'>22</a></li> <li><a href="#" onclick='return showDiv("page_23");'>23</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="401"> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1218021','PMC'); return false;" href="http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1218021"><span id="translatedtitle">Elevated intracellular calcium <span class="hlt">concentration</span> increases secretory processing of the amyloid precursor <span class="hlt">protein</span> by a tyrosine phosphorylation-dependent mechanism.</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Petryniak, M A; Wurtman, R J; Slack, B E</p> <p>1996-01-01</p> <p>Secretory cleavage of the amyloid precursor <span class="hlt">protein</span> (APP), a process that releases soluble APP derivatives (APPs) into the extracellular space, is stimulated by the activation of muscarinic receptors coupled to phosphoinositide hydrolysis. The signalling pathways involved in the release process exhibit both <span class="hlt">protein</span> kinase C- and <span class="hlt">protein</span> tyrosine phosphorylation-dependent components [Slack, Breu, Petryniak, Srivastava and Wurtman (1995) J. Biol. Chem. 270, 8337-8344]. The possibility that elevations in intracellular Ca2+ <span class="hlt">concentration</span> initiate the tyrosine phosphorylation-dependent release of APPs was examined in human embryonic kidney cells expressing muscarinic m3 receptors. Inhibition of <span class="hlt">protein</span> kinase C with the bisindolylmaleimide GF 109203X decreased the carbachol-evoked release of APPs by approx. 30%, as shown previously. The residual response was further decreased, in an additive manner, by the Ca2+ chelator EGTA, or by the tyrosine kinase inhibitor tyrphostin A25. The Ca2+ ionophore, ionomycin, like carbachol, stimulated both the release of APPs and the tyrosine phosphorylation of several <span class="hlt">proteins</span>, one of which was identified as paxillin, a component of focal adhesions. The effects of ionomycin on APPs release and on <span class="hlt">protein</span> tyrosine phosphorylation were <span class="hlt">concentration</span>-dependent, and occurred over similar <span class="hlt">concentration</span> ranges; both effects were inhibited only partly by GF 109203X, but were abolished by EGTA or by tyrosine kinase inhibitors. The results demonstrate for the first time that ionophore-induced elevations in intracellular Ca2+ levels elicit APPs release via increased tyrosine phosphorylation. Part of the increase in APPs release evoked by muscarinic receptor activation might be attributable to a similar mechanism. PMID:9003386</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4342078','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4342078"><span id="translatedtitle">Effects of Storage Time on Total <span class="hlt">Protein</span> and Globulin <span class="hlt">Concentrations</span> in Bovine Fresh Frozen Plasma Obtained for Transfusion</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Proverbio, D.; Spada, E.; Baggiani, L.; Bagnagatti De Giorgi, G.; Roggero, N.; Belloli, A.; Pravettoni, D.; Perego, R.</p> <p>2015-01-01</p> <p>To evaluate the effects of storage conditions on total <span class="hlt">protein</span> (TP) and globulin fractions in fresh frozen bovine plasma units prepared and stored for transfusion, TP and globulin fractions were evaluated in fresh plasma and at 1 month and 6 and 12 months after blood collection in plasma stored at −20°C. Significant differences in <span class="hlt">concentrations</span> were found in the median <span class="hlt">concentration</span> of total <span class="hlt">protein</span> (P = 0.0336), between 0 months and 1 month (P = 0.0108), 0 and 6 months (P = 0.0023), and 0 and 12 months (P = 0.0027), in mean <span class="hlt">concentration</span> (g/dL) of albumin (P = 0.0394), between 0 months and 1 month (P = 0.0131), 0 and 6 months (P = 0.0035), and 0 and 12 months (P = 0.0038), and beta-2 fraction (P = 0.0401), between 0 and 6 months (P = 0.0401) and 0 and 12 months (P = 0.0230). This study suggests that total gamma globulin <span class="hlt">concentration</span> in bovine frozen plasma is stable for 12 months at −20°C. Total <span class="hlt">protein</span>, ALB, and beta-2 fraction have significantly different <span class="hlt">concentrations</span> (g/dL) when compared to prestorage. This study has shown IgG <span class="hlt">protein</span> fraction stability in bovine fresh frozen plasma collected for transfusion; therefore, bovine fresh frozen plasma seems to be suitable for the treatment of hypogammaglobulinemia (failure of passive transfer) in calves when stored for 12 months at −20°C. PMID:25767825</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=273047','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=273047"><span id="translatedtitle">Matrix Gla <span class="hlt">Protein</span> polymorphism, but not <span class="hlt">concentrations</span>, is associated with radiographic hand osteoarthritis</span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>Objective. Factors associated with mineralization and osteophyte formation in osteoarthritis (OA) are incompletely understood. Genetic polymorphisms of matrix Gla <span class="hlt">protein</span> (MGP), a mineralization inhibitor, have been associated clinically with conditions of abnormal calcification. We therefore evalua...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4578863','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4578863"><span id="translatedtitle">Signaling Pathways Related to <span class="hlt">Protein</span> Synthesis and Amino Acid <span class="hlt">Concentration</span> in Pig Skeletal Muscles Depend on the Dietary <span class="hlt">Protein</span> Level, Genotype and Developmental Stages</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Liu, Yingying; Li, Fengna; Kong, Xiangfeng; Tan, Bie; Li, Yinghui; Duan, Yehui; Blachier, François; Hu, Chien-An A.; Yin, Yulong</p> <p>2015-01-01</p> <p>Muscle growth is regulated by the homeostatic balance of the biosynthesis and degradation of muscle <span class="hlt">proteins</span>. To elucidate the molecular interactions among diet, pig genotype, and physiological stage, we examined the effect of dietary <span class="hlt">protein</span> <span class="hlt">concentration</span>, pig genotype, and physiological stages on amino acid (AA) pools, <span class="hlt">protein</span> deposition, and related signaling pathways in different types of skeletal muscles. The study used 48 Landrace pigs and 48 pure-bred Bama mini-pigs assigned to each of 2 dietary treatments: lower/GB (Chinese conventional diet)- or higher/NRC (National Research Council)-<span class="hlt">protein</span> diet. Diets were fed from 5 weeks of age to respective market weights of each genotype. Samples of biceps femoris muscle (BFM, type I) and longissimus dorsi muscle (LDM, type II) were collected at nursery, growing, and finishing phases according to the physiological stage of each genotype, to determine the AA <span class="hlt">concentrations</span>, mRNA levels for growth-related genes in muscles, and <span class="hlt">protein</span> abundances of mechanistic target of rapamycin (mTOR) signaling pathway. Our data showed that the <span class="hlt">concentrations</span> of most AAs in LDM and BFM of pigs increased (P<0.05) gradually with increasing age. Bama mini-pigs had generally higher (P<0.05) muscle <span class="hlt">concentrations</span> of flavor-related AA, including Met, Phe, Tyr, Pro, and Ser, compared with Landrace pigs. The mRNA levels for myogenic determining factor, myogenin, myocyte-specific enhancer binding factor 2 A, and myostatin of Bama mini-pigs were higher (P<0.05) than those of Landrace pigs, while total and phosphorylated <span class="hlt">protein</span> levels for <span class="hlt">protein</span> kinase B, mTOR, and p70 ribosomal <span class="hlt">protein</span> S6 kinases (p70S6K), and ratios of p-mTOR/mTOR, p-AKT/AKT, and p-p70S6K/p70S6K were lower (P<0.05). There was a significant pig genotype-dependent effect of dietary <span class="hlt">protein</span> on the levels for mTOR and p70S6K. When compared with the higher <span class="hlt">protein</span>-NRC diet, the lower <span class="hlt">protein</span>-GB diet increased (P<0.05) the levels for mTOR and p70S6K in Bama mini-pigs, but</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/23201768','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/23201768"><span id="translatedtitle">Effects of egg white <span class="hlt">protein</span> supplementation on muscle strength and serum free amino acid <span class="hlt">concentrations</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Hida, Azumi; Hasegawa, Yuko; Mekata, Yuko; Usuda, Mika; Masuda, Yasunobu; Kawano, Hitoshi; Kawano, Yukari</p> <p>2012-10-01</p> <p>The aim of this study was to evaluate the effects of egg white <span class="hlt">protein</span> compared to carbohydrate intake prior to exercise on fat free mass (FFM), one repetition maximum (1RM) muscle strength and blood biochemistry in female athletes. Thirty healthy female collegiate athletes were recruited for this study and matched by sport type, body fat percentage and 1RM leg curl muscle strength. Participants were randomly divided into two groups: <span class="hlt">protein</span> group (15.0 g egg white <span class="hlt">protein</span>; 75 kcal) and carbohydrate group (17.5 g maltodextrin, 78 kcal). Supplements were administered daily at the same time in a double-blind manner prior to training during an 8-week period. Measurements were performed before and after the 8-week regimen. The mean dietary energy intake did not change throughout the study period. FFM and 1RM assessments (i.e., leg curl, leg extension, squat, and bench press) increased in both groups. Furthermore, serum urea and serum citrulline levels after the 8-week regimen increased significantly only in the <span class="hlt">protein</span> group. Our findings indicated that compared to the carbohydrate supplement, the <span class="hlt">protein</span> supplement was associated with some changes in <span class="hlt">protein</span> metabolites but not with changes in body composition or muscle strength.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4923140','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4923140"><span id="translatedtitle">Variations in <span class="hlt">Protein</span> <span class="hlt">Concentration</span> and Nitrogen Sources in Different Positions of Grain in Wheat</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Li, Xiangnan; Zhou, Longjing; Liu, Fulai; Zhou, Qin; Cai, Jian; Wang, Xiao; Dai, Tingbo; Cao, Weixing; Jiang, Dong</p> <p>2016-01-01</p> <p>The distribution patterns of total <span class="hlt">protein</span> and <span class="hlt">protein</span> components in different layers of wheat grain were investigated using the pearling technique, and the sources of different <span class="hlt">protein</span> components and pearling fractions were identified using 15N isotope tracing methods. It was found that N absorbed from jointing to anthesis (JA) and remobilized to the grain after anthesis was the principal source of grain N, especially in the outer layer. For albumin and globulin, the amount of N absorbed during different stages all showed a decreasing trend from the surface layer to the center part. Whereas, for globulin and glutenin, the N absorbed after anthesis accounted for the main part indicating that for storage <span class="hlt">protein</span>, the utilization of N assimilated after anthesis is greater than that of the stored N assimilated before anthesis. It is concluded that manipulation of the N application rate during different growth stages could be an effective approach to modulate the distribution of <span class="hlt">protein</span> fractions in pearled grains for specific end-uses. PMID:27446169</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2008NW.....95..787E','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2008NW.....95..787E"><span id="translatedtitle">Yellowjackets ( Vespula pensylvanica) thermoregulate in response to changes in <span class="hlt">protein</span> <span class="hlt">concentration</span></span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Eckles, M. A.; Wilson, E. E.; Holway, D. A.; Nieh, J. C.</p> <p>2008-09-01</p> <p>Social insects can modulate body temperature to increase foraging efficiency; however, little is known about how the relative value of <span class="hlt">protein</span> resources affects forager body temperature. Such regulation may be important given that colony growth is often limited by <span class="hlt">protein</span> availability. In this paper, we present what are, to our knowledge, the first data for social insects showing that thoracic temperatures ( T th) of foragers increase with the <span class="hlt">protein</span> content of food resources. In an introduced population of western yellowjacket ( Vespula pensylvanica), we measured T th of foragers collecting high-quality <span class="hlt">protein</span> (100% canned chicken) and low-quality <span class="hlt">protein</span> (50% canned chicken, 50% indigestible alpha-cellulose by volume) at different ambient air temperatures ( T a). Wasps foraging on 100% chicken consistently exhibited higher T th compared to wasps foraging on 50% chicken. After correcting for T a, the mean T th for wasps collecting 100% chicken were 1.98°C higher than those of individuals collecting 50% chicken. We suggest that this mechanism may increase foraging efficiency in this and other social wasp species.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/20629895','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/20629895"><span id="translatedtitle">Sorghum <span class="hlt">proteins</span>: the <span class="hlt">concentration</span>, isolation, modification, and food applications of kafirins.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>de Mesa-Stonestreet, Normell Jhoe; Alavi, Sajid; Bean, Scott R</p> <p>2010-06-01</p> <p>Celiac disease is a serious condition affecting millions of individuals. Those afflicted with this illness are resigned to a lifelong avoidance of products containing the storage prolamin <span class="hlt">proteins</span> found in cereal grains wheat, rye, and barley. Since many food products are based on these cereals, especially wheat, celiac patients have very limited food choices, and those that are available to them are generally poor in quality, often nutritionally deficient, and expensive. Furthermore, this condition also indirectly affects their families and friends with whom they share meals. Thus, a burgeoning need exists to develop nutritious, palatable, and affordable foods, especially staples like bread and pasta, for these individuals and their families and friends who are accustomed to wheat based products. Grain sorghum and its <span class="hlt">proteins</span> are safe for celiac patients and individuals with varying levels of gluten intolerances. However, the main sorghum <span class="hlt">proteins</span>, kafirins, are resistant to digestion. They are also difficult to extract and modify in an industrial-scale process and with food-compatible chemicals, thus limiting their use in foods. This review describes studies on kafirin extraction and methods for modifying sorghum <span class="hlt">proteins</span> for improved nutrition and functionality, as well as food applications. Armed with this knowledge, scientists and technologists will be in a better position to identify opportunities that will further enhance the nutritional and functional value of sorghum <span class="hlt">proteins</span>.