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1

A rapid and transient ROS generation by cadmium triggers apoptosis via caspase-dependent pathway in HepG2 cells and this is inhibited through N-acetylcysteine-mediated catalase upregulation  

SciTech Connect

Although reactive oxygen species (ROS) have been implicated in cadmium (Cd)-induced hepatotoxicity, the role of ROS in this pathway remains unclear. Therefore, we attempted to determine the molecular mechanisms relevant to Cd-induced cell death in HepG2 cells. Cd was found to induce apoptosis in the HepG2 cells in a time- and dose-dependent fashion, as confirmed by DNA fragmentation analysis and TUNEL staining. In the early stages, both rapid and transient ROS generation triggered apoptosis via Fas activation and subsequent caspase-8-dependent Bid cleavage, as well as by calpain-mediated mitochondrial Bax cleavage. The timing of Bid activation was coincided with the timing at which the mitochondrial transmembrane potential (MMP) collapsed as well as the cytochrome c (Cyt c) released into the cytosol. Furthermore, mitochondrial permeability transition (MPT) pore inhibitors, such as cyclosporin A (CsA) and bongkrekic acid (BA), did not block Cd-induced ROS generation, MMP collapse and Cyt c release. N-acetylcysteine (NAC) pretreatment resulted in the complete inhibition of the Cd-induced apoptosis via catalase upregulation and subsequent Fas downregulation. NAC treatment also completely blocked the Cd-induced intracellular ROS generation, MMP collapse and Cyt c release, indicating that Cd-induced mitochondrial dysfunction may be regulated indirectly by ROS-mediated signaling pathway. Taken together, a rapid and transient ROS generation by Cd triggers apoptosis via caspase-dependent pathway and subsequent mitochondrial pathway. NAC inhibits Cd-induced apoptosis through the blocking of ROS generation as well as the catalase upregulation.

Oh, Seon-Hee [Research Center for Resistant Cells, College of Medicine, Chosun University, Seosuk-dong, Dong-gu, Gwangju 501-759 (Korea, Republic of); Lim, Sung-Chul [Research Center for Resistant Cells, College of Medicine, Chosun University, Seosuk-dong, Dong-gu, Gwangju 501-759 (Korea, Republic of) and Department of Pathology, College of Medicine, Chosun University, Seosuk-dong, Dong-gu, Gwangju 501-759 (Korea, Republic of)]. E-mail: sclim@chosun.ac.kr

2006-05-01

2

Glabridin, a phytoestrogen from licorice root, up-regulates manganese superoxide dismutase, catalase and paraoxonase 2 under glucose stress.  

PubMed

The risk of death from cardiovascular diseases (CVDs), which are exacerbated by oxidative stress, is higher in diabetic women. This phenomenon has been attributed to the loss of estradiol-vascular protection. Such knowledge led us to examine the potential of glabridin, a phytoestrogen, to substitute estradiol up-regulation of antioxidant enzymes under high glucose conditions. Chronic glucose stress was found to down-regulate catalase (CAT) and paraoxonase 2 (PON2) mRNA expression by 20% and 17%, respectively, and to decrease PON2 activity by 83% in macrophages. Inflammatory conditions had an additive effect on PON2 expression in a time-dependent manner. Treatment with glabridin, under high glucose stress, increased PON2 activity by 60% and up-regulated its mRNA expression by 3.5 fold. Furthermore, glabridin up-regulated the expression of manganese superoxide dismutase (Mn-SOD) and CAT in monocytes. In conclusion, glabridin has the potential of strengthening the antioxidant defense mechanism and may serve as an antiatherogenic agent in diabetes. PMID:21053390

Yehuda, Itamar; Madar, Zecharia; Szuchman-Sapir, Andrea; Tamir, Snait

2010-10-29

3

The catalase and superoxide dismutase genes are transcriptionally up-regulated upon oxidative stress in the strictly anaerobic archaeon Methanosarcina barkeri.  

PubMed

Methanosarcina barkeri is a strictly anaerobic methanogenic archaeon, which can survive oxidative stress. The oxidative stress agent paraquat (PQ) suppressed growth of M. barkeri at concentrations of 50-200 microM. Hydrogen peroxide (H2O2) inhibited growth at concentrations of 0.4-1.6 mM. Catalase activity in cell-free extracts of M. barkeri increased about threefold during H2O2 stress (1.3 mM H2O2, 2-4 h exposure) and nearly twofold during superoxide stress (160 microM PQ, 2 h exposure). PQ (160 microM, 2-4 h exposure) and H2O2 (1.3 mM, 2 h exposure) also influenced superoxide dismutase activity in cell-free extracts of M. barkeri. Dot-blot analysis was performed on total RNA isolated from H2O2- and PQ-exposed cultures, using labelled internal DNA fragments of the sod and kat genes. It was shown that H2O2 but not PQ strongly induced up-regulation of the kat gene. PQ and to a lesser degree H2O2 induced the expression of superoxide dismutase. The results indicate the regulation of the adaptive response of M. barkeri to different oxidative stresses. PMID:16735730

Brioukhanov, Andrei L; Netrusov, Alexander I; Eggen, Rik I L

2006-06-01

4

Bentonite-supported catalase  

Microsoft Academic Search

The properties of the clay bentonite as a support for enzyme immobilization were studied using the enzyme catalase. Such an immobilization does not result in en- zyme inactivation and constitutes a valuable method for immobilizing catalase at high ionic strength. The bentonite-supported catalase was characterized in terms of pH and ionic strength dependencies, thermal and storage stability and kinetic parameters.

S. Alkan; H. Ceylan; O. Arslan

2005-01-01

5

Catalase Test Protocol  

NSDL National Science Digital Library

The catalase test is used to detect the presence of the enzyme catalase in bacteria. Catalase serves to neutralize the bactericidal effects of hydrogen peroxide. Its concentration in bacteria has been correlated with pathogenicity. This enzymatic test is essential in the scheme of identification for gram-positive organisms and certain gram-negative organisms. It is a primary test used in the differentiation of staphylococci and streptococci.

American Society For Microbiology;

2010-11-11

6

BAM R12: Catalase Test  

Center for Food Safety and Applied Nutrition (CFSAN)

... Pesticide Analytical Manual (PAM). -. BAM R12: Catalase Test. January 2001. Bacteriological Analytical Manual. R12 Catalase Test. ... More results from www.fda.gov/food/foodscienceresearch/laboratorymethods

7

Induction of cyclooxygenase-2 in macrophages by catalase: role of NF-?B and PI3K signaling pathways  

Microsoft Academic Search

Induction of COX-2 by catalase in smooth muscle cells, endothelial cells, and neuronal cells has been previously reported. However, the mechanism by which catalase up-regulates COX-2 remains poorly understood. In this study, we investigated the effect of catalase on induction of COX-2 in macrophages. The addition of catalase into Raw 264.7 macrophages induced COX-2 expression that was correlated with increased

Byeong-Churl Jang; Do-Hyun Kim; Jong-Wook Park; Taeg Kyu Kwon; Sang-Pyo Kim; Dae-Kyu Song; Jong-Gu Park; Jae-Hoon Bae; Kyo-Chul Mun; Won-Ki Baek; Min-Ho Suh; Timothy Hla; Seong-Il Suh

2004-01-01

8

Catalase Hybrid Enzymes in Maize  

Microsoft Academic Search

In maize endosperm there are two electrophoretic variants of catalase. The variations are under genetic control, and the heterozygote shows three hybrid enzymes with mobilities intermediate between the parental enzymes. Thus, maize catalase may exist as a tetramer, and the hybrid enzymes may be formed by random association of two different catalase monomers.

Lars Beckman; John G. Scandalios; James L. Brewbaker

1964-01-01

9

Catalase is inhibited by flavonoids.  