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4348753','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=4348753"><span id="translatedtitle">Two Distinct Families of <span class="hlt">Protein</span> Kinases Are Required for Plant Growth under High External Mg2+ <span class="hlt">Concentrations</span> in Arabidopsis1</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Mogami, Junro; Fujita, Yasunari; Yoshida, Takuya; Tsukiori, Yoshifumi; Nakagami, Hirofumi; Nomura, Yuko; Fujiwara, Toru; Nishida, Sho; Yanagisawa, Shuichi; Ishida, Tetsuya; Takahashi, Fuminori; Morimoto, Kyoko; Kidokoro, Satoshi; Mizoi, Junya; Shinozaki, Kazuo</p> <p>2015-01-01</p> <p><span class="hlt">Protein</span> phosphorylation events play key roles in maintaining cellular ion homeostasis in higher plants, and the regulatory roles of these events in Na+ and K+ transport have been studied extensively. However, the regulatory mechanisms governing Mg2+ transport and homeostasis in higher plants remain poorly understood, despite the vital roles of Mg2+ in cellular function. A member of subclass III sucrose nonfermenting-1-related <span class="hlt">protein</span> kinase2 (SnRK2), SRK2D/SnRK2.2, functions as a key positive regulator of abscisic acid (ABA)-mediated signaling in response to water deficit stresses in Arabidopsis (Arabidopsis thaliana). Here, we used immunoprecipitation coupled with liquid chromatography-tandem mass spectrometry analyses to identify Calcineurin B-like-interacting <span class="hlt">protein</span> kinase26 (CIPK26) as a novel <span class="hlt">protein</span> that physically interacts with SRK2D. In addition to CIPK26, three additional CIPKs (CIPK3, CIPK9, and CIPK23) can physically interact with SRK2D in planta. The srk2d/e/i triple mutant lacking all three members of subclass III SnRK2 and the cipk26/3/9/23 quadruple mutant lacking CIPK26, CIPK3, CIPK9, and CIPK23 showed reduced shoot growth under high external Mg2+ <span class="hlt">concentrations</span>. Similarly, several ABA biosynthesis-deficient mutants, including aba2-1, were susceptible to high external Mg2+ <span class="hlt">concentrations</span>. Taken together, our findings provided genetic evidence that SRK2D/E/I and CIPK26/3/9/23 are required for plant growth under high external Mg2+ <span class="hlt">concentrations</span> in Arabidopsis. Furthermore, we showed that ABA, a key molecule in water deficit stress signaling, also serves as a signaling molecule in plant growth under high external Mg2+ <span class="hlt">concentrations</span>. These results suggested that SRK2D/E/I- and CIPK26/3/9/23-mediated phosphorylation signaling pathways maintain cellular Mg2+ homeostasis. PMID:25614064</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1485244','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1485244"><span id="translatedtitle">Human resting extracellular heat shock <span class="hlt">protein</span> 72 <span class="hlt">concentration</span> decreases during the initial adaptation to exercise in a hot, humid environment</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Marshall, Helen C.; Ferguson, Richard A.; Nimmo, Myra A.</p> <p>2006-01-01</p> <p>Heat shock <span class="hlt">protein</span> (Hsp) 72 is a cytosolic <span class="hlt">protein</span> that also is present in the circulation. Extracellular Hsp72 (eHsp72) is inducible by exercise and is suggested to act as a danger signal to the immune system. The adaptive response of eHsp72 to repeated exercise-heat exposures in humans remains to be determined. An intracellular animal study found a reduced Hsp72 response, with no change in resting levels, during heat stress after a single day of passive heat acclimation. The current study therefore tested whether adaptations in human eHsp72 levels would similarly occur 24 hours after a single exercise-heat exposure. Seven males completed cycle exercise (42.5% V̇O2peak for 2 hours) in a hot, humid environment (38°C, 60% relative humidity) on each of 2 consecutive days. Blood samples were obtained from an antecubital vein before exercise and 0 hours and 22 hours postexercise for the analysis of eHsp72. Exercise-heat stress resulted in enhanced eHsp72, with a similar <span class="hlt">absolute</span> increase found on both days (day 1: 1.26 ng/mL [0.80 ng/mL]; day 2: 1.29 ng/mL [1.60 ng/mL]). Resting eHsp72 decreased from rest on day 1 to day 2's 22-hour postexercise sample (P < 0.05). It is suggested that the reduction in resting eHsp72 after 2 consecutive exercise-heat exposures is possibly due to an enhanced removal from the circulation, for either immunoregulatory functions, or for improved cellular stress tolerance in this initial, most stressful period of acclimation. PMID:16817318</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/610239','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/610239"><span id="translatedtitle">[Total <span class="hlt">protein</span> and immunoglobulin <span class="hlt">concentrations</span> in the parotid saliva of pregnant women].</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Donat, H; Tymnik, G; Bernstein, L; Knauthe, H; Kessler, L</p> <p>1977-01-01</p> <p>The content of total <span class="hlt">protein</span> and immunglobulins in the parotid saliva and blood serum of pregnant women and healthy test persons has been determined by the biuret method and radial immunofiffusion. It was stated that total <span class="hlt">protein</span> and IgG in the parotid saliva were higher in pregnant women than in healthy test persons, whereas the IgA-levels don't show any differences. IgM was not measurable in the parotid saliva. There was no relationship between saliva and serum immunglobulins. During the pregnancy show the parotid glands another typ of reaction than nonpregnant women.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://hdl.handle.net/2060/19790013324','NASA-TRS'); return false;" href="http://hdl.handle.net/2060/19790013324"><span id="translatedtitle">The AFGL <span class="hlt">absolute</span> gravity program</span></a></p> <p><a target="_blank" href="http://ntrs.nasa.gov/search.jsp">NASA Technical Reports Server (NTRS)</a></p> <p>Hammond, J. A.; Iliff, R. L.</p> <p>1978-01-01</p> <p>A brief discussion of the AFGL's (Air Force Geophysics Laboratory) program in <span class="hlt">absolute</span> gravity is presented. Support of outside work and in-house studies relating to gravity instrumentation are discussed. A description of the current transportable system is included and the latest results are presented. These results show good agreement with measurements at the AFGL site by an Italian system. The accuracy obtained by the transportable apparatus is better than 0.1 microns sq sec 10 microgal and agreement with previous measurements is within the combined uncertainties of the measurements.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1287535','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1287535"><span id="translatedtitle">Familial Aggregation of <span class="hlt">Absolute</span> Pitch</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Baharloo, Siamak; Service, Susan K.; Risch, Neil; Gitschier, Jane; Freimer, Nelson B.</p> <p>2000-01-01</p> <p><span class="hlt">Absolute</span> pitch (AP) is a behavioral trait that is defined as the ability to identify the pitch of tones in the absence of a reference pitch. AP is an ideal phenotype for investigation of gene and environment interactions in the development of complex human behaviors. Individuals who score exceptionally well on formalized auditory tests of pitch perception are designated as “AP-1.” As described in this report, auditory testing of siblings of AP-1 probands and of a control sample indicates that AP-1 aggregates in families. The implications of this finding for the mapping of loci for AP-1 predisposition are discussed. PMID:10924408</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/18624410','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/18624410"><span id="translatedtitle">Characterization and quantification of grape variety by means of shikimic acid <span class="hlt">concentration</span> and <span class="hlt">protein</span> fingerprint in still white wines.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Chabreyrie, David; Chauvet, Serge; Guyon, François; Salagoïty, Marie-Hélène; Antinelli, Jean-François; Medina, Bernard</p> <p>2008-08-27</p> <p><span class="hlt">Protein</span> profiles, obtained by high-performance capillary electrophoresis (HPCE) on white wines previously dialyzed, combined with shikimic acid <span class="hlt">concentration</span> and multivariate analysis, were used for the determination of grape variety composition of a still white wine. Six varieties were studied through monovarietal wines elaborated in the laboratory: Chardonnay (24 samples), Chenin (24), Petit Manseng (7), Sauvignon (37), Semillon (24), and Ugni Blanc (9). Homemade mixtures were elaborated from authentic monovarietal wines according to a Plackett-Burman sampling plan. After <span class="hlt">protein</span> peak area normalization, a matrix was elaborated containing <span class="hlt">protein</span> results of wines (mixtures and monovarietal). Partial least-squares processing was applied to this matrix allowing the elaboration of a model that provided a varietal quantification precision of around 20% for most of the grape varieties studied. The model was applied to commercial samples from various geographical origins, providing encouraging results for control purposes.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/16699116','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/16699116"><span id="translatedtitle">Manure composition of swine as affected by dietary <span class="hlt">protein</span> and cellulose <span class="hlt">concentrations</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Kerr, B J; Ziemer, C J; Trabue, S L; Crouse, J D; Parkin, T B</p> <p>2006-06-01</p> <p>An experiment was conducted to investigate the effects of reducing dietary CP and increasing dietary cellulose <span class="hlt">concentrations</span> on manure DM, C, N, S, VFA, indole, and phenol <span class="hlt">concentrations</span>. Twenty-two pigs (105 kg initial BW) were fed diets containing either 14.5 or 12.0% CP, in combination with either 2.5 or 8.7% cellulose. Pigs were fed twice daily over the 56-d study, with feed intake averaging 2.74 kg/d. Feces and urine were collected after each feeding and added to the manure storage containers. Manure storage containers were designed to provide a similar unit area per animal as found in industry (7,393 cm2). Before sampling on d 56, the manure was gently stirred to obtain a representative sample for subsequent analyses. An interaction of dietary CP and cellulose was observed for manure acetic acid <span class="hlt">concentration</span>, in that decreasing CP lowered acetic acid in pigs fed standard levels of cellulose but increased acetic acid in pigs fed greater levels of cellulose (P = 0.03). No other interactions were noted. Decreasing dietary CP reduced manure pH (P = 0.01), NH4 (P = 0.01), isovaleric acid (P = 0.06), phenol (P = 0.05), and 4-ethyl phenol (P = 0.02) <span class="hlt">concentrations</span>. Increasing dietary cellulose decreased pH (P = 0.01) and NH4 (P = 0.07) <span class="hlt">concentration</span> but increased manure C (P = 0.03), propionic acid (P = 0.01), butyric acid (P = 0.03), and cresol (P = 0.09) <span class="hlt">concentrations</span> in the manure. Increasing dietary cellulose also increased manure DM (P = 0.11), N (P = 0.11), and C (P = 0.02) contents as a percentage of nutrient intake. Neither cellulose nor CP level of the diet affected manure S composition or output as a percentage of S intake. Headspace N2O <span class="hlt">concentration</span> was increased by decreasing dietary CP (P = 0.03) or by increasing dietary cellulose (P = 0.05). Neither dietary CP nor cellulose affected headspace <span class="hlt">concentration</span> of CH4. This study demonstrates that diets differing in CP and cellulose content can significantly impact manure composition and <span class="hlt">concentrations</span></p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/22944586','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/22944586"><span id="translatedtitle">Effect of CoCl(2) treatment on major and trace elements metabolism and <span class="hlt">protein</span> <span class="hlt">concentration</span> in mice.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Zaksas, Nataliya; Gluhcheva, Yordanka; Sedykh, Sergey; Madzharova, Maria; Atanassova, Nina; Nevinsky, Georgy</p> <p>2013-01-01</p> <p>Cobalt (Co) is a transition metal and an essential trace element, required for vitamin B(12) biosynthesis, enzyme activation and other biological processes, but toxic in high <span class="hlt">concentrations</span>. There is lack of data for the effect of long-term Co(II) treatment on the <span class="hlt">concentrations</span> of other trace elements. We estimate the influence of cobalt chloride (CoCl(2)) on the relative content of different metals in mouse plasma using two-jet arc plasmatron atomic emission and on the total <span class="hlt">protein</span> content. On average, the content of different elements in the plasma of 2-month-old balb/c mice (control group) decreased in the order: Ca>Mg>Si>Fe>Zn>Cu≥Al≥B. The treatment of mice for 60 days with CoCl(2) (daily dose 125 mg/kg) did not appreciably change the relative content of Ca, Cu, and Zn, while a 2.4-fold statistically significant decrease in the content of B and significant increase in the content of Mg (1.4-fold), Al and Fe (2.0-fold) and Si (3.2-fold) was found. A detectable amount of Mo was observed only for two control mice, while the plasma of 9 out of 16 mice of the treated group contained this metal. The administration of Co made its <span class="hlt">concentration</span> detectable in the plasma of all mice of the treated group, but the relative content varied significantly. The treatment led to a 2.2-fold decrease in the <span class="hlt">concentration</span> of the total plasma <span class="hlt">protein</span>. Chronic exposure to CoCl(2) affects homeostasis as well as the <span class="hlt">concentrations</span> and metabolism of other essential elements, probably due to competition of Co ions for similar binding sites within cells, altered signal transduction and <span class="hlt">protein</span> biosynthesis. Long-term treatment also leads to significant weight changes and reduces the total <span class="hlt">protein</span> <span class="hlt">concentration</span>. The data may be useful for an understanding of Co toxicity, its effect on the <span class="hlt">concentration</span> of other metal ions and different physiological processes.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2041878','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2041878"><span id="translatedtitle">Plasma membrane calcium pump activity is affected by the membrane <span class="hlt">protein</span> <span class="hlt">concentration</span>. Evidence for the involvement of the actin cytoskeleton</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Vanagas, Laura; Rossi, Rolando C.; Caride, Ariel J.; Filoteo, Adelaida G.; Strehler, Emanuel E.; Rossi, Juan Pablo F.C.