PubMed

Catalases, heme enzymes, which catalyze decomposition of hydrogen peroxide to water and molecular oxygen, belong to the antioxidant defense system of the cell. In this work we have shown that catalase from bovine liver is inhibited by flavonoids. The inhibition is, at least partially, due to the formation of hydrogen bonds between catalase and flavonoids. In the presence of some flavonoids the formation of unreactive catalase compound II has been detected. The most potent catalase inhibitors among the tested flavonoids have appeared myricetin, epicatechin gallate and epigallocatechin gallate. The relationship between the degree of enzyme inhibition and molecular structure of flavonoids has been analyzed. PMID:23567286

Krych, Justyna; Gebicka, Lidia

2013-04-06

10

Immobilization of catalase on chitosan film  

Microsoft Academic Search

Catalase was immobilized on the chitosan film that is a natural polymer. Studies were done on free catalase and immobilized catalase on chitosan film concerning the determination of optimum temperature, optimum pH, thermal stability, storage stability, operational stability, and kinetic parameters. It was determined that optimum temperature for free catalase and immobilized catalase on chitosan film is 25°C, and optimum

?enay Akku? Çetinus; H. Nursevin Öztop

2000-01-01

11

Non-heme manganese catalase - the 'other' catalase  

PubMed Central

Non-heme manganese catalases are widely distributed over microbial life and represent an environmentally important alternative to heme-containing catalases in antioxidant defense. Manganese catalases contain a binuclear manganese complex as their catalytic active site rather than a heme, and cycle between Mn2(II,II) and Mn2(III,III) states during turnover. X-ray crystallography has revealed the key structural elements of the binuclear manganese active site complex that can serve as the starting point for computational studies on the protein. Four manganese catalase enzymes have been isolated and characterized, and the enzyme appears to have a broad phylogenetic distribution including both bacteria and archae. More than 100 manganese catalase genes have been annotated in genomic databases, although the assignment of many of these putative manganese catalases needs to be experimentally verified. Iron limitation, exposure to low levels of peroxide stress, thermostability and cyanide resistance may provide the biological and environmental context for the occurrence of manganese catalases.

Whittaker, James W.

2012-01-01

12

Non-heme manganese catalase--the 'other' catalase.  

PubMed

Non-heme manganese catalases are widely distributed over microbial life and represent an environmentally important alternative to heme-containing catalases in antioxidant defense. Manganese catalases contain a binuclear manganese complex as their catalytic active site rather than a heme, and cycle between Mn(2)(II,II) and Mn(2)(III,III) states during turnover. X-ray crystallography has revealed the key structural elements of the binuclear manganese active site complex that can serve as the starting point for computational studies on the protein. Four manganese catalase enzymes have been isolated and characterized, and the enzyme appears to have a broad phylogenetic distribution including both bacteria and archae. More than 100 manganese catalase genes have been annotated in genomic databases, although the assignment of many of these putative manganese catalases needs to be experimentally verified. Iron limitation, exposure to low levels of peroxide stress, thermostability and cyanide resistance may provide the biological and environmental context for the occurrence of manganese catalases. PMID:22198285

Whittaker, James W

2011-12-16

13

7 CFR 58.432 - Catalase.  

Code of Federal Regulations, 2010 CFR

...for Raw Material § 58.432 Catalase. The catalase preparation shall be a stable, buffered solution, neutral in pH, having a potency of not less...milliliter. The source of the catalase, its application and usage...

2009-01-01

14

7 CFR 58.432 - Catalase.  

Code of Federal Regulations, 2013 CFR

...for Raw Material § 58.432 Catalase. The catalase preparation shall be a stable, buffered solution, neutral in pH, having a potency of not less...milliliter. The source of the catalase, its application and usage...

2013-01-01

15

7 CFR 58.432 - Catalase.  

Code of Federal Regulations, 2010 CFR

...for Raw Material § 58.432 Catalase. The catalase preparation shall be a stable, buffered solution, neutral in pH, having a potency of not less...milliliter. The source of the catalase, its application and usage...

2010-01-01

16

Regulation of Brucella abortus Catalase  

PubMed Central

All aerobic organisms have mechanisms that protect against oxidative compounds. Catalase, peroxidase, superoxide dismutase, glutathione, and thioredoxin are widely distributed in many taxa and constitute elements of a nearly ubiquitous antioxidant metabolic strategy. Interestingly, the regulatory mechanisms that control these elements are rather different depending on the nature of the oxidative stress and the organism. Catalase is well documented to play an important role in protecting cells from oxidative stress. In particular, pathogenic bacteria seem to use this enzyme as a defensive tool against attack by the host. To investigate the significance of catalase in hostile environments, we made catalase deletion mutations in two different B. abortus strains and used two-dimensional gel analysis, survival tests, and adaptation experiments to explore the behavior and role of catalase under several oxidative stress conditions. These studies show that B. abortus strains that do not express catalase activity exhibit increased sensitivity to hydrogen peroxide. We also demonstrate that catalase expression is regulated in this species, and that preexposure to a sublethal concentration of hydrogen peroxide allows B. abortus to adapt so as to survive subsequent exposure to higher concentrations of hydrogen peroxide.

Kim, Jeong-a; Sha, Zengyu; Mayfield, John E.

2000-01-01

17

High dietary fat selectively increases catalase expression within cardiac mitochondria.  

PubMed

Obesity is a predictor of diabetes and cardiovascular disease. One consequence of obesity is dyslipidemia characterized by high blood triglycerides. It has been proposed that oxidative stress, driven by utilization of lipids for energy, contributes to these diseases. The effects of oxidative stress are mitigated by an endogenous antioxidant enzyme network, but little is known about its response to high fat utilization. Our experiments used a multiplexed quantitative proteomics method to measure antioxidant enzyme expression in heart tissue in a mouse model of diet-induced obesity. This experiment showed a rapid and specific up-regulation of catalase protein, with subsequent assays showing increases in activity and mRNA. Catalase, traditionally considered a peroxisomal protein, was found to be present in cardiac mitochondria and significantly increased in content and activity during high fat feeding. These data, coupled with the fact that fatty acid oxidation enhances mitochondrial H(2)O(2) production, suggest that a localized catalase increase is needed to consume excessive mitochondrial H(2)O(2) produced by increased fat metabolism. To determine whether the catalase-specific response is a common feature of physiological conditions that increase blood triglycerides and fatty acid oxidation, we measured changes in antioxidant expression in fasted versus fed mice. Indeed, a similar specific catalase increase was observed in mice fasted for 24 h. Our findings suggest a fundamental metabolic process in which catalase expression is regulated to prevent damage while preserving an H(2)O(2)-mediated sensing of diet composition that appropriately adjusts insulin sensitivity in the short term as needed to prioritize lipid metabolism for complete utilization. PMID:23204527

Rindler, Paul M; Plafker, Scott M; Szweda, Luke I; Kinter, Michael

2012-11-30

18

Molecular evolution of maize catalases and their relationship to other eukaryotic and prokaryotic catalases  

Microsoft Academic Search

We have compared the nucleotide and protein sequences of the three maize catalase genes with other plant catalases to reconstruct\\u000a the evolutionary relationship among these catalases. These sequences were also compared with other eukaryotic and prokaryotic\\u000a catalases. Phylogenies based on distances and parsimony analysis show that all plant catalases derive from a common ancestral\\u000a catalase gene and can be divided

Lingqiang Guan; John G. Scandalios

1996-01-01

19

Redundancy, phylogeny and differential expression of Histoplasma capsulatum catalases  

Microsoft Academic Search

Histoplasma capsulatum produces an extracellular catalase termed M antigen, which is similar to catalase B of Aspergillus and Emericella species. Evidence is presented here for two additional catalase isozymes in H. capsulatum. Catalase A is highly similar to a large-subunit catalase in Aspergillus and Emericella species, while catalase P is a small-subunit catalase protein with greatest similarity to known peroxisomal

Clayton H. Johnson; Martin G. Klotz; J. Lyndal York; Volker Kruft; Joan E. McEwen; Donald W. Reynolds

2002-01-01

20

Coimmobilization of Superoxide Dismutase, Catalase, and Peroxidase  

Microsoft Academic Search

Various orders of sequential coimmobilization of superoxide dismutase (SOD), catalase, and horseradish peroxidase (HRP) were tested in order to prepare a multienzyme antioxidant complex of these enzymes. Simultaneous coimmobilization of catalase with a preliminarily cross-linked complex between SOD and HRP was found to be the optimum procedure. The catalytic enzyme activity and working stability of catalase was tested kinetically in

A. N. Eremin

2001-01-01

21

High Temperature and Alkaline Stable Catalase.  

National Technical Information Service (NTIS)

The invention relates to thermal and pH stable catalases. One catalase of the invention was purified and characterized from Thermus brockianus. As a part of the characterization, the enzyme was compared to typical catalases from commercial sources and fou...

K. D. Schaller V. Thompson W. A. Apel

2004-01-01

22

The Role of Catalase in Pulmonary Fibrosis  

Microsoft Academic Search

BACKGROUND: Catalase is preferentially expressed in bronchiolar and alveolar epithelial cells, and acts as an endogenous antioxidant enzyme in normal lungs. We thus postulated epithelial damage would be associated with a functional deficiency of catalase during the development of lung fibrosis. METHODS: The present study evaluates the expression of catalase mRNA and protein in human interstitial pneumonias and in mouse

Nao Odajima; Tomoko Betsuyaku; Katsura Nagai; Chinatsu Moriyama; Da-Hong Wang; Tomoko Takigawa; Keiki Ogino; Masaharu Nishimura

2010-01-01

23

The Role of Catalase in Pulmonary Fibrosis  

PubMed Central

Background Catalase is preferentially expressed in bronchiolar and alveolar epithelial cells, and acts as an endogenous antioxidant enzyme in normal lungs. We thus postulated epithelial damage would be associated with a functional deficiency of catalase during the development of lung fibrosis. Methods The present study evaluates the expression of catalase mRNA and protein in human interstitial pneumonias and in mouse bleomycin-induced lung injury. We examined the degree of bleomycin-induced inflammation and fibrosis in the mice with lowered catalase activity. Results In humans, catalase was decreased at the levels of activity, protein content and mRNA expression in fibrotic lungs (n = 12) compared to control lungs (n = 10). Immunohistochemistry revealed a decrease in catalase in bronchiolar epithelium and abnormal re-epithelialization in fibrotic areas. In C57BL/6J mice, catalase activity was suppressed along with downregulation of catalase mRNA in whole lung homogenates after bleomycin administration. In acatalasemic mice, neutrophilic inflammation was prolonged until 14 days, and there was a higher degree of lung fibrosis in association with a higher level of transforming growth factor-? expression and total collagen content following bleomycin treatment compared to wild-type mice. Conclusions Taken together, these findings demonstrate diminished catalase expression and activity in human pulmonary fibrosis and suggest the protective role of catalase against bleomycin-induced inflammation and subsequent fibrosis.

2010-01-01

24

Sirt1 protects against oxidative stress-induced renal tubular cell apoptosis by the bidirectional regulation of catalase expression  

SciTech Connect

NAD{sup +}-dependent protein deacetylase Sirt1 regulates cellular apoptosis. We examined the role of Sirt1 in renal tubular cell apoptosis by using HK-2 cells, proximal tubular cell lines with or without reactive oxygen species (ROS), H{sub 2}O{sub 2}. Without any ROS, Sirt1 inhibitors enhanced apoptosis and the expression of ROS scavenger, catalase, and Sirt1 overexpression downregulated catalase. When apoptosis was induced with H{sub 2}O{sub 2}, Sirt1 was upregulated with the concomitant increase in catalase expression. Sirt1 overexpression rescued H{sub 2}O{sub 2}-induced apoptosis through the upregulation of catalase. H{sub 2}O{sub 2} induced the nuclear accumulation of forkhead transcription factor, FoxO3a and the gene silencing of FoxO3a enhanced H{sub 2}O{sub 2}-induced apoptosis. In conclusion, endogenous Sirt1 maintains cell survival by regulating catalase expression and by preventing the depletion of ROS required for cell survival. In contrast, excess ROS upregulates Sirt1, which activates FoxO3a and catalase leading to rescuing apoptosis. Thus, Sirt1 constitutes a determinant of renal tubular cell apoptosis by regulating cellular ROS levels.

Hasegawa, Kazuhiro [Department of Internal Medicine, Keio University, 35 Shinanomachi, Shinjuku-ku, Tokyo 1608582 (Japan); Wakino, Shu [Department of Internal Medicine, Keio University, 35 Shinanomachi, Shinjuku-ku, Tokyo 1608582 (Japan)], E-mail: swakino@sc.itc.keio.ac.jp; Yoshioka, Kyoko; Tatematsu, Satoru; Hara, Yoshikazu; Minakuchi, Hitoshi; Washida, Naoki; Tokuyama, Hirobumi; Hayashi, Koichi; Itoh, Hiroshi [Department of Internal Medicine, Keio University, 35 Shinanomachi, Shinjuku-ku, Tokyo 1608582 (Japan)

2008-07-18

25

Purification and characterization of liver catalase in acatalasemic beagle dog: comparison with normal dog liver catalase  

Microsoft Academic Search

Catalase from acatalasemic dog liver was purified to homogeneity and its properties were compared with those of normal dog liver catalase. The purified acatalasemic and normal dog liver catalases were found to have the same molecular weight (230,000 Da) and isoelectric point (pI: 6.0–6.2) and both enzymes contained four hematins per molecule. The catalytic activity of catalase from acatalasemic dog

Kouichi Nakamura; Misa Watanabe; Yukio Sasaki; Toshihiko Ikeda

2000-01-01

26

Search for Micromycetes Producing Extracellular Catalase and Study of Conditions of Catalase Synthesis  

Microsoft Academic Search

Production of extracellular catalase by microscopic mycelial fungi (255 strains) belonging to different taxonomic groups was studied. Producers of extracellular catalase were found among fungi of the genera Penicillium, Talaromyces, and Aspergillus. Strains of the genus Penicillium were the most active producers. The formation of catalase depended on the initial pH, carbon and nitrogen sources and their ratio, and the

A. V. Kurakov; M. B. Kupletskaya; E. V. Skrynnikova; N. G. Somova

2001-01-01

27

Influence of stabilizers cosolutes on catalase conformation  

Microsoft Academic Search

The effects of sucrose, mannitol and betaine on the thermodynamic stability and the conformational state of the catalase enzyme were analyzed in order to understand the molecular mechanism whereby the solutes stabilized the enzyme. Catalase was selected as the model enzyme because it is used in several biotechnological processes. In the presence of each cosolute, our data have shown that

Soledad Belluzo; Valeria Boeris; Beatriz Farruggia; Guillermo Picó

2011-01-01

28

Aspergillus fumigatus catalases: cloning of an Aspergillus nidulans catalase B homologue and evidence for at least three catalases.  

PubMed

The presence of catalases in the water soluble fractions of three Aspergillus fumigatus strains was investigated using non-denaturing and denaturing polyacrylamide gel electrophoresis and Western analysis. Using non-denaturing polyacrylamide gel electrophoresis and staining for catalase activity, three separate catalases were identified. An A. fumigatus catalase gene (catB) was cloned from genomic DNA using the Aspergillus niger catR gene as a probe. Polyclonal antibodies were raised to a glutathione S-transferase-CatB fusion product expressed in Escherichia coli. Western analysis indicated that, under denaturing conditions, the polyclonal antibody recognised a 90-kDa band and under non-denaturing conditions, two separate bands were identified. These results indicate that A. fumigatus in addition to CatB, produces at least two other catalases, one of which is similar in size to CatB. The polyclonal antibody was also used to observe catalase expression in mice, experimentally infected with A. fumigatus. Staining was observed heterogeneously throughout the fungal hyphae. This result indicates that catalase is produced by A. fumigatus during invasive aspergillosis. PMID:10076909

Takasuka, T; Sayers, N M; Anderson, M J; Benbow, E W; Denning, D W

1999-02-01

29

21 CFR 173.135 - Catalase derived from Micrococcus lysodeikticus.  

Code of Federal Regulations, 2010 CFR

...2010-01-01 2009-04-01 true Catalase derived from Micrococcus lysodeikticus...Preparations and Microorganisms § 173.135 Catalase derived from Micrococcus lysodeikticus. Bacterial catalase derived from Micrococcus...

2010-01-01

30

Tubular Flow Reactor Studies of Immobilized Catalase and Glucose Oxidase.  

National Technical Information Service (NTIS)

Catalase was immobilized on porous glass and several nickel silica alumina supports. Catalase immobilized on nickel silica alumina was studied in a tubular plug flow reactor. Several physical mixtures of singly immobilized catalase on nickel silica alumin...