</p> <p>2007-01-01</p> <p>Plasma membrane calcium pumps (PMCAs) are integral membrane <span class="hlt">proteins</span> that actively expel Ca2+ from the cell. Specific Ca2+-ATPase activity of erythrocyte membranes increased steeply up to 1.5–5 times when the membrane <span class="hlt">protein</span> <span class="hlt">concentration</span> decreased from 50 μg/ml to 1 μg/ml. The activation by dilution was also observed for ATP-dependent Ca2+ uptake into vesicles from Sf9 over-expressing the PMCA 4b isoform, confirming that it is a property of the PMCA. Dilution of the <span class="hlt">protein</span> did not modify the activation by ATP, Ca2+ or Ca2+-calmodulin. Treatment with non-ionic detergents did not abolish the dilution effect, suggesting that it was not due to resealing of the membrane vesicles. Pre-incubation of erythrocyte membranes with Cytochalasin D under conditions that promote actin polymerization abolished the dilution effect. Highly-purified, micellar PMCA showed no dilution effect and was not affected by Cytochalasin D. Taken together, these results suggest that the <span class="hlt">concentration</span>-dependent behavior of the PMCA activity was due to interactions with cytoskeletal <span class="hlt">proteins</span>. The dilution effect was also observed with different PMCA isoforms, indicating that this is a general phenomenon for all PMCAs. PMID:17481573</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2014JASMS.tmp..180K','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2014JASMS.tmp..180K"><span id="translatedtitle">Screening Carbohydrate Libraries for <span class="hlt">Protein</span> Interactions Using the Direct ESI-MS Assay. Applications to Libraries of Unknown <span class="hlt">Concentration</span></span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Kitova, Elena N.; El-Hawiet, Amr; Klassen, John S.</p> <p>2014-08-01</p> <p>A semiquantitative electrospray ionization mass spectrometry (ESI-MS) binding assay suitable for analyzing mixtures of oligosaccharides, at unknown <span class="hlt">concentrations</span>, for interactions with target <span class="hlt">proteins</span> is described. The assay relies on the differences in the ratio of the relative abundances of the ligand-bound and free <span class="hlt">protein</span> ions measured by ESI-MS at two or more initial <span class="hlt">protein</span> <span class="hlt">concentrations</span> to distinguish low affinity (≤103 M-1) ligands from moderate and high affinity (>105 M-1) ligands present in the library and to rank their affinities. Control experiments were performed on solutions of a single chain antibody and a mixture of synthetic oligosaccharides, with known affinities, in the absence and presence of a 40-component carbohydrate library to demonstrate the implementation and reliability of the assay. The application of the assay for screening natural libraries of carbohydrates against <span class="hlt">proteins</span> is also demonstrated using mixtures of human milk oligosaccharides, isolated from breast milk, and fragments of a bacterial toxin and human galectin 3.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26585380','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26585380"><span id="translatedtitle">Serum Amyloid A <span class="hlt">Protein</span> <span class="hlt">Concentration</span> in Blood is Influenced by Genetic Differences in the Cheetah (Acinonyx jubatus).</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Franklin, Ashley D; Schmidt-Küntzel, Anne; Terio, Karen A; Marker, Laurie L; Crosier, Adrienne E</p> <p>2016-03-01</p> <p>Systemic amyloid A (AA) amyloidosis is a major cause of morbidity and mortality among captive cheetahs. The self-aggregating AA <span class="hlt">protein</span> responsible for this disease is a byproduct of serum amyloid A (SAA) <span class="hlt">protein</span> degradation. Transcriptional induction of the SAA1 gene is dependent on both C/EBPβ and NF-κB cis-acting elements within the promoter region. In cheetahs, 2 alleles exist for a single guanine nucleotide deletion in the putative NF-κB binding site. In this study, a novel genotyping assay was developed to screen for the alleles. The results show that the SAA1A (-97delG) allele is associated with decreased SAA <span class="hlt">protein</span> <span class="hlt">concentrations</span> in the serum of captive cheetahs (n = 58), suggesting genetic differences at this locus may be affecting AA amyloidosis prevalence. However, there was no significant difference in the frequency of the SAA1A (-97delG) allele between individuals confirmed AA amyloidosis positive versus AA amyloidosis negative at the time of necropsy (n = 48). Thus, even though there is evidence that having more copies of the SAA1A (-97delG) allele results in a potentially protective decrease in serum <span class="hlt">concentrations</span> of SAA <span class="hlt">protein</span> in captive cheetahs, genotype is not associated with this disease within the North American population. These results suggest that other factors are playing a more significant role in the pathogenesis of AA amyloidosis among captive cheetahs.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/27288339','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/27288339"><span id="translatedtitle">Seminal plasma <span class="hlt">protein</span> <span class="hlt">concentrations</span> vary with feed efficiency and fertility-related measures in young beef bulls.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Montanholi, Y R; Fontoura, A B P; Diel de Amorim, M; Foster, R A; Chenier, T; Miller, S P</p> <p>2016-06-01</p> <p>Fertility-associated <span class="hlt">proteins</span> (FAP) found in seminal plasma indicate sexual maturity, which appears to be influenced by feed efficiency in cattle. This study characterized FAP via proteomics and verified associations of these <span class="hlt">proteins</span> with feed efficiency, body composition and fertility-related measures in yearling beef bulls. Assessments including testicular ultrasonography, infrared thermography, seminal quality, seminal plasma proteomics, carcass composition, and reproductive organ biometry were obtained. From a population of 31 bulls, the seven most and least feed efficient (efficient, inefficient) bulls were used for categorical comparisons. Correlations between FAP, productive performance and fertility-related measures were determined. These traits were also correlated with orthogonal factors summarized from the FAP. Efficient bulls had increased epididymal sperm-binding <span class="hlt">protein</span>-1 and decreased <span class="hlt">concentration</span> of <span class="hlt">protein</span>-C inhibitor compared to inefficient bulls. Correlations between FAP with age, body size, body composition, reproductive organ biometry, scrotal temperature, and seminiferous tubule maturity are reported. Acrosin and cathepsin D increased with development of the testes and osteopontin increased with greater numbers of mature seminiferous tubules. Phosphoglycerate kinase-2 was higher in animals with a higher scrotum temperature and a higher prevalence of sperm morphology defects. The principal factor indicated that FAP variability <span class="hlt">concentrations</span> were positively correlated with age, reproductive organ biometry, body size and composition. Our results indicate that FAP changes with body size and sexual development, and demonstrates differences in the proteomics of bulls with diverging feed efficiency. This is related to the delay in the sexual maturity of efficient young bulls.</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_19");'>19</a></li> <li><a href="#" onclick='return showDiv("page_20");'>20</a></li> <li class="active"><span>21</span></li> <li><a href="#" onclick='return showDiv("page_22");'>22</a></li> <li><a href="#" onclick='return showDiv("page_23");'>23</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_21 --> <div id="page_22" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_20");'>20</a></li> <li><a href="#" onclick='return showDiv("page_21");'>21</a></li> <li class="active"><span>22</span></li> <li><a href="#" onclick='return showDiv("page_23");'>23</a></li> <li><a href="#" onclick='return showDiv("page_24");'>24</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="421"> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/27288339','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/27288339"><span id="translatedtitle">Seminal plasma <span class="hlt">protein</span> <span class="hlt">concentrations</span> vary with feed efficiency and fertility-related measures in young beef bulls.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Montanholi, Y R; Fontoura, A B P; Diel de Amorim, M; Foster, R A; Chenier, T; Miller, S P</p> <p>2016-06-01</p> <p>Fertility-associated <span class="hlt">proteins</span> (FAP) found in seminal plasma indicate sexual maturity, which appears to be influenced by feed efficiency in cattle. This study characterized FAP via proteomics and verified associations of these <span class="hlt">proteins</span> with feed efficiency, body composition and fertility-related measures in yearling beef bulls. Assessments including testicular ultrasonography, infrared thermography, seminal quality, seminal plasma proteomics, carcass composition, and reproductive organ biometry were obtained. From a population of 31 bulls, the seven most and least feed efficient (efficient, inefficient) bulls were used for categorical comparisons. Correlations between FAP, productive performance and fertility-related measures were determined. These traits were also correlated with orthogonal factors summarized from the FAP. Efficient bulls had increased epididymal sperm-binding <span class="hlt">protein</span>-1 and decreased <span class="hlt">concentration</span> of <span class="hlt">protein</span>-C inhibitor compared to inefficient bulls. Correlations between FAP with age, body size, body composition, reproductive organ biometry, scrotal temperature, and seminiferous tubule maturity are reported. Acrosin and cathepsin D increased with development of the testes and osteopontin increased with greater numbers of mature seminiferous tubules. Phosphoglycerate kinase-2 was higher in animals with a higher scrotum temperature and a higher prevalence of sperm morphology defects. The principal factor indicated that FAP variability <span class="hlt">concentrations</span> were positively correlated with age, reproductive organ biometry, body size and composition. Our results indicate that FAP changes with body size and sexual development, and demonstrates differences in the proteomics of bulls with diverging feed efficiency. This is related to the delay in the sexual maturity of efficient young bulls. PMID:27288339</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26036686','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26036686"><span id="translatedtitle">Hydrolysis with Cucurbita ficifolia serine protease reduces antigenic response to bovine whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> and αs-casein.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Babij, Konrad; Bajzert, Joanna; Dąbrowska, Anna; Szołtysik, Marek; Zambrowicz, Aleksandra; Lubec, Gert; Stefaniak, Tadeusz; Willak-Janc, Ewa; Chrzanowska, Józefa</p> <p>2015-11-01</p> <p>In the present study the effect of hydrolysis with non-commercial Cucurbita ficifolia serine protease on a reduction of the IgE and IgG binding capacity of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> and αs-casein was investigated. The intensity of the <span class="hlt">protein</span> degradation was analyzed by the degree of hydrolysis, the free amino groups content and RP-HPLC. The ability to bind the antibodies by native <span class="hlt">proteins</span> and their hydrolysates was determined using a competitive ELISA test. Deep hydrolysis contributed to a significant reduction of immunoreactive epitopes present in WPC. In the case of IgE and IgG present in the serum pool of children with CMA, the lowest binding capacity was detected in the 24 h WPC hydrolysate, where the inhibition of the reaction with native WPC was ≤23 and ≤60 %, respectively. The analysis of the IgG reactivity in the antiserum of the immunized goat showed that the lowest antibody binding capacity was exhibited also by 24 h WPC hydrolysate at a <span class="hlt">concentration</span> of 1000 μg/ml where the inhibition of the reaction with nWPC was ≤47 %. One-hour hydrolysis of α-casein was sufficient to significant reduction of the <span class="hlt">protein</span> antigenicity, while the longer time (5 h) of hydrolysis probably lead to the appearance of new epitopes reactive with polyclonal.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26186133','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26186133"><span id="translatedtitle">Effect of prolonged exposure to sublethal <span class="hlt">concentrations</span> of DDT and DDE on <span class="hlt">protein</span> expression in human pancreatic beta cells.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Pavlikova, Nela; Smetana, Pavel; Halada, Petr; Kovar, Jan</p> <p>2015-10-01</p> <p>Pollution of the environment represents one of less explored potential reasons for the worldwide epidemic of type 2 diabetes. One of the most prevalent organochlorine pollutants remains the pesticide DDT and its degradation product DDE. Despite some epidemiologic correlations between levels of DDT and DDE in human organism and the prevalence of diabetes, there is almost no information about the exact targets of these compounds inside pancreatic beta cells. To detect functional areas of pancreatic beta cells that could be affected by exposure to DDT and DDE, we analyzed changes in <span class="hlt">protein</span> expression in the NES2Y human pancreatic beta cell line exposed to three sublethal <span class="hlt">concentrations</span> (0.1 μM, 1 μM, 10 μM) of DDT and DDE for 1 month. <span class="hlt">Protein</span> separation and identification was achieved using high-resolution 2D-electrophoresis, computer analysis and mass spectrometry. With these techniques, four <span class="hlt">proteins</span> were found downregulated after exposure to 10 μM DDT: three cytoskeletal <span class="hlt">proteins</span> (cytokeratin 8, cytokeratin 18 and actin) and one <span class="hlt">protein</span> involved in glycolysis (alpha-enolase). Two <span class="hlt">proteins</span> were downregulated after exposure to 10 μM DDE: cytokeratin 18 and heterogenous nuclear ribonucleoprotein H1 (HNRH1). These changes correlate with previously described effects of other stress conditions (e.g. exposure to palmitate, hyperglycemia, imidazoline derivative, and cytokines) on <span class="hlt">protein</span> expression in pancreatic beta cells. We conclude that cytoskeletal <span class="hlt">proteins</span> and their processing, glucose metabolism, and mRNA processing may represent targets affected by exposure to conditions hostile to pancreatic beta cells, including exposure to DDT and DDE.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/23721750','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/23721750"><span id="translatedtitle">Effect of varying the <span class="hlt">concentrations</span> of carbohydrate and milk <span class="hlt">protein</span> in rehydration solutions ingested after exercise in the heat.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>James, Lewis J; Evans, Gethin H; Madin, Joshua; Scott, Darren; Stepney, Michael; Harris, Russell; Stone, Robert; Clayton, David J</p> <p>2013-10-01</p> <p>The present study investigated the relationship between the milk <span class="hlt">protein</span> content of a rehydration solution and fluid balance after exercise-induced dehydration. On three occasions, eight healthy males were dehydrated to an identical degree of body mass loss (BML, approximately 1·8%) by intermittent cycling in the heat, rehydrating with 150% of their BML over 1 h with either a 60 g/l carbohydrate solution (C), a 40 g/l carbohydrate, 20 g/l milk <span class="hlt">protein</span> solution (CP20) or a 20 g/l carbohydrate, 40 g/l milk <span class="hlt">protein</span> solution (CP40). Urine samples were collected pre-exercise, post-exercise, post-rehydration and for a further 4 h. Subjects produced less urine after ingesting the CP20 or CP40 drink compared with the C drink (P<0·01), and at the end of the study, more of the CP20 (59 (SD 12)%) and CP40 (64 (SD 6)%) drinks had been retained compared with the C drink (46 (SD 9)%) (P<0·01). At the end of the study, whole-body net fluid balance was more negative for trial C (- 470 (SD 154) ml) compared with both trials CP20 (- 181 (SD 280) ml) and CP40 (2107 (SD 126) ml) (P<0·01). At 2 and 3 h after drink ingestion, urine osmolality was greater for trials CP20 and CP40 compared with trial C (P<0·05). The present study further demonstrates that after exercise-induced dehydration, a carbohydrate--milk <span class="hlt">protein</span> solution is better retained than a carbohydrate solution. The results also suggest that high <span class="hlt">concentrations</span> of milk <span class="hlt">protein</span> are not more beneficial in terms of fluid retention than low <span class="hlt">concentrations</span> of milk <span class="hlt">protein</span> following exercise-induced dehydration.