A. D. Traher

1973-01-01

31

21 CFR 173.135 - Catalase derived from Micrococcus lysodeikticus.  

Code of Federal Regulations, 2010 CFR

...2009-04-01 2009-04-01 false Catalase derived from Micrococcus lysodeikticus...Preparations and Microorganisms § 173.135 Catalase derived from Micrococcus lysodeikticus. Bacterial catalase derived from Micrococcus...

2009-04-01

32

Evolution of Catalases from Bacteria to Humans  

PubMed Central

Excessive hydrogen peroxide is harmful for almost all cell components, so its rapid and efficient removal is of essential importance for aerobically living organisms. Conversely, hydrogen peroxide acts as a second messenger in signal-transduction pathways. H2O2 is degraded by peroxidases and catalases, the latter being able both to reduce H2O2 to water and to oxidize it to molecular oxygen. Nature has evolved three protein families that are able to catalyze this dismutation at reasonable rates. Two of the protein families are heme enzymes: typical catalases and catalase–peroxidases. Typical catalases comprise the most abundant group found in Eubacteria, Archaeabacteria, Protista, Fungi, Plantae, and Animalia, whereas catalase–peroxidases are not found in plants and animals and exhibit both catalatic and peroxidatic activities. The third group is a minor bacterial protein family with a dimanganese active site called manganese catalases. Although catalyzing the same reaction (2 H2O2 ? 2 H2O + O2), the three groups differ significantly in their overall and active-site architecture and the mechanism of reaction. Here, we present an overview of the distribution, phylogeny, structure, and function of these enzymes. Additionally, we report about their physiologic role, response to oxidative stress, and about diseases related to catalase deficiency in humans.

Zamocky, Marcel; Furtmuller, Paul G.; Obinger, Christian

2010-01-01

33

[Catalase activity of hydrocarbon-oxidizing bacteria].  

PubMed

The dynamics of catalase activity of the hydrocarbon-oxidizing bacteria Cordona terrae, Rhodococcus rubropertinctus, and Rhodococcus erythropolis during petroleum product destruction has been studied. A direct relationship between decreasing catalase activity of hydrocarbon-oxidizing microorganisms and the intensity of petroleum product destruction has been established experimentally. The revealed dependence allows one to consider the catalase activity of bacteria as an indicator of the initial stage of petroleum product oxidation and may be used for choosing destructor strains to construct biopreparations suitable for natural ecosystem remediation. PMID:23330387

Gogoleva, O A; Nemtseva, N V; Bukharin, O V

34

Molecular and kinetic study of catalase-1, a durable large catalase of Neurospora crassa  

Microsoft Academic Search

Catalase-1 (Cat-1), one of the two monofunctional catalases of Neurospora crassa, increases during asexual spore formation to constitute 0.6% of total protein in conidia. Cat-1 was purified 170-fold with a yield of 48% from conidiating cultures. Like most monofunctional catalases, Cat-1 is a homotetramer, resistant to inactivation by solvents, fully active over a pH range of 4–12, and inactivated by

Adelaida D??az; Pablo Rangel; Yésika Montes de Oca; Fernando Lled??as; Wilhelm Hansberg

2001-01-01

35

Detection of catalase in rat heart mitochondria.  

PubMed

The presence of heme-containing catalase in rat heart mitochondria (20 +/- 5 units/mg) was demonstrated by biochemical and immunocytochemical analysis. Intact rat heart mitochondria efficiently consumed exogenously added H2O2. The rate of H2O2 consumption was not influenced by succinate, glutamate/malate, or N-ethylmaleimide but was significantly inhibited by cyanide. Hydrogen peroxide decomposition by mitochondria yielded molecular oxygen in a 2:1 stoichiometry, consistent with a catalytic mechanism. Mitochondrial fractionation studies and quantitative electron microscopic immunocytochemistry revealed that most catalase was matrix-associated. Electrophoretic analysis and Western blotting of the mitochondrial matrix fraction indicated the presence of a protein with similar electrophoretic mobility to bovine and rat liver catalase and immunoreactive to anti-catalase antibody. Myocardial tissue has a lower catalase-specific activity and a greater mitochondrial H2O2 production/g of tissue than most organs. Thus catalase, representing 0.025% of heart mitochondrial protein, is important for detoxifying mitochondrial derived H2O2 and represents a key antioxidant defense mechanism for myocardial tissue. PMID:1657986

Radi, R; Turrens, J F; Chang, L Y; Bush, K M; Crapo, J D; Freeman, B A

1991-11-15

36

Protection of Bacillus pumilus Spores by Catalases  

PubMed Central

Bacillus pumilus SAFR-032, isolated at spacecraft assembly facilities of the National Aeronautics and Space Administration Jet Propulsion Laboratory, is difficult to kill by the sterilization method of choice, which uses liquid or vapor hydrogen peroxide. We identified two manganese catalases, YjqC and BPUM_1305, in spore protein extracts of several B. pumilus strains by using PAGE and mass spectrometric analyses. While the BPUM_1305 catalase was present in six of the B. pumilus strains tested, YjqC was not detected in ATCC 7061 and BG-B79. Furthermore, both catalases were localized in the spore coat layer along with laccase and superoxide dismutase. Although the initial catalase activity in ATCC 7061 spores was higher, it was less stable over time than the SAFR-032 enzyme. We propose that synergistic activity of YjqC and BPUM_1305, along with other coat oxidoreductases, contributes to the enhanced resistance of B. pumilus spores to hydrogen peroxide. We observed that the product of the catalase reaction, gaseous oxygen, forms expanding vesicles on the spore surface, affecting the mechanical integrity of the coat layer, resulting in aggregation of the spores. The accumulation of oxygen gas and aggregations may play a crucial role in limiting further exposure of Bacilli spore surfaces to hydrogen peroxide or other toxic chemicals when water is present.

Checinska, Aleksandra; Burbank, Malcolm

2012-01-01

37

Semipermeable Microcapsules containing Catalase for Enzyme Replacement in Acatalasaemic Mice  

Microsoft Academic Search

Semipermeable microcapsules containing catalase can be used to counteract catalase deficiency in acatalasaemic mice. The advantage of such microencapsulated enzymes is that they cannot leak out to become involved in immunological reactions.

T. M. S. Chang; M. J. Poznansky

1968-01-01

38

Immobilization and kinetics of catalase onto magnesium silicate  

Microsoft Academic Search

Bovine liver catalase was immobilized covalently with glutaraldehyde, or glutaraldehyde+3-aminopropionic acid as a spacer, onto magnesium silicate. The coupling time was determined as 2h for immobilization. The pH and temperature optima as well as the changes in the kinetics (Km, Vmax, Ea) of the immobilized catalase was observed and discussed. Immobilized catalase preparations showed higher storage stabilities than free catalase.

S. Seyhan Tukel; Ozlem Alptekin

2004-01-01

39

Formation and use of poly-L-histidine-catalase complexes  

Microsoft Academic Search

Insoluble complexes of poly-L-histidine (polyhistidine) and catalase were prepared by mixing the two reactants together in solution at pH 5.5 and subsequently elevating the pH to approximately 7.0, at which point they precipitated. Complexes formed at optimal ratios of polyhistidine to catalase contained essentially all of the catalase present in the original solution. The catalase present in such complexes contained

Douglas Gibbs; James Varani; Isaac Ginsburg

1989-01-01

40

Molecular Analysis of the DrosophilaCatalase Gene  

Microsoft Academic Search

The main objective of this study was to isolate and characterize the catalase gene and accompanyingcis-regulatory regions inDrosophila melanogaster.Genomic clones were obtained on the basis of cross-hybridization to catalase cDNA and a 7-kbSalI–KpnI fragment encompassing the catalase gene was introduced intoDrosophilaby P element-mediated transformation. A single transgene, when placed in a catalase null background, was sufficient to restore resistance to

William C. Orr; Elizabeth C. Orr; Susan K. Legan; Rajindar S. Sohal

1996-01-01

41

21 CFR 184.1034 - Catalase (bovine liver).  

Code of Federal Regulations, 2010 CFR

...2010-01-01 2009-04-01 true Catalase (bovine liver). 184.1034 Section 184.1034 Food and...Affirmed as GRAS § 184.1034 Catalase (bovine liver). (a) Catalase (bovine liver) (CAS Reg. No. 81457-95-6) is an...

2010-01-01

42

21 CFR 184.1034 - Catalase (bovine liver).  

Code of Federal Regulations, 2010 CFR

...2009-04-01 2009-04-01 false Catalase (bovine liver). 184.1034 Section 184.1034 Food and...Affirmed as GRAS § 184.1034 Catalase (bovine liver). (a) Catalase (bovine liver) (CAS Reg. No. 81457-95-6) is an...

2009-04-01

43

Catalases Are NAD(P)H-Dependent Tellurite Reductases  

Microsoft Academic Search

Reactive oxygen species damage intracellular targets and are implicated in cancer, genetic disease, mutagenesis, and aging. Catalases are among the key enzymatic defenses against one of the most physiologically abundant reactive oxygen species, hydrogen peroxide. The well-studied, heme-dependent catalases accelerate the rate of the dismutation of peroxide to molecular oxygen and water with near kinetic perfection. Many catalases also bind

Iván L. Calderón; Felipe A. Arenas; José Manuel Pérez; Derie E. Fuentes; Manuel A. Araya; Claudia P. Saavedra; Juan C. Tantaleán; Sergio E. Pichuantes; Philip A. Youderian; Claudio C. Vásquez; Christophe Herman

2006-01-01

44

CMC\\/PDM capsule immobilize catalase  

Microsoft Academic Search

The nature of catalase, immobilized in sodium carboxymethyl cellulose (CMC) and poly(n,n-dimethylaminoethyl methacrylate)(PDM), were primarily studied. The results showed that the CMC\\/PDM capsules, which were made by 2.0% of mass concentration of CMC and 25% of mass concentration of PDM, were the smoothest, the hardest, and the most effective. The optimum pH and temperature were 7.0 and 40°C respectively for

Wenlong Hou; Zhiwei Zhang; Shaoli Niu; Yuedong Yang; Zhiqing Duan; Xiaomin Liu

2010-01-01

45

Catalytic scavenging of peroxynitrite by catalase  

Microsoft Academic Search

Peroxynitrite (ONOO?\\/ONOOH), the product of the diffusion controlled reaction between nitric oxide (NO) and superoxide anion (O2-), is a strong oxidizing and nitrating agent. Several heme proteins react rapidly with peroxynitrite, some of them catalyze its decomposition. In this work we found, contrary to previous reports, that catalase, a ferriheme enzyme, catalytically scavenges peroxynitrite. The second-order reaction rate constants of

Lidia Gebicka; Joanna Didik

2009-01-01

46

Role of oxyradicals in the inactivation of catalase by ozone  

SciTech Connect

The antioxidant enzymes, catalase and superoxide dismutase, are inactivated upon exposure to ozone. In this study, the mechanism of this inactivation was examined using catalase as a model system. The data show that the inactivation of catalase is dependent on ozone concentration, time of exposure, and pH. Loss of catalase activity is accompanied with loss of the heme spectra. Tiron, desferal-Mn, trolox-c, and pyruvate protect the enzyme against ozone inactivation. SOD is less effective due to its inactivation by ozone. On the other hand, alcohols do not provide significant protection. The data suggest the possible involvement of superoxide radicals in the inactivation of catalase by ozone.

Whiteside, C.; Hassan, H.M. (North Carolina State Univ., Raleigh (USA))

1988-01-01

47

Probing the binding of flavonoids to catalase by molecular spectroscopy  

NASA Astrophysics Data System (ADS)

The binding of flavonoids (quercetin and myricetin) to catalase was investigated by fluorescence and circular dichroism (CD) techniques under physiological conditions. The binding parameters and binding mode between flavonoids and catalase were determined, and the results of synchronous fluorescence spectra and CD indicated a conformational change of catalase with addition of flavonoids. The effect of both Cu2+ and vitamin C on the binding constant of flavonoid-catalase was also examined. The experiment data show that the difference of the structure characteristics of quercetin and myricetin has a significant effect on their binding affinity for catalase.

Zhu, Jingfeng; Zhang, Xia; Li, Daojin; Jin, Jing

2007-10-01

48

The Stringent Response Controls Catalases in Pseudomonas aeruginosa and Is Required for Hydrogen Peroxide and Antibiotic Tolerance  

PubMed Central

Pseudomonas aeruginosa, a human opportunistic pathogen, possesses a number of antioxidant defense enzymes under the control of multiple regulatory systems. We recently reported that inactivation of the P. aeruginosa stringent response (SR), a starvation stress response controlled by the alarmone (p)ppGpp, caused impaired antioxidant defenses and antibiotic tolerance. Since catalases are key antioxidant enzymes in P. aeruginosa, we compared the levels of H2O2 susceptibility and catalase activity in P. aeruginosa wild-type and ?relA ?spoT (?SR) mutant cells. We found that the SR was required for optimal catalase activity and mediated H2O2 tolerance during both planktonic and biofilm growth. Upon amino acid starvation, induction of the SR upregulated catalase activity. Full expression of katA and katB also required the SR, and this regulation occurred through both RpoS-independent and RpoS-dependent mechanisms. Furthermore, overexpression of katA was sufficient to restore H2O2 tolerance and to partially rescue the antibiotic tolerance of ?SR cells. All together, these results suggest that the SR regulates catalases and that this is an important mechanism in protecting nutrient-starved and biofilm bacteria from H2O2- and antibiotic-mediated killing.

Khakimova, Malika; Ahlgren, Heather G.; Harrison, Joe J.; English, Ann M.

2013-01-01

49

The stringent response controls catalases in Pseudomonas aeruginosa and is required for hydrogen peroxide and antibiotic tolerance.  

PubMed

Pseudomonas aeruginosa, a human opportunistic pathogen, possesses a number of antioxidant defense enzymes under the control of multiple regulatory systems. We recently reported that inactivation of the P. aeruginosa stringent response (SR), a starvation stress response controlled by the alarmone (p)ppGpp, caused impaired antioxidant defenses and antibiotic tolerance. Since catalases are key antioxidant enzymes in P. aeruginosa, we compared the levels of H2O2 susceptibility and catalase activity in P. aeruginosa wild-type and ?relA ?spoT (?SR) mutant cells. We found that the SR was required for optimal catalase activity and mediated H2O2 tolerance during both planktonic and biofilm growth. Upon amino acid starvation, induction of the SR upregulated catalase activity. Full expression of katA and katB also required the SR, and this regulation occurred through both RpoS-independent and RpoS-dependent mechanisms. Furthermore, overexpression of katA was sufficient to restore H2O2 tolerance and to partially rescue the antibiotic tolerance of ?SR cells. All together, these results suggest that the SR regulates catalases and that this is an important mechanism in protecting nutrient-starved and biofilm bacteria from H2O2- and antibiotic-mediated killing. PMID:23457248

Khakimova, Malika; Ahlgren, Heather G; Harrison, Joe J; English, Ann M; Nguyen, Dao

2013-03-01

50

Loading PEG-Catalase into Filamentous and Spherical Polymer Nanocarriers  

PubMed Central

Purpose Based on a unique phase alignment that occurs during formulation, we postulated that PEG-ylation of the cargo enzyme would enhance its encapsulation within diblock copolymer nanocarriers and thus resistance to proteases. Methods A freeze–thaw modified double emulsion technique was utilized to encapsulate either the catalytically active enzyme catalase (MW ~250 kDa) or PEG-catalase in PEG–PLA polymer nanocarriers (PNC). Spectrophotometer measurement of substrate depletion was utilized to monitor enzyme activity. Isotope labeling of the enzyme was used in conjunction with activity measurements to determine PNC loading efficiency and PNC-enzyme resistance to proteases. This labeling also enabled blood clearance measurements of PNC-loaded and non-loaded enzymes in mice. Results Non-loaded PEG-catalase exhibited longer circulation times than catalase, but was equally susceptible to proteolysis. Modulation of the ratio of relatively hydrophilic to hydrophobic domains in the diblock PEG–PLA copolymer provided either filamentous or spherical PNC loaded with PEG-catalase. For both PNC geometries, encapsulation and resistance to proteases of the resultant PNC-loaded enzyme were more effective for PEG-catalase than catalase. Isotope tracing showed similar blood levels of PNC-loaded and free PEG-catalase in mice. Conclusions PEGylation enhances active catalase loading within PNC and resistance to protease degradation, relative to unloaded PEG-catalase.