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/22062918','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/22062918"><span id="translatedtitle">Effect of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> and sodium chloride <span class="hlt">concentrations</span> on the odour profile of sous vide cooked whole-muscle beef from Argentina.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Grigioni, G; Langman, L; Szerman, N; Irurueta, M; Vaudagna, S R</p> <p>2008-07-01</p> <p>Semitendinosus muscles added with whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) and sodium chloride (NaCl) were submitted to sous vide cooking. Four enhancement treatments and a control were tested: 0.875% WPC (w/w)+0.625% NaCl, 2.625% WPC+0.625% NaCl, 0.875% WPC+1.875% NaCl, 2.625% WPC+1.875% NaCl, and control (non-injected muscles). Odour analyses were carried out with an electronic nose (EN) system. EN data were evaluated applying Principal Component Analysis, Linear Discriminant Analysis and Partial Least Squares algorithm. EN was able to discriminate the odour profiles of cooked enhanced beef as a function of the amount of WPC added. No significant differences in odour profiles were observed regarding NaCl <span class="hlt">concentration</span>. These results agreed with those obtained when odour profiles were analysed in WPC dispersions. The reported results support the applicability of EN methodology for analysing the impact of processing parameters on beef odour profiles. PMID:22062918</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/22062918','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/22062918"><span id="translatedtitle">Effect of whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> and sodium chloride <span class="hlt">concentrations</span> on the odour profile of sous vide cooked whole-muscle beef from Argentina.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Grigioni, G; Langman, L; Szerman, N; Irurueta, M; Vaudagna, S R</p> <p>2008-07-01</p> <p>Semitendinosus muscles added with whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) and sodium chloride (NaCl) were submitted to sous vide cooking. Four enhancement treatments and a control were tested: 0.875% WPC (w/w)+0.625% NaCl, 2.625% WPC+0.625% NaCl, 0.875% WPC+1.875% NaCl, 2.625% WPC+1.875% NaCl, and control (non-injected muscles). Odour analyses were carried out with an electronic nose (EN) system. EN data were evaluated applying Principal Component Analysis, Linear Discriminant Analysis and Partial Least Squares algorithm. EN was able to discriminate the odour profiles of cooked enhanced beef as a function of the amount of WPC added. No significant differences in odour profiles were observed regarding NaCl <span class="hlt">concentration</span>. These results agreed with those obtained when odour profiles were analysed in WPC dispersions. The reported results support the applicability of EN methodology for analysing the impact of processing parameters on beef odour profiles.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.osti.gov/scitech/biblio/1035822','SCIGOV-STC'); return false;" href="http://www.osti.gov/scitech/biblio/1035822"><span id="translatedtitle">The effect of sub-minimum inhibitory <span class="hlt">concentration</span> of ciprofloxacin <span class="hlt">concentrations</span> on enteroaggregative Escherichia coli and the role of the surface <span class="hlt">protein</span> dispersin</span></a></p> <p><a target="_blank" href="http://www.osti.gov/scitech">SciTech Connect</a></p> <p>Mortensen, Ninell P; Fowlkes, Jason Davidson; Trevino-Dopatka, Sonia; Maggart, Michael J; Boisen, Nadia; Doktycz, Mitchel John; Nataro, James; Allison, David P</p> <p>2011-01-01</p> <p>Enteroaggregative Escherichia coli (EAEC) are bacterial pathogens that cause watery diarrhea, which is often persistent and can be inflammatory. The antibiotic ciprofloxacin is used to treat EAEC infections, but a full understanding of the antimicrobial effects of ciprofloxacin is needed for more efficient treatment of bacterial infections. In this study, it was found that sub-minimum inhibitory <span class="hlt">concentrations</span> (sub-MICs) of ciprofloxacin had an inhibitory effect on EAEC adhesion to glass and mammalian HEp-2 cells. It was also observed that bacterial surface properties play an important role in bacterial sensitivity to ciprofloxacin. In an EAEC mutant strain where the hydrophobic positively charged surface <span class="hlt">protein</span> dispersin was absent, sensitivity to ciprofloxacin was reduced compared with the wild-type strain. Identified here are several antimicrobial effects of ciprofloxacin at sub-MIC <span class="hlt">concentrations</span> indicating that bacterial surface hydrophobicity affects the response to ciprofloxacin. Investigating the effects of sub-MIC doses of antibiotics on targeted bacteria could help to further our understanding of bacterial pathogenicity and elucidate future antibiotic treatment modalities.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26617047','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26617047"><span id="translatedtitle">Selective separation and <span class="hlt">concentration</span> of antihypertensive peptides from rapeseed <span class="hlt">protein</span> hydrolysate by electrodialysis with ultrafiltration membranes.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>He, Rong; Girgih, Abraham T; Rozoy, Elodie; Bazinet, Laurent; Ju, Xing-Rong; Aluko, Rotimi E</p> <p>2016-04-15</p> <p>Rapeseed <span class="hlt">protein</span> isolate was subjected to alcalase digestion to obtain a <span class="hlt">protein</span> hydrolysate that was separated into peptide fractions using electrodialysis with ultrafiltration membrane (EDUF) technology. The EDUF process (6h duration) led to isolation of three peptide fractions: anionic (recovered in KCl-1 compartment), cationic (recovered in KCl-2 compartment), and those that remained in the feed compartment, which was labeled final rapeseed <span class="hlt">protein</span> hydrolysate (FRPH). As expected the KCl-1 peptides were enriched in negatively-charged (43.57%) while KCl-2 contained high contents of positively-charged (28.35%) amino acids. All the samples inhibited angiotensin converting enzyme (ACE) and renin activities in dose-dependent manner with original rapeseed <span class="hlt">protein</span> hydrolysate having the least ACE-inhibitory IC50 value of 0.0932±0.0037 mg/mL while FRPH and KCl-2 had least renin-inhibitory IC50 values of 0.47±0.05 and 0.55±0.06 mg/mL, respectively. Six hours after oral administration (100 mg/kg body weight) to spontaneously hypertensive rats, the FRPH produced the maximum systolic blood pressure reduction of -51 mmHg.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=265501','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=265501"><span id="translatedtitle"><span class="hlt">Concentration</span>-dependent displacement of cholesterol in micelles by hydrophobic rice bran <span class="hlt">protein</span> hydrolysates</span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>The recent production of rice bran oil in Asia and the U.S. has resulted in large quantities of defatted rice bran as a low-value byproduct. Peptides from soy, milk, and other foods have been shown to have the potential hypocholesterolemic property and rice bran <span class="hlt">protein</span> (RBP) may also contain bioact...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=249207','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=249207"><span id="translatedtitle">Sorghum <span class="hlt">Proteins</span>: The <span class="hlt">Concentration</span>, Isolation, Modification and Food Applications of Kafirins</span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>Celiac disease is a serious condition affecting millions of individuals. Those afflicted with these illnesses are resigned to a lifelong avoidance of products containing gluten, the storage <span class="hlt">protein</span> found in cereal grains wheat, rye and barley. Since many food products contain gluten, these individ...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/19729195','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/19729195"><span id="translatedtitle">Dynamics of heat shock <span class="hlt">protein</span> 70 <span class="hlt">concentrations</span> in peripheral blood lymphocyte lysates during pregnancy in lactating Holstein-Friesian cows.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Yániz, J L; López-Gatius, F; Almería, S; Carretero, T; García-Ispierto, I; Serrano, B; Smith, R F; Dobson, H; Santolaria, P</p> <p>2009-11-01</p> <p>The aim of this study was to characterize the dynamics of the <span class="hlt">concentrations</span> of heat shock <span class="hlt">protein</span> 70 kDa (HSP70) in peripheral blood lymphocytes of lactating Holstein-Friesian dairy cows (Bos taurus) during pregnancy. The detection of pregnancy was carried out and blood samples collected on Days 40, 90, 120, 150, 180, and 210 of gestation from 46 cows (11 primiparous and 35 pluriparous, 34 seropositive and 12 seronegative to Neospora caninum). Peripheral blood lymphocytes were isolated by density gradient centrifugation. Serologic analysis of Neospora infection and determinations of HSP70 <span class="hlt">concentrations</span> in lymphocyte lysates were carried out using commercial enzyme-linked immunosorbent assay kits. Climate variables were monitored using on-farm data loggers. Heat shock <span class="hlt">protein</span> 70 <span class="hlt">concentrations</span> increased in lymphocytes as gestation progressed, particularly in primiparous cows, with no effect from Neospora infection, climate variables, milk production, semen-providing bull, or outcome of gestation (singletons or twins). Our results show that HSP70 <span class="hlt">concentrations</span> increased in lymphocytes as gestation progressed and were not affected by stressful factors, such as milk production, heat stress, chronic infection (neosporosis), or twin pregnancies.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=372103','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=372103"><span id="translatedtitle">Sex Differences in Long Chain Fatty Acid Utilization and Fatty Acid Binding <span class="hlt">Protein</span> <span class="hlt">Concentration</span> in Rat Liver</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Ockner, Robert K.; Burnett, David A.; Lysenko, Nina; Manning, Joan A.</p> <p>1979-01-01</p> <p>Female sex and estrogen administration are associated with increased hepatic production of triglyceride-rich lipoproteins; the basis for this has not been fully elucidated. Inasmuch as hepatic lipoprotein production is also influenced by FFA availability and triglyceride biosynthesis, we investigated sex differences in FFA utilization in rat hepatocyte suspensions and in the components of the triglyceride biosynthetic pathway. Isolated adult rat hepatocyte suspensions were incubated with albumin-bound [14C]oleate for up to 15 min. At physiological and low oleate <span class="hlt">concentrations</span>, cells from females incorporated significantly more 14C into glycerolipids, especially triglycerides, and into oxidation products than did male cells, per milligram cell <span class="hlt">protein</span>. At 0.44 mM oleate, incorporation into triglycerides in female cells was approximately twice that in male cells. Comparable sex differences were observed in cells from fasted animals and when [14C]-glycerol incorporation was measured. At higher oleate <span class="hlt">concentrations</span>, i.e., fatty acid:albumin mole ratios in excess of 2:1, these sex differences were no longer demonstrable, suggesting that maximal rates of fatty acid esterification and oxidation were similar in female and male cells. In female and male hepatic microsomes, specific activities of long chain acyl coenzyme A synthetase, phosphatidate phosphohydrolase, and diglyceride acyltransferase were similar, but glycerol-3-phosphate acyltransferase activity was slightly greater in females at certain substrate <span class="hlt">concentrations</span>. Microsomal incorporation of [14C]oleate into total glycerolipids was not significantly greater in females. In further contrast to intact cells, microsomal incorporation of [14C]oleate into triglycerides, although significantly greater in female microsomes, accounted for only a small fraction of the fatty acid esterified. The binding affinity and stoichiometry of partially purified female hepatic fatty acid binding <span class="hlt">protein</span> (FABP) were similar to</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://hdl.handle.net/2060/20000000444','NASA-TRS'); return false;" href="http://hdl.handle.net/2060/20000000444"><span id="translatedtitle">Micron Accurate <span class="hlt">Absolute</span> Ranging System: Range Extension</span></a></p> <p><a target="_blank" href="http://ntrs.nasa.gov/search.jsp">NASA Technical Reports Server (NTRS)</a></p> <p>Smalley, Larry L.; Smith, Kely L.</p> <p>1999-01-01</p> <p>The purpose of this research is to investigate Fresnel diffraction as a means of obtaining <span class="hlt">absolute</span> distance measurements with micron or greater accuracy. It is believed that such a system would prove useful to the Next Generation Space Telescope (NGST) as a non-intrusive, non-contact measuring system for use with secondary <span class="hlt">concentrator</span> station-keeping systems. The present research attempts to validate past experiments and develop ways to apply the phenomena of Fresnel diffraction to micron accurate measurement. This report discusses past research on the phenomena, and the basis of the use Fresnel diffraction distance metrology. The apparatus used in the recent investigations, experimental procedures used, preliminary results are discussed in detail. Continued research and equipment requirements on the extension of the effective range of the Fresnel diffraction systems is also described.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ars.usda.gov/research/publications/publication/?seqNo115=293700','TEKTRAN'); return false;" href="http://www.ars.usda.gov/research/publications/publication/?seqNo115=293700"><span id="translatedtitle">Rising atmospheric CO2 lowers food zinc, iron, and <span class="hlt">protein</span> <span class="hlt">concentrations</span></span></a></p> <p><a target="_blank" href="http://www.ars.usda.gov/services/TekTran.htm">Technology Transfer Automated Retrieval System (TEKTRAN)</a></p> <p></p> <p></p> <p>Dietary deficiencies of zinc and iron are a major global public health problem. Most people who experience these deficiencies depend on agricultural crops for zinc and iron. In this context, the influence of rising <span class="hlt">concentrations</span> of atmospheric CO2 on the availability of these nutrients from crops i...