Simone, Eric A.; Dziubla, Thomas D.; Arguiri, Evguenia; Vardon, Vanessa; Shuvaev, Vladimir V.; Christofidou-Solomidou, Melpo; Muzykantov, Vladimir R.

2011-01-01

51

Molecular Characterization of a Catalase from Hydra vulgaris  

PubMed Central

Catalase, an antioxidant and hydroperoxidase enzyme protects the cellular environment from harmful effects of hydrogen peroxide by facilitating its degradation to oxygen and water. Molecular information on a cnidarian catalase and/or peroxidase is, however, limited. In this work an apparent full length cDNA sequence coding for a catalase (HvCatalase) was isolated from Hydra vulgaris using 3’- and 5’- (RLM) RACE approaches. The 1859 bp HvCatalase cDNA included an open reading frame of 1518 bp encoding a putative protein of 505 amino acids with a predicted molecular mass of 57.44 kDa. The deduced amino acid sequence of HvCatalase contained several highly conserved motifs including the heme-ligand signature sequence RLFSYGDTH and the active site signature FXRERIPERVVHAKGXGA. A comparative analysis showed the presence of conserved catalytic amino acids [His(71), Asn(145), and Tyr(354)] in HvCatalase as well. Homology modeling indicated the presence of the conserved features of mammalian catalase fold. Hydrae exposed to thermal, starvation, metal and oxidative stress responded by regulating its catalase mRNA transcription. These results indicated that the HvCatalase gene is involved in the cellular stress response and (anti)oxidative processes triggered by stressor and contaminant exposure.

Dash, Bhagirathi; Phillips, Timothy D.

2012-01-01

52

Activity of magnetite-immobilized catalase in hydrogen peroxide decomposition  

Microsoft Academic Search

The present work analyzes the activity in decomposition of H2O2 using magnetite-immobilized catalase. The support of catalase is a glutaraldehyde-treated magnetite (Fe3O4). The data obtained in the H2O2 decomposition are analyzed. The fitting of the initial rate of the H2O2 decomposition versus hydrogen peroxide concentration data is discussed using a specific program for enzyme kinetics modeling (Leonora). The free catalase

F. Horst; E. H. Rueda; M. L. Ferreira

2006-01-01

53

Regulation of catalase enzyme activity by cell signaling molecules  

Microsoft Academic Search

Mitogenic cell proliferation requires a rapid and transient H2O2 generation, which is blocked by catalase or PKA activators. Previously, we observed that anemic HIV(+) individuals expressed acidic pIs of catalase in RBC with significantly high activities [Mol Cell Biochem 165: 77–81, 1996]. These findings led us to hypothesize that cell signaling molecules regulate catalase to control cell mitogenesis. To test

Sumio Yano; Noriko Yano

2002-01-01

54

Immobilization of catalase into chemically crosslinked chitosan beads  

Microsoft Academic Search

Bovine liver catalase was immobilized into chitosan beads prepared in crosslinking solution. Various characteristics of immobilized catalase such as the pH–activity curve, the temperature–activity curve, thermal stability, operational stability, and storage stability were evaluated. Among them the pH optimum and temperature optimum of free and immobilized catalase were found to be pH 7.0 and 35°C. The Km value of immobilized

?enay Akku? Çetinus; H. Nursevin Öztop

2003-01-01

55

Catalytic properties of three catalases from Kohlrabi (Brassica oleracea gongylodes)  

Microsoft Academic Search

Catalase (EC 1.11.1.6) was extracted from kohlrabi bulbs (Brassica oleracea gongylodes) with 0.05 M phosphate buffer, pH 7.0. On the basis of kinetic studies and activity stain for catalase, only three isoenzymes of catalases were detected in kohlrabi bulbs extract with pH optima at 4.5, 6.5 and 10. Highest catalytic efficiency (Vmax\\/Km) value was found for isoenzyme active at pH

Hossein Tayefi-Nasrabadi

2008-01-01

56

Three-dimensional structure of the enzyme catalase  

Microsoft Academic Search

Catalase (H2O2 : H2O2-oxidoreductase, EC 1.11.1.6) is an enzyme that catalyses decomposition of hydrogen peroxide to oxygen and water, and is present in all aerobic cells. All catalases studied so far are tetrameric, each subunit (molecular weight ~60,000) being formed by a single polypeptide chain with haemin as a prosthetic group1,2. Catalase is one of the most efficient enzymes known,

B. K. Vainshtein; W. R. Melik-Adamyan; V. V. Barynin; A. A. Vagin; A. I. Grebenko

1981-01-01

57

Inhibition of catalase activity in vitro by diesel exhaust particles  

SciTech Connect

The effect of diesel exhaust particles (DEP) on the activity of catalase, an intracellular anti-oxidant, was investigated because H{sub 2}O{sub 2} is a cytotoxic oxidant, and catalase released from alveolar cells is an important antioxidant in the epithelial lining fluid in the lung. DEP inhibited the activity of bovine liver catalase dose-dependently, to 25-30% of its original value. The inhibition of catalase by DEP was observed only in the presence of anions such as Cl{sup {minus}}, Br{sup {minus}}, or thiocyanate. Other anions, such as CH{sub 3}COO{sup {minus}} or SO{sub 4}{sup {minus}}, and cations such as K{sup +}, Na{sup +}, Mg{sup 2+}, or Fe{sup 2+}, did not affect the activity of catalase, even in the presence of DEP extract. Catalase from guinea pig alveolar cells and catalase from red blood cells were also inhibited by DEP extracts, as was catalase from bovine liver. These results suggest that DEP taken up in the lung and located on alveolar spaces might cause cell injury by inhibiting the activity of catalase in epithelial lining fluid, enhancing the toxicity of H{sub 2}O{sub 2} generated from cells in addition to that of O{sub 2}{sup {minus}} generated by the chemical reaction of DEP with oxygen. 10 refs., 6 figs.

Mori, Yoki; Murakami, Sumika; Sagae, Toshiyuki [Health Sciences Univ. of Hokkaido (Japan)] [and others

1996-02-09

58

Catalase-positive microbial detection by using different ultrasonic parameters  

NASA Astrophysics Data System (ADS)

A method for rapid detection of catalase enzyme activity using ultrasonic parameters is presented in this work. It is based on the detection of the hydrolysis of hydrogen peroxide molecule into water and oxygen induced by the enzyme catalase. A special medium was made to amplify changes produced by catalase enzyme during the hydrolysis process. Enzymatic process can be monitored by means of ultrasonic parameters such as wave amplitude, time of flight (TOF), and backscattering measurements which are sensitive to oxygen bubble production. It is shown that catalase activity of the order of 10-3unit/ml can be detected using different ultrasonic parameters. The sensitivity provided by them is discussed.

Shukla, S. K.; Durán, C.; Elvira, L.

2012-12-01

59

Catalases are NAD(P)H-dependent tellurite reductases.  

PubMed

Reactive oxygen species damage intracellular targets and are implicated in cancer, genetic disease, mutagenesis, and aging. Catalases are among the key enzymatic defenses against one of the most physiologically abundant reactive oxygen species, hydrogen peroxide. The well-studied, heme-dependent catalases accelerate the rate of the dismutation of peroxide to molecular oxygen and water with near kinetic perfection. Many catalases also bind the cofactors NADPH and NADH tenaciously, but, surprisingly, NAD(P)H is not required for their dismutase activity. Although NAD(P)H protects bovine catalase against oxidative damage by its peroxide substrate, the catalytic role of the nicotinamide cofactor in the function of this enzyme has remained a biochemical mystery to date. Anions formed by heavy metal oxides are among the most highly reactive, natural oxidizing agents. Here, we show that a natural isolate of Staphylococcus epidermidis resistant to tellurite detoxifies this anion thanks to a novel activity of its catalase, and that a subset of both bacterial and mammalian catalases carry out the NAD(P)H-dependent reduction of soluble tellurite ion (TeO(3)(2-)) to the less toxic, insoluble metal, tellurium (Te(o)), in vitro. An Escherichia coli mutant defective in the KatG catalase/peroxidase is sensitive to tellurite, and expression of the S. epidermidis catalase gene in a heterologous E. coli host confers increased resistance to tellurite as well as to hydrogen peroxide in vivo, arguing that S. epidermidis catalase provides a physiological line of defense against both of these strong oxidizing agents. Kinetic studies reveal that bovine catalase reduces tellurite with a low Michaelis-Menten constant, a result suggesting that tellurite is among the natural substrates of this enzyme. The reduction of tellurite by bovine catalase occurs at the expense of producing the highly reactive superoxide radical. PMID:17183702

Calderón, Iván L; Arenas, Felipe A; Pérez, José Manuel; Fuentes, Derie E; Araya, Manuel A; Saavedra, Claudia P; Tantaleán, Juan C; Pichuantes, Sergio E; Youderian, Philip A; Vásquez, Claudio C

2006-12-20

60

Low Catalase Levels in the Epidermis of Patients with Vitiligo  

Microsoft Academic Search

Suction blister roofs taken from the involve and uninvolved epidermis of patients with vitiligo showed a consistent reduction in level of catalase compared to normal healthy controls of matched photo-skin types (Fitzpatrick classification). A decrease in catalase activity is expected to increase the concentration of hydrogen peroxide in the epidermis of these patients. Hydrogen peroxide function as a reversible inhibitor

Karin U. Schallreuter; John M. Wood; Jürgen Berger

1991-01-01

61

Cloning of a catalase gene from Bdellovibrion bacteriovorus  

Microsoft Academic Search

Bdellovibrio has one of the highest energy efficiencies known. Attack phase Bdellovibrio cells are extremely motile, and die swiftly under anaeobic or microaerophilic conditions. Many Bdellovibrio species are know to swiftly possess catalase and super oxcide dismutase (oxygen detoxifying) enzymes. By knocking out the catalase gene in Bdellovibrio, we believe that the bacterium will not be able to survive the

Min Kim

2002-01-01

62

Characterization of a Heme-Dependent Catalase from Methanobrevibacter arboriphilus  

Microsoft Academic Search

Recently it was reported that methanogens of the genus Methanobrevibacter exhibit catalase activity. This was surprising, since Methanobrevibacter species belong to the order Methanobacteriales, which are known not to contain cytochromes and to lack the ability to synthesize heme. We report here that Methanobrevibacter arboriphilus strains AZ and DH1 contained catalase activity only when the growth medium was supplemented with

SEIGO SHIMA; MELANIE SORDEL-KLIPPERT; ANDREI BRIOUKHANOV; ALEXANDER NETRUSOV; DIETMAR LINDER; RUDOLF K. THAUER

2001-01-01

63

Deactivation of Immobilized Beef Liver Catalase by Hydrogen Peroxide.  

National Technical Information Service (NTIS)

Immobilized beef liver catalase has been used in a flow reactor to decompose hydrogen peroxide; at the same time the catalase is inactivated by its substrate. A model has been developed which predicts this rate of decomposition of peroxide and inactivatio...

R. E. Altomare J. Kohler P. F. Greenfield J. R. Kittrell

1974-01-01

64

PARADOXICAL POTENTIATION OF RADIOINACTIVATION OF SULFHYDRYL ENZYMES BY CATALASE  

Microsoft Academic Search

Catalase was previously shown to inhibit the radiationinduced ; suppression of glycolysis in ascites tumor cells and the suppression of ; methemoglobin formation in irradiated erythrocytes. However, in experiments with ; liver alcohol dehydrogenase, catalase showed in opposite effect, i.e., it ; promoted radioinactivation. Addition of 10 mu g liver catalise per ml to a ; solution of 80 mu

H. Aebi; A. Temperli

1961-01-01

65

IS CATALASE ACTIVITY ASSOCIATED WITH MAIZE RESISTANCE TO ASPERGILLUS FLAVUS  

Technology Transfer Automated Retrieval System (TEKTRAN)

Catalase activity was measured in various cob tissues during maize ear development because of its role in maintaining reactive oxygen homeostasis during biotic and abiotic stress. Catalase activity was determined in immature and mature embryos, pericarp, and rachis tissues of maize lines that are re...

66

Interaction of nitric oxide with catalase: structural and kinetic analysis.  

PubMed

We present the structures of bovine catalase in its native form and complexed with ammonia and nitric oxide, obtained by X-ray crystallography. Using the NO generator 1-(N,N-diethylamino)diazen-1-ium-1,2-diolate, we were able to generate sufficiently high NO concentrations within the catalase crystals that substantial occupation was observed despite a high dissociation rate. Nitric oxide seems to be slightly bent from the heme normal that may indicate some iron(II) character in the formally ferric catalase. Microspectrophotometric investigations inline with the synchrotron X-ray beam reveal photoreduction of the central heme iron. In the cases of the native and ammonia-complexed catalase, reduction is accompanied by a relaxation phase. This is likely not the case for the catalase NO complex. The kinetics of binding of NO to catalase were investigated using NO photolyzed from N,N'-bis(carboxymethyl)-N,N'-dinitroso-p-phenylenediamine using an assay that combines catalase with myoglobin binding kinetics. The off rate is 1.5 s(-1). Implications for catalase function are discussed. PMID:21524057

Purwar, Namrta; McGarry, Jennifer M; Kostera, Joshua; Pacheco, A Andrew; Schmidt, Marius

2011-05-06

67

Catalase (antioxidant enzyme) activity in streptozotocin-induced diabetic rats  

Microsoft Academic Search

Background: High concentration and\\/or inadequate removal of reactive oxygen species may result in oxidative stress that may cause severe metabolic malfunction. An imbalance in antioxidant enzymes has been related to specific pathologies such as diabetic complications. Catalase catalyzes the reduction of hydroperoxides, thereby protecting mammalian cells against oxidative damage. In addition, catalase is active in neutralizing reactive oxygen species and

Durdi Qujeq; Timur Rezvani

68

Peroxidatic degradation of azide by catalase and irreversible enzyme inactivation  

Microsoft Academic Search

A study of the azide reaction with bovine liver catalase in presence of hydrogen peroxide has been performed, using conventional UV-visible spectrometry and activity measurements. Compound III and NO-ferrocatalase were the forms of the enzyme observed in air and under nitrogen, respectively. A reaction scheme for peroxidatic degradation of azide by catalase is proposed. Accordingly, accumulation of Compound III is

Olivier M. Lardinois; Paul G. Rouxhet

1996-01-01

69

Purification and Characterization of a Catalase from the Facultatively Psychrophilic Bacterium Vibrio rumoiensis S-1T Exhibiting High Catalase Activity  

PubMed Central

Catalase from the facultatively psychrophilic bacterium Vibrio rumoiensis S-1T, which was isolated from an environment exposed to H2O2 and exhibited high catalase activity, was purified and characterized, and its localization in the cell was determined. Its molecular mass was 230 kDa, and the molecule consisted of four identical subunits. The enzyme, which was not apparently reduced by dithionite, showed a Soret peak at 406 nm in a resting state. The catalytic activity was 527,500 U · mg of protein?1 under standard reaction conditions at 40°C, 1.5 and 4.3 times faster, respectively, than those of the Micrococcus luteus and bovine catalases examined under the same reaction conditions, and showed a broad optimum pH range (pH 6 to 10). The catalase from strain S-1T is located not only in the cytoplasmic space but also in the periplasmic space. There is little difference in the activation energy for the activity between strain S-1T catalase and M. luteus and bovine liver catalases. The thermoinstability of the activity of the former catalase were significantly higher than those of the latter catalases. The thermoinstability suggests that the catalase from strain S-1T should be categorized as a psychrophilic enzyme. Although the catalase from strain S-1T is classified as a mammal type catalase, it exhibits the unique enzymatic properties of high intensity of enzymatic activity and thermoinstability. The results obtained suggest that these unique properties of the enzyme are in accordance with the environmental conditions under which the microorganism lives.