</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26996967','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26996967"><span id="translatedtitle">Time course of hepatic gene expression and plasma vitellogenin <span class="hlt">protein</span> <span class="hlt">concentrations</span> in estrone-exposed juvenile rainbow trout (Oncorhynchus mykiss).</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Osachoff, Heather L; Brown, Lorraine L Y; Tirrul, Leena; van Aggelen, Graham C; Brinkman, Fiona S L; Kennedy, Christopher J</p> <p>2016-09-01</p> <p>Estrone (E1), a natural estrogen hormone found in sewage effluents and surface waters, has known endocrine disrupting effects in fish, thus, it is a contaminant of emerging concern. Juvenile rainbow trout (Oncorhynchus mykiss) were exposed to an environmentally-relevant <span class="hlt">concentration</span> of E1 (24ng/L E1 [0.1nM]) for 7d and then placed in clean water for a 9d recovery period. RNA sequencing showed transcripts from numerous affected biological processes (e.g. immune, metabolic, apoptosis, clotting, and endocrine) were altered by E1 after 4d of treatment. The time course of E1-inducible responses relating to vitellogenesis was examined daily during the two phases of exposure. Hepatic gene expression alterations evaluated by quantitative polymerase chain reaction (QPCR) were found during the treatment period for vitellogenin (VTG), vitelline envelope <span class="hlt">proteins</span> (VEPs) α, β and γ, and estrogen receptor α1 (ERα1) transcripts. ERα1 was the only transcript induced each day during the treatment phase, thus it was a good indicator of E1 exposure. Gradual increases occurred in VEPβ and VEPγ transcripts, peaking at d7. VTG transcript was only elevated at d4, making it less sensitive than VEPs to this low-level E1 treatment. Inductions of ERα1, VEPα, VEPβ and VEPγ transcripts ceased 1d into the recovery phase. Plasma VTG <span class="hlt">protein</span> <span class="hlt">concentrations</span> were not immediately elevated but peaked 7d into the recovery phase. Thus, elevated vitellogenesis-related gene expression and <span class="hlt">protein</span> production occurred slowly but steadily at this <span class="hlt">concentration</span> of E1, confirming the sequence of events for transcripts and VTG <span class="hlt">protein</span> responses to xenoestrogen exposure.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26996967','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26996967"><span id="translatedtitle">Time course of hepatic gene expression and plasma vitellogenin <span class="hlt">protein</span> <span class="hlt">concentrations</span> in estrone-exposed juvenile rainbow trout (Oncorhynchus mykiss).</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Osachoff, Heather L; Brown, Lorraine L Y; Tirrul, Leena; van Aggelen, Graham C; Brinkman, Fiona S L; Kennedy, Christopher J</p> <p>2016-09-01</p> <p>Estrone (E1), a natural estrogen hormone found in sewage effluents and surface waters, has known endocrine disrupting effects in fish, thus, it is a contaminant of emerging concern. Juvenile rainbow trout (Oncorhynchus mykiss) were exposed to an environmentally-relevant <span class="hlt">concentration</span> of E1 (24ng/L E1 [0.1nM]) for 7d and then placed in clean water for a 9d recovery period. RNA sequencing showed transcripts from numerous affected biological processes (e.g. immune, metabolic, apoptosis, clotting, and endocrine) were altered by E1 after 4d of treatment. The time course of E1-inducible responses relating to vitellogenesis was examined daily during the two phases of exposure. Hepatic gene expression alterations evaluated by quantitative polymerase chain reaction (QPCR) were found during the treatment period for vitellogenin (VTG), vitelline envelope <span class="hlt">proteins</span> (VEPs) α, β and γ, and estrogen receptor α1 (ERα1) transcripts. ERα1 was the only transcript induced each day during the treatment phase, thus it was a good indicator of E1 exposure. Gradual increases occurred in VEPβ and VEPγ transcripts, peaking at d7. VTG transcript was only elevated at d4, making it less sensitive than VEPs to this low-level E1 treatment. Inductions of ERα1, VEPα, VEPβ and VEPγ transcripts ceased 1d into the recovery phase. Plasma VTG <span class="hlt">protein</span> <span class="hlt">concentrations</span> were not immediately elevated but peaked 7d into the recovery phase. Thus, elevated vitellogenesis-related gene expression and <span class="hlt">protein</span> production occurred slowly but steadily at this <span class="hlt">concentration</span> of E1, confirming the sequence of events for transcripts and VTG <span class="hlt">protein</span> responses to xenoestrogen exposure. PMID:26996967</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26869116','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26869116"><span id="translatedtitle">Modulating the textural characteristics of whey <span class="hlt">protein</span> nanofibril gels with different <span class="hlt">concentrations</span> of calcium chloride.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Farjami, Toktam; Madadlou, Ashkan; Labbafi, Mohsen</p> <p>2016-02-01</p> <p><span class="hlt">Protein</span> nanofibrils with 10-20 nm diameters were formed by heating whey <span class="hlt">protein</span> solution at pH 2.0. Nanofibrils solution was deacidified slowly through dialysis followed by adding different amounts of CaCl2 (0-80 mM) into the dialysis water resulting in formation of a soft viscoelastic gel over time. The gel fabricated from the nanofibrils solution dialyzed against distilled water with 0 mM CaCl2 had zero ash content. Fourier transform infra-red spectroscopy revealed a change in the pattern of hydrogen bond formation in gel network by calcium chloride. The higher the ash content of gels, the lower was the storage modulus and fracture stress of samples. Gels with higher ash contents had a more porous microstructure which was attributed to the diminished hydrophobic interactions and hydrogen bonding among nanofibrils by the action of chloride. Higher ash contents also led to higher water holding capacity of gels which was attributed to the influence of the strongly hydrated calcium ions that interacted with the non-charged regions of <span class="hlt">proteins</span> via site-specific interactions.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25306874','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25306874"><span id="translatedtitle">Wheat germ cell-free expression: Two detergents with a low critical micelle <span class="hlt">concentration</span> allow for production of soluble HCV membrane <span class="hlt">proteins</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Fogeron, Marie-Laure; Badillo, Aurélie; Jirasko, Vlastimil; Gouttenoire, Jérôme; Paul, David; Lancien, Loick; Moradpour, Darius; Bartenschlager, Ralf; Meier, Beat H; Penin, François; Böckmann, Anja</p> <p>2015-01-01</p> <p>Membrane <span class="hlt">proteins</span> are notoriously difficult to express in a soluble form. Here, we use wheat germ cell-free expression in the presence of various detergents to produce the non-structural membrane <span class="hlt">proteins</span> 2, 4B and 5A of the hepatitis C virus (HCV). We show that lauryl maltose neopentyl glycol (MNG-3) and dodecyl octaethylene glycol ether (C12E8) detergents can yield essentially soluble membrane <span class="hlt">proteins</span> at detergent <span class="hlt">concentrations</span> that do not inhibit the cell-free reaction. This finding can be explained by the low critical micelle <span class="hlt">concentration</span> (CMC) of these detergents, which keeps the monomer <span class="hlt">concentrations</span> low while at the same time providing the necessary excess of detergent <span class="hlt">concentration</span> above CMC required for full target <span class="hlt">protein</span> solubilization. We estimate that a tenfold excess of detergent micelles with respect to the <span class="hlt">protein</span> <span class="hlt">concentration</span> is sufficient for solubilization, a number that we propose as a guideline for detergent screening assays.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/11434780','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/11434780"><span id="translatedtitle">Ion <span class="hlt">concentration</span> and temperature dependence of DNA binding: comparison of PurR and LacI repressor <span class="hlt">proteins</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Moraitis, M I; Xu, H; Matthews, K S</p> <p>2001-07-10</p> <p>Purine repressor (PurR) binding to specific DNA is enhanced by complexing with purines, whereas lactose repressor (LacI) binding is diminished by interaction with inducer sugars despite 30% identity in their <span class="hlt">protein</span> sequences and highly homologous tertiary structures. Nonetheless, in switching from low- to high-affinity DNA binding, these <span class="hlt">proteins</span> undergo a similar structural change in which the hinge region connecting the DNA and effector binding domains folds into an alpha-helix and contacts the DNA minor groove. The differences in response to effector for these <span class="hlt">proteins</span> should be manifest in the polyelectrolyte effect which arises from cations displaced from DNA by interaction with positively charged side chains on a <span class="hlt">protein</span> and is quantitated by measurement of DNA binding affinity as a function of ion <span class="hlt">concentration</span>. Consistent with structural data for these <span class="hlt">proteins</span>, high-affinity operator DNA binding by the PurR-purine complex involved approximately 15 ion pairs, a value significantly greater than that for the corresponding state of LacI (approximately 6 ion pairs). For both <span class="hlt">proteins</span>, however, conversion to the low-affinity state results in a decrease of approximately 2-fold in the number of cations released per dimeric DNA binding site. Heat capacity changes (DeltaC(p)) that accompany DNA binding, derived from buried apolar surface area, coupled folding, and restriction of motional freedom of polar groups in the interface, also reflect the differences between these homologous repressor <span class="hlt">proteins</span>. DNA binding of the PurR-guanine complex is accompanied by a DeltaC(p) (-2.8 kcal mol(-1) K(-1)) more negative than that observed previously for LacI (-0.9 to -1.5 kcal mol(-1) K(-1)), suggesting that more extensive <span class="hlt">protein</span> folding and/or enhanced structural rigidity may occur upon DNA binding for PurR compared to DNA binding for LacI. The differences between these <span class="hlt">proteins</span> illustrate plasticity of function despite high-level sequence and structural homology and</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26944977','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26944977"><span id="translatedtitle">Interactive effects of dietary <span class="hlt">protein</span> <span class="hlt">concentration</span> and aflatoxin B1 on performance, nutrient digestibility, and gut health in broiler chicks.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Chen, X; Naehrer, K; Applegate, T J</p> <p>2016-06-01</p> <p>A 20-day trial was conducted to determine the impact of aflatoxin B1 (AFB1) and dietary <span class="hlt">protein</span> <span class="hlt">concentration</span> on performance, nutrient digestibility, and gut health in broiler chicks. The 6 dietary treatments were arranged in a 2 × 3 factorial with 3 crude <span class="hlt">protein</span> (CP) <span class="hlt">concentrations</span> (16, 22, and 26%) with or without 1.5 mg/kg AFB1 Each diet was fed to 6 replicate cages (6 chicks per cage) from zero to 20 d of age. Endogenous N and amino acid loss were estimated from birds fed a N-free diet with or without 1.5 mg/kg AFB1 A significant interaction between AFB1 and CP <span class="hlt">concentration</span> was observed for growth performance, where reduction of BW gain, feed intake, gain:feed ratio, and breast muscle weight by AFB1 were most profound in birds fed the 16%-CP diet, and were completely eliminated when birds were fed the 26%-CP diet (AFB1 by CP interaction; P ≤ 0.023). Similarly, AFB1 reduced serum albumin, total <span class="hlt">protein</span>, and globulin <span class="hlt">concentrations</span> in birds fed 16 and 22% CP diets, but not in those fed the 26%-CP (AFB1 by CP interaction; P ≤ 0.071). Gut permeability was increased in birds fed AFB1-contamiated diets as measured by serum lactulose/rhamnose ratio (main effect; P = 0.04). Additionally, AFB1 tended to increase endogenous N loss (P = 0.09), and significantly reduced apparent ileal digestible energy and standardized ileal N and amino acid digestibility in birds fed the 16%-CP diet, while birds fed higher dietary CP were not affected (AFB1 by CP interaction; P ≤ 0.01). Further, AFB1 increased the translation initiation factor 4E-binding <span class="hlt">protein</span> (4EBP1), claudin1, and multiple jejunal amino acid transporters expression (main effect; P ≤ 0.04). Results from this study indicate that a 1.5 mg AFB1/kg diet significantly impairs growth, major serum biochemistry measures, gut barrier, endogenous loss, and energy and amino acid digestibility. Aflatoxicosis can be augmented by low dietary CP, while higher dietary CP completely eliminated the impairment of</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_20");'>20</a></li> <li><a href="#" onclick='return showDiv("page_21");'>21</a></li> <li class="active"><span>22</span></li> <li><a href="#" onclick='return showDiv("page_23");'>23</a></li> <li><a href="#" onclick='return showDiv("page_24");'>24</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_22 --> <div id="page_23" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_21");'>21</a></li> <li><a href="#" onclick='return showDiv("page_22");'>22</a></li> <li class="active"><span>23</span></li> <li><a href="#" onclick='return showDiv("page_24");'>24</a></li> <li><a href="#" onclick='return showDiv("page_25");'>25</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="441"> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/20678663','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/20678663"><span id="translatedtitle">Kinetics independent spectrometric analysis using non-linear calibration modelling and exploitation of <span class="hlt">concentration</span> gradients generated by a flow-batch system for albumin and total <span class="hlt">protein</span> determination in blood serum.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Souza, Margarida C; Martins, Valdomiro L; Almeida, Luciano F; Pessoa Neto, Osmundo D; Gaião, Edvaldo N; Araujo, Mario Cesar U</p> <p>2010-08-15</p> <p>An automatic method for kinetics independent spectrometric analysis is proposed in this study. It uses a non-linear calibration model that explores <span class="hlt">concentration</span> gradients generated by a flow-batch analyser (FBA) for the samples, dye, and the single standard solution. The procedure for obtaining the gradients of the dye and standard solution is performed once at the beginning of analysis. The same procedure is applied thereafter for each sample. For illustration, the proposed automatic methodology was applied to determine total <span class="hlt">protein</span> and albumin in blood serum by using the Biuret and Bromocresol Green (BCG) methods. The measurements were made by using a laboratory-made photometer based on a red and green bicolour LED (Light-Emitting Diode) and a phototransistor, coupled to a "Z" form flow cell. The sample throughput was about 50 h(-1) for albumin and 60 h(-1) for total <span class="hlt">protein</span>, consuming about 7 microL of sample, 2.6 mL of BCG and 1.2 mL of biuret reagents for each determination. Applying the paired t-test for results from the proposed analyser and the reference method, no statistic differences at 95% confidence level were found. The <span class="hlt">absolute</span> standard deviation was usually smaller than 0.2 g dL(-1). The proposed method is valuable for the determination of total <span class="hlt">protein</span> and albumin; and can also be used in other determinations where kinetic effects may or may not exist. PMID:20678663</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/20678663','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/20678663"><span id="translatedtitle">Kinetics independent spectrometric analysis using non-linear calibration modelling and exploitation of <span class="hlt">concentration</span> gradients generated by a flow-batch system for albumin and total <span class="hlt">protein</span> determination in blood serum.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Souza, Margarida C; Martins, Valdomiro L; Almeida, Luciano F; Pessoa Neto, Osmundo D; Gaião, Edvaldo N; Araujo, Mario Cesar U</p> <p>2010-08-15</p> <p>An automatic method for kinetics independent spectrometric analysis is proposed in this study. It uses a non-linear calibration model that explores <span class="hlt">concentration</span> gradients generated by a flow-batch analyser (FBA) for the samples, dye, and the single standard solution. The procedure for obtaining the gradients of the dye and standard solution is performed once at the beginning of analysis. The same procedure is applied thereafter for each sample. For illustration, the proposed automatic methodology was applied to determine total <span class="hlt">protein</span> and albumin in blood serum by using the Biuret and Bromocresol Green (BCG) methods. The measurements were made by using a laboratory-made photometer based on a red and green bicolour LED (Light-Emitting Diode) and a phototransistor, coupled to a "Z" form flow cell. The sample throughput was about 50 h(-1) for albumin and 60 h(-1) for total <span class="hlt">protein</span>, consuming about 7 microL of sample, 2.6 mL of BCG and 1.2 mL of biuret reagents for each determination. Applying the paired t-test for results from the proposed analyser and the reference method, no statistic differences at 95% confidence level were found. The <span class="hlt">absolute</span> standard deviation was usually smaller than 0.2 g dL(-1). The proposed method is valuable for the determination of total <span class="hlt">protein</span> and albumin; and can also be used in other determinations where kinetic effects may or may not exist.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/23477815','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/23477815"><span id="translatedtitle">In situ <span class="hlt">protein</span> degradation of alfalfa and birdsfoot trefoil hays and silages as influenced by condensed tannin <span class="hlt">concentration</span>.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Coblentz, W K; Grabber, J H</p> <p>2013-05-01</p> <p>Dairy cattle often make poor use of <span class="hlt">protein</span> when offered diets comprising high proportions of alfalfa (Medicago sativa L.) hay or silage because nonprotein N formed during forage conservation and ruminal fermentation exceeds requirements for rumen microbial <span class="hlt">protein</span> synthesis; however, condensed tannins (CT) may reduce proteolysis in the silo and in the rumen, thereby potentially improving the efficiency of crude <span class="hlt">protein</span> (CP) use in ruminant diets. Two harvests, yielding 12 hays and 12 silages made from alfalfa and birdsfoot trefoil (Lotus corniculatus L.) that varied in <span class="hlt">concentrations</span> of CT, were evaluated for in situ disappearance kinetics of CP in 6 ruminally cannulated lactating Holstein dairy cows (627 ± 56.3 kg). Prior to conservation, alfalfa contained no detectable CT, whereas CT in fresh lyophilized birdsfoot trefoil ranged from 1.16 to 2.77% of dry matter, as determined by a modified acetone-butanol-HCl assay. Percentages of CP remaining at each incubation time were fitted to nonlinear regression models with or without a discrete lag time. Effective ruminal disappearance of CP (rumen-degradable <span class="hlt">protein</span>, RDP) was calculated by 3 procedures that included (1) no discrete lag (RDPNL), (2) discrete lag (RDPL), and (3) discrete lag with a lag adjustment (RDPLADJ). Regardless of the calculation method, RDP declined linearly with increasing CT <span class="hlt">concentrations</span> (R(2)=0.62 to 0.97). Generally, tests of homogeneity showed that conservation type (hay or silage) or harvest (silage only) affected intercepts, but not slopes in regressions of RDP on CT. A positive relationship between lag time and CT suggests that the RDPLADJ approach may be most appropriate for calculating RDP for legumes containing tannins. With this approach, regression intercepts were mainly affected by conservation method, and RDPLADJ averaged 77.5 and 88.7% of CP for hay and silage, respectively, when no CT was present. Greater estimates of RDP for silages were related to extensive proteolysis in</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/8763990','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/8763990"><span id="translatedtitle">The <span class="hlt">concentration</span> of Ca2+ that solubilizes outer capsid <span class="hlt">proteins</span> from rotavirus particles is dependent on the strain.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Ruiz, M C; Charpilienne, A; Liprandi, F; Gajardo, R; Michelangeli, F; Cohen, J</p> <p>1996-08-01</p> <p>It has been previously shown that rotavirus maturation and stability of the outer capsid are calcium-dependent processes. More recently, it has been hypothesized that penetration of the cell membrane is also affected by conformational changes of the capsid induced by Ca2+. In this study, we determined quantitatively the critical <span class="hlt">concentration</span> of calcium ion that leads to solubilization of the outer capsid <span class="hlt">proteins</span> VP4 and VP7. Since this critical <span class="hlt">concentration</span> is below or close to trace levels of Ca2+, we have used buffered solutions based on ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) and Ca-EGTA. This method allowed us to show a very high variability of the free [Ca2+] needed to stabilize, at room temperature, the outer capsid of several rotavirus strains. This <span class="hlt">concentration</span> is about 600 nM for the two bovine strains tested (RF and UK), 100 nM for the porcine strain OSU, and only 10 to 20 nM for the simian strain SA11. Titration of viral infectivity after incubation in buffer of defined [Ca2+] confirmed that the loss of infectivity occurs at different [Ca2+] for these three strains. For the bovine strain, the cleavage of VP4 by trypsin has no significant effect on the [Ca2+] that solubilizes outer shell <span class="hlt">proteins</span>. The outer layer (VP7) of virus-like particles (VLP) made of recombinant <span class="hlt">proteins</span> VP2, VP6, and VP7 (VLP2/6/7) was also solubilized by lowering the [Ca2+]. The critical <span class="hlt">concentration</span> of Ca2+ needed to solubilize VP7 from VLP2/6/7 made of <span class="hlt">protein</span> from the bovine strain is close to the <span class="hlt">concentration</span> needed for the corresponding virus. Genetic analysis of this phenotype in a set of reassortant viruses from two parental strains having the phenotypes of strains OSU (porcine) and UK (bovine) confirmed that this property of viral particles is probably associated with the gene coding for VP7. The analysis of VLP by reverse genetics might allow the identification of the region(s) essential for calcium binding.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=190437','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=190437"><span id="translatedtitle">The <span class="hlt">concentration</span> of Ca2+ that solubilizes outer capsid <span class="hlt">proteins</span> from rotavirus particles is dependent on the strain.</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Ruiz, M C; Charpilienne, A; Liprandi, F; Gajardo, R; Michelangeli, F; Cohen, J</p> <p>1996-01-01</p> <p>It has been previously shown that rotavirus maturation and stability of the outer capsid are calcium-dependent processes. More recently, it has been hypothesized that penetration of the cell membrane is also affected by conformational changes of the capsid induced by Ca2+. In this study, we determined quantitatively the critical <span class="hlt">concentration</span> of calcium ion that leads to solubilization of the outer capsid <span class="hlt">proteins</span> VP4 and VP7. Since this critical <span class="hlt">concentration</span> is below or close to trace levels of Ca2+, we have used buffered solutions based on ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) and Ca-EGTA. This method allowed us to show a very high variability of the free [Ca2+] needed to stabilize, at room temperature, the outer capsid of several rotavirus strains. This <span class="hlt">concentration</span> is about 600 nM for the two bovine strains tested (RF and UK), 100 nM for the porcine strain OSU, and only 10 to 20 nM for the simian strain SA11. Titration of viral infectivity after incubation in buffer of defined [Ca2+] confirmed that the loss of infectivity occurs at different [Ca2+] for these three strains. For the bovine strain, the cleavage of VP4 by trypsin has no significant effect on the [Ca2+] that solubilizes outer shell <span class="hlt">proteins</span>. The outer layer (VP7) of virus-like particles (VLP) made of recombinant <span class="hlt">proteins</span> VP2, VP6, and VP7 (VLP2/6/7) was also solubilized by lowering the [Ca2+]. The critical <span class="hlt">concentration</span> of Ca2+ needed to solubilize VP7 from VLP2/6/7 made of <span class="hlt">protein</span> from the bovine strain is close to the <span class="hlt">concentration</span> needed for the corresponding virus. Genetic analysis of this phenotype in a set of reassortant viruses from two parental strains having the phenotypes of strains OSU (porcine) and UK (bovine) confirmed that this property of viral particles is probably associated with the gene coding for VP7. The analysis of VLP by reverse genetics might allow the identification of the region(s) essential for calcium binding. PMID:8763990</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=2016JCAP...08..060V&link_type=ABSTRACT','NASAADS'); return false;" href="http://adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=2016JCAP...08..060V&link_type=ABSTRACT"><span id="translatedtitle">Cosmology with negative <span class="hlt">absolute</span> temperatures</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Vieira, J. P. P.; Byrnes, Christian T.; Lewis, Antony</p> <p>2016-08-01</p> <p>Negative <span class="hlt">absolute</span> temperatures (NAT) are an exotic thermodynamical consequence of quantum physics which has been known since the 1950's (having been achieved in the lab on a number of occasions). Recently, the work of Braun et al. [1] has rekindled interest in negative temperatures and hinted at a possibility of using NAT systems in the lab as dark energy analogues. This paper goes one step further, looking into the cosmological consequences of the existence of a NAT component in the Universe. NAT-dominated expanding Universes experience a borderline phantom expansion (w < ‑1) with no Big Rip, and their contracting counterparts are forced to bounce after the energy density becomes sufficiently large. Both scenarios might be used to solve horizon and flatness problems analogously to standard inflation and bouncing cosmologies. We discuss the difficulties in obtaining and ending a NAT-dominated epoch, and possible ways of obtaining density perturbations with an acceptable spectrum.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://hdl.handle.net/2060/19730021662','NASA-TRS'); return false;" href="http://hdl.handle.net/2060/19730021662"><span id="translatedtitle">Apparatus for <span class="hlt">absolute</span> pressure measurement</span></a></p> <p><a target="_blank" href="http://ntrs.nasa.gov/search.jsp">NASA Technical Reports Server (NTRS)</a></p> <p>Hecht, R. (Inventor)</p> <p>1969-01-01</p> <p>An <span class="hlt">absolute</span> pressure sensor (e.g., the diaphragm of a capacitance manometer) was subjected to a superimposed potential to effectively reduce the mechanical stiffness of the sensor. This substantially increases the sensitivity of the sensor and is particularly useful in vacuum gauges. An oscillating component of the superimposed potential induced vibrations of the sensor. The phase of these vibrations with respect to that of the oscillating component was monitored, and served to initiate an automatic adjustment of the static component of the superimposed potential, so as to bring the sensor into resonance at the frequency of the oscillating component. This establishes a selected sensitivity for the sensor, since a definite relationship exists between resonant frequency and sensitivity.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://adsabs.harvard.edu/abs/2016JCAP...08..060V','NASAADS'); return false;" href="http://adsabs.harvard.edu/abs/2016JCAP...08..060V"><span id="translatedtitle">Cosmology with negative <span class="hlt">absolute</span> temperatures</span></a></p> <p><a target="_blank" href="http://adsabs.harvard.edu/abstract_service.html">NASA Astrophysics Data System (ADS)</a></p> <p>Vieira, J. P. P.; Byrnes, Christian T.; Lewis, Antony</p> <p>2016-08-01</p> <p>Negative <span class="hlt">absolute</span> temperatures (NAT) are an exotic thermodynamical consequence of quantum physics which has been known since the 1950's (having been achieved in the lab on a number of occasions). Recently, the work of Braun et al. [1] has rekindled interest in negative temperatures and hinted at a possibility of using NAT systems in the lab as dark energy analogues. This paper goes one step further, looking into the cosmological consequences of the existence of a NAT component in the Universe. NAT-dominated expanding Universes experience a borderline phantom expansion (w < -1) with no Big Rip, and their contracting counterparts are forced to bounce after the energy density becomes sufficiently large. Both scenarios might be used to solve horizon and flatness problems analogously to standard inflation and bouncing cosmologies. We discuss the difficulties in obtaining and ending a NAT-dominated epoch, and possible ways of obtaining density perturbations with an acceptable spectrum.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/24792804','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/24792804"><span id="translatedtitle">The effect of acidification of liquid whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> on the flavor of spray-dried powder.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Park, Curtis W; Bastian, Eric; Farkas, Brian; Drake, MaryAnne</p> <p>2014-07-01</p> <p>Off-flavors in whey <span class="hlt">protein</span> negatively influence consumer acceptance of whey <span class="hlt">protein</span> ingredient applications. Clear acidic beverages are a common application of whey <span class="hlt">protein</span>, and recent studies have demonstrated that beverage processing steps, including acidification, enhance off-flavor production from whey <span class="hlt">protein</span>. The objective of this study was to determine the effect of preacidification of liquid ultrafiltered whey <span class="hlt">protein</span> <span class="hlt">concentrate</span> (WPC) before spray drying on flavor of dried WPC. Two experiments were performed to achieve the objective. In both experiments, Cheddar cheese whey was manufactured, fat-separated, pasteurized, bleached (250 mg/kg of hydrogen peroxide), and ultrafiltered (UF) to obtain liquid WPC that was 13% solids (wt/wt) and 80% <span class="hlt">protein</span> on a solids basis. In experiment 1, the liquid retentate was then acidified using a blend of phosphoric and citric acids to the following pH values: no acidification (control; pH 6.5), pH 5.5, or pH 3.5. The UF permeate was used to normalize the <span class="hlt">protein</span> <span class="hlt">concentration</span> of each treatment. The retentates were then spray dried. In experiment 2, 150 μg/kg of deuterated hexanal (D₁₂-hexanal) was added to each treatment, followed by acidification and spray drying. Both experiments were replicated 3 times. Flavor properties of the spray-dried WPC were evaluated by sensory and instrumental analyses in experiment 1 and by instrumental analysis in experiment 2. Preacidification to pH 3.5 resulted in decreased cardboard flavor and aroma intensities and an increase in soapy flavor, with decreased <span class="hlt">concentrations</span> of hexanal, heptanal, nonanal, decanal, dimethyl disulfide, and dimethyl trisulfide compared with spray drying at pH 6.5 or 5.5. Adjustment to pH 5.5 before spray drying increased cabbage flavor and increased <span class="hlt">concentrations</span> of nonanal at evaluation pH values of 3.5 and 5.5 and dimethyl trisulfide at all evaluation pH values. In general, the flavor effects of preacidification were consistent regardless of the pH to</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2902130','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2902130"><span id="translatedtitle">Duffy antigen receptor for chemokines (Darc) polymorphism regulates circulating <span class="hlt">concentrations</span> of monocyte chemoattractant <span class="hlt">protein</span>-1 and other inflammatory mediators</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Schnabel, Renate B.; Baumert, Jens; Barbalic, Maja; Dupuis, Josée; Ellinor, Patrick T.; Durda, Peter; Dehghan, Abbas; Bis, Joshua C.; Illig, Thomas; Morrison, Alanna C.; Jenny, Nancy S.; Keaney, John F.; Gieger, Christian; Tilley, Cathy; Yamamoto, Jennifer F.; Khuseyinova, Natalie; Heiss, Gerardo; Doyle, Margaret; Blankenberg, Stefan; Herder, Christian; Walston, Jeremy D.; Zhu, Yanyan; Vasan, Ramachandran S.; Klopp, Norman; Boerwinkle, Eric; Larson, Martin G.; Psaty, Bruce M.; Peters, Annette; Ballantyne, Christie M.; Witteman, Jacqueline C. M.</p> <p>2010-01-01</p> <p>To identify the genetic basis of circulating <span class="hlt">concentrations</span> of monocyte chemoattractant <span class="hlt">protein</span>-1 (MCP-1), we conducted genome-wide association analyses for MCP-1 in 3 independent cohorts (n = 9598). The strongest association was for serum MCP-1 with a nonsynonymous polymorphism, rs12075 (Asp42Gly) in DARC, the gene for Duffy antigen receptor for chemokines, a known vascular reservoir of proinflammatory cytokines (minor allele frequency, 45.6%; P < 1.0 * 10−323). This association was supported by family-based genetic linkage at a locus encompassing the DARC gene (genome-wide P = 8.0 * 10−13). Asp42Gly accounted for approximately 20% of the variability in serum MCP-1 <span class="hlt">concentrations</span> and also was associated with serum <span class="hlt">concentrations</span> of interleukin-8 and RANTES. While exploring a lack of association between this polymorphism and EDTA plasma MCP-1 <span class="hlt">concentrations</span> (P = .82), we determined that both clotting and exogenous heparan sulfate (unfractionated heparin) released substantial amounts of MCP-1 from Darc. Quantitative immunoflow cytometry failed to identify meaningful Asp42Gly-associated differences in Darc expression, suggesting that a functional change is responsible for the differential cytokine binding. We conclude that Asp42Gly is a major regulator of erythrocyte Darc-mediated cytokine binding and thereby the circulating <span class="hlt">concentrations</span> of several proinflammatory cytokines. We have also identified for the first time 2 mechanisms for the release of reservoir chemokines with possible clinical implications. PMID:20040767</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2229123','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2229123"><span id="translatedtitle">Cytosolic <span class="hlt">protein</span> <span class="hlt">concentration</span> is the primary volume signal for swelling-induced [K-Cl] cotransport in dog red cells</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p></p> <p>1992-01-01</p> <p>Chloride-dependent K transport ([K-Cl] cotransport) in dog red cells is activated by cell swelling. Whether the volume signal is generated by a change in cell configuration or by the dilution of some cytosolic constituent is not known. To differentiate between these two alternatives we prepared resealed ghosts that, compared with intact red cells, had the same surface area and similar hemoglobin <span class="hlt">concentration</span>, but a greatly diminished volume. Swelling-induced [K-Cl] cotransport was activated in the ghosts at a volume (20 fl) well below the activation volume for intact cells (70 fl), but at a similar hemoglobin <span class="hlt">concentration</span> (30-35 g dry solids per 100 g wet weight). Ghosts made to contain 40% albumin and 60% hemoglobin showed activation of [K-Cl] cotransport at a <span class="hlt">concentration</span> of cell solids similar to intact cells or ghosts containing only hemoglobin. [K-Cl] cotransport in the resealed ghosts became quiescent at a dry solid <span class="hlt">concentration</span> close to that at which shrinkage-induced Na/H exchange became activated. These results support the notion that the primary volume sensor in dog red cells is cytosolic <span class="hlt">protein</span> <span class="hlt">concentration</span>. We speculate that macromolecular crowding is the mechanism by which cells initiate responses to volume perturbation. PMID:1512553</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/12112780','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/12112780"><span id="translatedtitle">Increased interleukin-8 and monocyte chemoattractant <span class="hlt">protein</span>-1 <span class="hlt">concentrations</span> in mechanically ventilated preterm infants with pulmonary hemorrhage.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Baier, R John; Loggins, John; Kruger, Thomas E</p> <p>2002-08-01</p> <p>Pulmonary hemorrhage (PH) is a serious complication causing acute respiratory distress in the premature infant, and it is associated with significant mortality and morbidity. The role of inflammatory mediators in this condition is largely undefined. Serial tracheal aspirates (TA) were obtained at intervals from 65 mechanically ventilated infants with birth weights less than 1,250 g during the first 21 days of life. Clinically significant PH developed in 15 infants. TA <span class="hlt">concentrations</span> of interleukin-8 (IL-8) and monocyte chemoattractant <span class="hlt">protein</span>-1 (MCP-1) were determined by enzyme-linked immunosorbent assay (ELISA).PH was associated with an increased risk of death, bronchopulmonary dysplasia, intraventricular hemorrhage, and prolonged need for mechanical ventilation and supplemental oxygen. TA aspirate <span class="hlt">concentrations</span> of IL-8 and MCP-1 (P = 0.001, ANOVA) were significantly increased in infants with PH compared to infants who did not develop this condition. TA cytokine <span class="hlt">concentrations</span> were also significantly increased in infants who developed bronchopulmonary dysplasia (BPD). Peak TA <span class="hlt">concentrations</span> of IL-8 and MCP-1 were significantly higher in infants with poor outcome (BPD or death). TA MCP-1 but not IL-8 <span class="hlt">concentrations</span> were significantly higher in infants who were oxygen-dependent at 36 weeks postconceptional age. These data suggest a pathogenic role for IL-8 and MCP-1 in the development of adverse pulmonary outcome in preterm infants with clinically significant PH.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25213434','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25213434"><span id="translatedtitle">Effects of milk <span class="hlt">proteins</span> on sperm binding to the zona pellucida and intracellular Ca(2+) <span class="hlt">concentration</span> in stallion sperm.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Coutinho da Silva, Marco A; Seidel, George E; Squires, Edward L; Graham, James K; Carnevale, Elaine M</p> <p>2014-11-10</p> <p>Objectives were to determine the effects of extracellular Ca(2+) and milk <span class="hlt">proteins</span> on intracellular Ca(2+) <span class="hlt">concentrations</span> in stallion sperm; and to determine the effects of single caseins on sperm binding to the zona pellucida (ZP). In Experiment I, sperm were incubated in media containing 2 or 4mM Ca(2+) and intracellular Ca(2+) <span class="hlt">concentration</span> was determined after ionomycin treatment and long-term incubation (3h). Extracellular Ca(2+) <span class="hlt">concentrations</span> (2 compared with 4mM) did not affect baseline intracellular Ca(2+) <span class="hlt">concentration</span> of sperm. However, incubating sperm in a medium containing 4 compared with 2mM Ca(2+) resulted in greater (P<0.05) influx of Ca(2+) into sperm. In Experiment II, sperm incubated in media containing 1mg/mL of native phosphocaseinate (NP) or sodium caseinate (SC) showed similar baseline intracellular Ca(2+) and influx of Ca(2+) than control (TALP). In Experiment III, sperm-ZP binding assays were performed in TALP medium containing: no additions (TALP); 1mg/mL SC; 1 or 3mg/mL of α-casein; 1 or 3mg/mL of β-casein; and 1 or 3mg/mL of κ-casein. The number of stallion sperm bound to bovine ZP was greatest (P<0.05) when SC was used. Co-incubation in media containing single caseins (α-, β- or κ-casein) resulted in similar results to TALP; however, a dose effect (P<0.05) was observed for β- and κ-caseins. In conclusion, extracellular Ca(2+) <span class="hlt">concentration</span> and milk <span class="hlt">proteins</span> did not affect baseline intracellular calcium in stallion sperm. It appears that β- and κ-caseins may be responsible for enhancing sperm binding to ZP, but the mechanism remains unknown.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/10701869','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/10701869"><span id="translatedtitle"><span class="hlt">Concentrated</span> expression of Ca2+/ calmodulin-dependent <span class="hlt">protein</span> kinase II and <span class="hlt">protein</span> kinase C in the mushroom bodies of the brain of the honeybee Apis mellifera L.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Kamikouchi, A; Takeuchi, H; Sawata, M; Natori, S; Kubo, T</p> <p>2000-02-21</p> <p>We have previously used the differential display method to identify a gene that is expressed preferentially in the mushroom bodies of worker honeybees and to show that it encodes a putative inositol 1,4,5-trisphosphate receptor (IP3R) homologue (Kamikouchi et al. [1998] Biochem. Biophys. Res. Commun. 242:181-186). In the present study, we examined whether the expression of some of the genes for <span class="hlt">proteins</span> involved in the intracellular Ca2+ signal transduction is also <span class="hlt">concentrated</span> in the mushroom bodies of the honeybee by isolating cDNA fragments that encode the Ca2+/calmodulin-dependent <span class="hlt">protein</span> kinase II (CaMKII) and <span class="hlt">protein</span> kinase C (PKC) homologues of the honeybee. In situ hybridization analysis revealed that the expression of these genes was also <span class="hlt">concentrated</span> in the mushroom bodies of the honeybee brain: The CaMKII gene was expressed preferentially in the large-type Kenyon cells of the mushroom bodies, whereas that for PKC was expressed in both the large and small types of Kenyon cells. The expression of the genes for IP3R and CaMKII was <span class="hlt">concentrated</span> in the mushroom bodies of the queen and drone as well as in those of the worker bee. Furthermore, the enzymatic activities of CaMKII and PKC were found to be higher in the mushroom bodies/central bodies than in the optic and antennal lobes of the worker bee brain. These results suggest that the function of the intracellular Ca2+ signal transduction is enhanced in Kenyon cells in comparison to other neuronal cell types in the honeybee brain.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/25162628','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/25162628"><span id="translatedtitle">Effect of different <span class="hlt">concentrations</span> of metabolisable energy and <span class="hlt">protein</span> on performance of White Leghorn layers in a tropical climate.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Rama Rao, S V; Ravindran, V; Raju, M V L N; Srilatha, T; Panda, A K</p> <p>2014-01-01</p> <p>1. An experiment was conducted to study the effects of feeding graded <span class="hlt">concentrations</span> of metabolisable energy (ME) and crude <span class="hlt">protein</span> (CP) on the performance of layers. Nine diets with three <span class="hlt">concentrations</span> each of ME (10.04, 10.67 and 11.30 MJ/kg) and CP (150, 165 and 180 g/kg) in a 3 × 3 factorial arrangement of treatments were formulated. 2. A total of 5544 White Leghorn (WL) pullets (20 weeks of age) were housed in 4-bird colony cages and 22 adjacent cages constituted a replicate. Each diet was fed ad libitum to 7 replicates from 21 to 72 weeks of age. Production variables were recorded in 13 laying periods of 28 d each, and the data were pooled into three production phases, namely initial (21-32 weeks), peak (33-52 weeks) and post-peak (53-72 weeks). 3. No interaction was observed between ME and CP for egg production (EP), food intake (FI), food efficiency (FE), egg weight (EW), egg mass (EM) and body weight gain. 4. The EP, EW and EM during the initial phase of production were not affected by dietary ME <span class="hlt">concentrations</span>, while the EW and EM improved with increasing <span class="hlt">concentrations</span> of dietary CP from 150 to 165 g/kg. 5. During the peak production phase, improvements in EP (ME and CP), FI (ME), FE (ME, CP), EW (ME) and EM (ME, CP) were observed with increasing <span class="hlt">concentrations</span> of energy and <span class="hlt">protein</span> to 11.30 and 180 g/kg diet, respectively. 6. EP, EW and EM were unaffected by dietary variation in <span class="hlt">concentrations</span> of ME and CP during post-peak production phase, but the FE improved and FI reduced with increasing dietary <span class="hlt">concentrations</span> of these nutrients. 7. It is concluded that the optimum <span class="hlt">concentrations</span> of ME for WL layers during the 21-32, 33-52 and 53-72 weeks of age are 11.30, 11.30 and 10.04 MJ/kg diet, respectively. The corresponding values for CP in diets are 180, 180 and 150 g/kg.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/26377938','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/26377938"><span id="translatedtitle">Nutritional evaluation of phosphorylated pumpkin seed (Cucurbita moschata) <span class="hlt">protein</span> <span class="hlt">concentrate</span> in silver catfish Rhamdia quelen (Quoy and Gaimard, 1824).</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Lovatto, Naglezi de Menezes; Goulart, Fernanda Rodrigues; de Freitas, Silvandro Tonetto; Mombach, Patricia Inês; Loureiro, Bruno Bianch; Bender, Ana Betine Beutinger; Boligon, Aline Augusti; Radünz Neto, João; da Silva, Leila Picolli</p> <p>2015-12-01</p> <p>An 8-week feeding trial was conducted to evaluate the effect of replacing fish meal with pumpkin seed meal (PSM) or phosphorylated <span class="hlt">protein</span> <span class="hlt">concentrate</span> of pumpkin seed meal (PPCPS) on growth and metabolic responses of silver catfish. Five isonitrogenous and isocaloric diets were formulated. Control diet contained fish meal as the main <span class="hlt">protein</span> source. The treatment groups contained 25 and 50% of either PSM or PPCPS <span class="hlt">protein</span> replaced the fishmeal <span class="hlt">protein</span>. A total of 400 silver catfish, with initial mean weight of 24 ± 0.46 g, were distributed into 20 tanks. For data four orthogonal contrasts were applied: control diet versus PSM diets; control diets versus PPCPS diets; control versus other diets; PSM diets versus PPCPS diets. The results indicated that the fish fed PSM diets had lower weight gain when compared to either control diet or PPCPS. The PPCPS do not affect growth and <span class="hlt">protein</span> efficiency ratio. Lower albumin contents were found for the control diet fish for the contrasts control diet versus PPCPS diet and control diet versus other diets. The hepatic ALAT enzyme activity was higher in the fish fed the control diet (P < 0.05). The hepatic ALP was most active in fish that received the PPCPS diets, when comparing control diet versus PPCPS diets and control diet versus other diets. The hepatosomatic index was higher for fish fed the PPCPS. Our results indicated that PPCPS presents relevant nutritional quality for fish and can replace the fish meal <span class="hlt">protein</span> up to 50% without affecting growth, PER and intermediate metabolites in silver catfish.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/26377938','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/26377938"><span id="translatedtitle">Nutritional evaluation of phosphorylated pumpkin seed (Cucurbita moschata) <span class="hlt">protein</span> <span class="hlt">concentrate</span> in silver catfish Rhamdia quelen (Quoy and Gaimard, 1824).</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Lovatto, Naglezi de Menezes; Goulart, Fernanda Rodrigues; de Freitas, Silvandro Tonetto; Mombach, Patricia Inês; Loureiro, Bruno Bianch; Bender, Ana Betine Beutinger; Boligon, Aline Augusti; Radünz Neto, João; da Silva, Leila Picolli</p> <p>2015-12-01</p> <p>An 8-week feeding trial was conducted to evaluate the effect of replacing fish meal with pumpkin seed meal (PSM) or phosphorylated <span class="hlt">protein</span> <span class="hlt">concentrate</span> of pumpkin seed meal (PPCPS) on growth and metabolic responses of silver catfish. Five isonitrogenous and isocaloric diets were formulated. Control diet contained fish meal as the main <span class="hlt">protein</span> source. The treatment groups contained 25 and 50% of either PSM or PPCPS <span class="hlt">protein</span> replaced the fishmeal <span class="hlt">protein</span>. A total of 400 silver catfish, with initial mean weight of 24 ± 0.46 g, were distributed into 20 tanks. For data four orthogonal contrasts were applied: control diet versus PSM diets; control diets versus PPCPS diets; control versus other diets; PSM diets versus PPCPS diets. The results indicated that the fish fed PSM diets had lower weight gain when compared to either control diet or PPCPS. The PPCPS do not affect growth and <span class="hlt">protein</span> efficiency ratio. Lower albumin contents were found for the control diet fish for the contrasts control diet versus PPCPS diet and control diet versus other diets. The hepatic ALAT enzyme activity was higher in the fish fed the control diet (P < 0.05). The hepatic ALP was most active in fish that received the PPCPS diets, when comparing control diet versus PPCPS diets and control diet versus other diets. The hepatosomatic index was higher for fish fed the PPCPS. Our results indicated that PPCPS presents relevant nutritional quality for fish and can replace the fish meal <span class="hlt">protein</span> up to 50% without affecting growth, PER and intermediate metabolites in silver catfish. PMID:26377938</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/23864192','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/23864192"><span id="translatedtitle">Selective and efficient extraction of recombinant <span class="hlt">proteins</span> from the periplasm of Escherichia coli using low <span class="hlt">concentrations</span> of chemicals.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Jalalirad, Reza</p> <p>2013-10-01</p> <p>Experiments were conducted to determine chemicals at low <span class="hlt">concentrations</span>, which can be utilized for selective release of periplasmic <span class="hlt">proteins</span>. It was revealed that 80-100 % of the activity of alpha-amylase, beta-lactamase, and Fab D1.3 was retained in the presence of 0.05 and 0.1 % Triton X-100, 0.1 % Tween 20, 0.1 % DOC, 0.01 % BAC, 0.01 % CTAB, 10 mM EDTA, 1 mM and 10 mM DEA, 10 mM NTA, 0.1 and 1 % SHMP, 200 mM urea, 100-500 mM GndCl, and 1 % solvents (hexane, xylene, toluene, benzene, pyridine and isoamyl alcohol). Performance of these chemicals, recognized as generally safe, for selective release of <span class="hlt">proteins</span> from the periplasm of Escherichia coli was investigated. DOC was a general and very efficient agent, and at <span class="hlt">concentrations</span> as low as 0.05, 0.1, and 0.025 %, released beta-lactamase, alpha-amylase, and Fab D1.3 selectively with yield factors of 2.7, 2.3, and 3.6 times greater than osmotic shock procedure, respectively. EDTA (1 and 10 mM) discharged Fab D1.3 with efficiency more than osmotic shock (target <span class="hlt">protein</span> yield of 110 and 138 %, correspondingly). Isoamyl alcohol (10 % v/v) was effective for periplasmic release of alpha-amylase and particularly Fab D1.3, with target <span class="hlt">protein</span> yields of 75 and 168 %, respectively.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1302424','PMC'); return false;" href="https://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1302424"><span id="translatedtitle">Resonance energy transfer in a calcium <span class="hlt">concentration</span>-dependent cameleon <span class="hlt">protein</span>.</span></a></p> <p><a target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pmc">PubMed Central</a></p> <p>Habuchi, Satoshi; Cotlet, Mircea; Hofkens, Johan; Dirix, Gunter; Michiels, Jan; Vanderleyden, Jos; Subramaniam, Vinod; De Schryver, Frans C</p> <p>2002-01-01</p> <p>We report investigations of resonance energy transfer in the green fluorescent <span class="hlt">protein</span> and calmodulin-based fluorescent indicator constructs for Ca(2+) called cameleons using steady-state and time-resolved spectroscopy of the full construct and of the component green fluorescent <span class="hlt">protein</span> mutants, namely ECFP (donor) and EYFP (acceptor). EYFP displays a complicated photophysical behavior including protonated and deprotonated species involved in an excited-state proton transfer. When EYFP is excited in the absorption band of the protonated species, a fast nonradiative deactivation occurs involving almost 97% of the excited protonated population and leading to a low efficiency of excited-state proton transfer to the deprotonated species. ECFP displays a multiexponential fluorescence decay with a major contributing component of 3.2 ns. The time-resolved fluorescence data obtained upon excitation at 420 nm of Ca(2+)-free and Ca(2+)-bound YC3.1 cameleon constructs point to the existence of different conformations of calmodulin dependent on Ca(2+) binding. Whereas steady-state data show only an increase in the efficiency of energy transfer upon Ca(2+) binding, the time-resolved data demonstrate the existence of three distinct conformations/populations within the investigated sample. Although the mechanism of the interconversion between the different conformations and the extent of interconversion are still unclear, the time-resolved fluorescence data offer an estimation of the rate constants, of the efficiency of the energy transfer, and of the donor-acceptor distances in the Ca(2+)-free and Ca(2+)-bound YC3.1 samples. PMID:12496116</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/23627930','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/23627930"><span id="translatedtitle"><span class="hlt">Protein</span> oxidation at different salt <span class="hlt">concentrations</span> affects the cross-linking and gelation of pork myofibrillar <span class="hlt">protein</span> catalyzed by microbial transglutaminase.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Li, Chunqiang; Xiong, Youling L; Chen, Jie</p> <p>2013-06-01</p> <p>In a fabricated then restructured meat product, <span class="hlt">protein</span> gelation plays an essential role in producing desirable binding and fat-immobilization properties. In the present study, myofibrillar <span class="hlt">protein</span> (MFP) suspended in 0.15, 0.45, and 0.6 M NaCl was subjected to hydroxyl radical stress for 2 or 24 h and then treated with microbial transglutaminase (MTGase) in 0.6 M NaCl (E : S = 1 : 20) at 4 and 15 °C for 2 h. <span class="hlt">Protein</span> cross-linking and dynamic rheological tests were performed to assess the efficacy of MTGase for mediating the gelation of oxidized MFP. MTGase treatments affected more remarkable polymerization of myosin in oxidized MFP than in nonoxidized, especially for samples oxidized at 0.6 M NaCl. Notably, the extent of MTGase-induced myosin cross-linking at 15 °C in oxidized MFP improved up to 46.8%, compared to 31.6% in nonoxidized MFP. MTGase treatment at 4 °C for MFP oxidized in 0.6 M NaCl, but not MFP oxidized in 0.15 M NaCl, produced stronger gels than nonoxidized MFP (P < 0.05). The final (75 °C) storage modulus (G') of oxidized MFP gels was significantly greater than that of nonoxidized, although the G' of the transient peak (∼44.5 °C) showed the opposite trend. Overall, oxidation at high salt <span class="hlt">concentrations</span> significantly improved MTGase-mediated myosin cross-linking and MFP gelation. This might be because under this condition, MTGase had an increased accessibility to glutamine and lysine residues to effectively initiate <span class="hlt">protein-protein</span> interactions and gel network formation. PMID:23627930</p> </li> </ol> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_21");'>21</a></li> <li><a href="#" onclick='return showDiv("page_22");'>22</a></li> <li class="active"><span>23</span></li> <li><a href="#" onclick='return showDiv("page_24");'>24</a></li> <li><a href="#" onclick='return showDiv("page_25");'>25</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div><!-- col-sm-12 --> </div><!-- row --> </div><!-- page_23 --> <div id="page_24" class="hiddenDiv"> <div class="row"> <div class="col-sm-12"> <div class="pull-right"> <ul class="pagination"> <li><a href="#" onclick='return showDiv("page_1");'>«</a></li> <li><a href="#" onclick='return showDiv("page_21");'>21</a></li> <li><a href="#" onclick='return showDiv("page_22");'>22</a></li> <li><a href="#" onclick='return showDiv("page_23");'>23</a></li> <li class="active"><span>24</span></li> <li><a href="#" onclick='return showDiv("page_25");'>25</a></li> <li><a href="#" onclick='return showDiv("page_25");'>»</a></li> </ul> </div> </div> </div> <div class="row"> <div class="col-sm-12"> <ol class="result-class" start="461"> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/21916247','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/21916247"><span id="translatedtitle">[Dynamics of blood <span class="hlt">concentration</span> of neurospecific <span class="hlt">proteins</span> and risk of neuropathy development in the conditions of 105-day confinement].</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Nichiporuk, I A; Vasil'eva, G Iu; Rykova, M P; Morukov, B V</p> <p>2011-01-01</p> <p>Six male volunteers (aged 25 to 40 years) were subjects in all-round psychophysiological, hormonal and immunological studies before, in and after 105-day isolation and confinement. Blood was drawn and the 16-factorial Cattell personality inventory was filled out every 30 days. <span class="hlt">Concentrations</span> of blood hormones, neurospecific <span class="hlt">proteins</span> and cytokines point to a close interrelation between antibody titers to myelin-associated glycoprotein and changes in the parameters of metabolism and reproduction-related hormones, as well as cytokines and individual psychophysiology (extra-introversion, dominance, intropunitiveness, social contact selectivity, etc.), and suggest a minimum risk of demyelinizing neuropathy due to exposure to the conditions of isolation and confinement.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('https://www.ncbi.nlm.nih.gov/pubmed/20120953','PUBMED'); return false;" href="https://www.ncbi.nlm.nih.gov/pubmed/20120953"><span id="translatedtitle">[Evaluation of the usefulness cerebrospinal fluid myelin basic <span class="hlt">protein</span> (MBP) <span class="hlt">concentration</span> examination in patients with Lyme neuroborreliosis--preliminary study].</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Kepa, Lucjan</p> <p>2009-01-01</p> <p>The aim of the study was evaluation of usefulness of cerebrospinal fluid (CSF) myelin basic <span class="hlt">protein</span> (MBP) level examination in diagnostics of Lyme neuroborreliosis. The study was performed in 24 subjects. In all individuals CSF MBP <span class="hlt">concentration</span> was estimated on the 1st day of hospitalization. In patients with depressive and cognitive impairments, proved in neuropsychological tests (group I), mean CSF MBP <span class="hlt">concentration</span> was 3.1 ng/mL, whereas in subjects without abnormalities in tests (group II), respectively, 1.2 ng/mL. The difference of mean CSF MBP levels was statistically significant (p<0.01). The obtained results indicate usefulness of this CSF parameter, besides neuropsychological tests, in objective evaluation of clinical state in patients with chronic Lyme neuroborreliosis.</p> </li> <li> <p><a target="_blank" onclick="trackOutboundLink('http://www.ncbi.nlm.nih.gov/pubmed/19617516','PUBMED'); return false;" href="http://www.ncbi.nlm.nih.gov/pubmed/19617516"><span id="translatedtitle">Dietary <span class="hlt">protein</span> during gestation affects maternal insulin-like growth factor, insulin-like growth factor binding <span class="hlt">protein</span>, leptin <span class="hlt">concentrations</span>, and fetal growth in heifers.</span></a></p> <p><a target="_blank" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?DB=pubmed">PubMed</a></p> <p>Sullivan, T M; Micke, G C; Perkins, N; Martin, G B; Wallace, C R; Gatford, K L; Owens, J A; Perry, V E A</p> <p>2009-10-01</p> <p>The influence of supplemental <span class="hlt">protein</span> during gestation on maternal hormones and fetal growth was determined in composite beef heifers. At AI, 118 heifers were stratified by BW within each composite genotype (BeefX = 1/2 Senepol, 1/4 Brahman, 1/8 Charolais, 1/8 Red Angus and CBX = 1/2 Senepol, 1/4 Brahman, 1/4 Charolais) into 4 treatment groups: high high (HH = 1.4 kg CP/d for first and second trimesters of gestation), high low (HL = 1.4 kg of CP/d for first trimester and 0.4 kg of CP/d for second trimester), low high (lowH = 0.4 kg CP/d for first trimester and 1.4 kg of CP/d and for second trimester), or low low (LL = 0.4 kg CP/d for first and second trimesters). Maternal plasma IGF-I and -II, total IGFBP, and leptin <span class="hlt">concentrations</span> were determined at 14 d before AI and at d 28, 82, 179, and 271 post-AI (mean gestation length 286 d), and leptin <span class="hlt">concentrations</span> were also determined at calving. Increased dietary <span class="hlt">protein</span> increased maternal plasma IGF-I (P < 0.001 on d 28, 82, and 179), IGF-