Yumoto, Isao; Ichihashi, Daisen; Iwata, Hideaki; Istokovics, Anita; Ichise, Nobutoshi; Matsuyama, Hidetoshi; Okuyama, Hidetoshi; Kawasaki, Kosei

2000-01-01

70

The effect of various food parameters on the activity and stability of catalase from Aspergillus niger and catalase from bovine liver  

Microsoft Academic Search

The effects of a number of food relevant parameters on catalase activity and stability were studied. The direct responses of different combinations of the parameters ethanol, pH and ionic strength on bovine liver catalase and Aspergillus niger catalase activity were investigated in a full factorial 24 statistically designed experiment. Statistically significant effects (p = 0.001) on both types of catalases

Anne S. Meyer; Lærke H. Pedersen; Anette Isaksen

1997-01-01

71

Immobilization of catalase onto Eupergit C and its characterization  

Microsoft Academic Search

Bovine liver catalase was covalently immobilized onto Eupergit C. Optimum conditions of immobilization: pH, buffer concentration, temperature, coupling time and initial catalase amount per gram of carrier were determined as 7.5, 1.0M, 25°C, 24h and 4.0mg\\/g, respectively. Vmax and Km were determined as 1.4(±0.2)×105U\\/mg protein and 28.6±3.6mM, respectively, for free catalase, and as 3.7(±0.4)×103U\\/mg protein and 95.9±0.6mM, respectively, for immobilized

Özlem Alptekin; S. Seyhan Tükel; Deniz Y?ld?r?m; Dilek Alagöz

2010-01-01

72

Microcalorimetric studies on catalase reaction and inhibition of catalase by cyanide ion  

Microsoft Academic Search

As Chance et al. [1–3] proposed, the decomposition of hydrogen peroxide catalyzed by catalase is an overall first-order reaction. In this paper, we have studied this enzyme-catalyzed reaction with a thermokinetic method. The rate constant and the molar reaction enthalpy of this reaction have been measured. At 310.15K and pH=8.2, kcat=1.75×106lmol?1s?1, ?rHm=88.99kJmol?1. Furthermore, we have studied the competitive inhibition of

Wang Zhiyong; Wang Cunxin; Qu Songsheng

2000-01-01

73

Antioxidative and immunogenic properties of catalase-peroxidase protein in Penicillium marneffei.  

PubMed

Abstract Penicillium marneffei is a significant opportunistic fungal pathogen in Southeast Asia and its ability to survive inside the host macrophages is believed to be important in the establishment of infection. Previously, we isolated a gene encoding a catalase- peroxidase (cpeA) from P. marneffei and showed that the cpeA transcript is specifically upregulated during yeast phase growth at 37°C. In this study, the cpeA transcript was found to be induced during the mycelium to yeast phase transition and during stress conditions induced by hydrogen peroxide treatment. Null mutation of cpeA reduced the fungal tolerance to hydrogen peroxide but not to heat stress. These results indicated that the CpeA plays a crucial role in this fungus' oxidative stress response. Western blot analysis demonstrated that the CpeA induced antibody production in P. marneffei-infected patients, including highly exposed-healthy people. This is the first report that the catalase-peroxidase possesses an immunogenic property in fungi. PMID:23859079

Pongpom, Monsicha; Sawatdeechaikul, Pritsana; Kummasook, Aksarakorn; Khanthawong, Sophit; Vanittanakom, Nongnuch

2013-07-16

74

The catalase activity of diiron adenine deaminase.  

PubMed

Adenine deaminase (ADE) from the amidohydrolase superfamily (AHS) of enzymes catalyzes the conversion of adenine to hypoxanthine and ammonia. Enzyme isolated from Escherichia coli was largely inactive toward the deamination of adenine. Molecular weight determinations by mass spectrometry provided evidence that multiple histidine and methionine residues were oxygenated. When iron was sequestered with a metal chelator and the growth medium supplemented with Mn(2+) before induction, the post-translational modifications disappeared. Enzyme expressed and purified under these conditions was substantially more active for adenine deamination. Apo-enzyme was prepared and reconstituted with two equivalents of FeSO(4). Inductively coupled plasma mass spectrometry and Mössbauer spectroscopy demonstrated that this protein contained two high-spin ferrous ions per monomer of ADE. In addition to the adenine deaminase activity, [Fe(II) /Fe(II) ]-ADE catalyzed the conversion of H(2)O(2) to O(2) and H(2)O. The values of k(cat) and k(cat)/K(m) for the catalase activity are 200 s(-1) and 2.4 × 10(4) M(-1) s(-1), respectively. [Fe(II)/Fe(II)]-ADE underwent more than 100 turnovers with H(2)O(2) before the enzyme was inactivated due to oxygenation of histidine residues critical for metal binding. The iron in the inactive enzyme was high-spin ferric with g(ave) = 4.3 EPR signal and no evidence of anti-ferromagnetic spin-coupling. A model is proposed for the disproportionation of H(2)O(2) by [Fe(II)/Fe(II)]-ADE that involves the cycling of the binuclear metal center between the di-ferric and di-ferrous oxidation states. Oxygenation of active site residues occurs via release of hydroxyl radicals. These findings represent the first report of redox reaction catalysis by any member of the AHS. PMID:21998098

Kamat, Siddhesh S; Holmes-Hampton, Gregory P; Bagaria, Ashima; Kumaran, Desigan; Tichy, Shane E; Gheyi, Tarun; Zheng, Xiaojing; Bain, Kevin; Groshong, Chris; Emtage, Spencer; Sauder, J Michael; Burley, Stephen K; Swaminathan, Subramanyam; Lindahl, Paul A; Raushel, Frank M

2011-11-09

75

Immobilization of Catalase and Glucose Oxidase on Inorganic Supports.  

National Technical Information Service (NTIS)

Glucose oxidase and catalase have been individually immobilized on several inorganic supports using the glutaraldehyde procedure. Enzymic activity depended on the support type and the particle size of the support used in the assay. Interestingly, the leas...

P. E. Markey P. F. Greenfield J. R. Kittrell

1974-01-01

76

On the multiplicity of the enzyme catalase in mammalian liver  

Microsoft Academic Search

The literature on the complex multiplicity of mammlian catalase and the nature of the epigenetic modifications undergone by this enzyme has been reviewed, along with relevant comment on the subcellular localization and biological role of the enzyme.

Colin Masters; Michael Pegg; Denis Crane

1986-01-01

77

Inactivation of Immobilized Fungal Catalase by Hydrogen Peroxide.  

National Technical Information Service (NTIS)

The deactivation of immobilized fungal catalase derived from Aspergillus by peroxide was studied in a continuous, tubular packed bed reactor. Effects of temperature peroxide concentration, and residence time were observed. Comparison with immobilized beef...

R. E. Altomare P. F. Greenfield J. R. Kittrell

1974-01-01

78

A Laboratory Experiment of the Purification of Catalase.  

ERIC Educational Resources Information Center

|Describes a simple method for purifying catalase for the study of proteins. Procedures are systematically and diagramatically presented. Also identifies polyacrylamide gel electrophoresis, kinetic studies, and apparent molecular weight determination as possible techniques to be used in studying proteins. (ML)|

Busquets, Montserrat; Franco, Rafael

1986-01-01

79

Comparative immunological study of catalases in the genus Micrococcus  

Microsoft Academic Search

Double immunodiffusion tests were performed with crude extracts from various Micrococcus species and antisera against catalase of Micrococcus luteus CCM 169. Cell-free extracts of M. lylae ATCC 27566 exhibited good cross-reaction. Cell-free extracts or catalase enriched preparations of M. varians reacted very weakly and no reaction has been found with preparations of M. kristinae, M. nishinomiyaensis, M. roseus and M.

Manfred Rupprecht; Karl-Heinz Schleifer

1977-01-01

80

Simultaneous production of glucose oxidase and catalase by Alternaria alternata  

Microsoft Academic Search

A number of factors affecting simultaneous production of cell-bound glucose oxidase and catalase by the fungus Alternaria alternata have been investigated. Consecutive optimization of the type and concentration of nitrogen and carbon source, the initial pH and growth temperature resulted in a simultaneous increase in glucose oxidase and catalase by 780% and 68% respectively. Two second-order equations, describing the combined

Konstantina-Anna Caridis; Paul Christakopoulos; Basil J. Macris

1991-01-01

81

Purification and characterization of catalase from goat ( Capra capra ) lung  

Microsoft Academic Search

Catalase plays a major role in the protection of tissues from toxic effects of H2O2 and partially reduced oxygen species. In the present study catalase was extracted and purified 330-fold from goat lung by acetone fractionation and successive chromatographies on DEAE-cellulose, Sephadex G-200, Blue Sepharose CL-6B and Ultrogel AcA-34. The purified enzyme was almost homogeneous as judged by polyacrylamide gel

Uttam Chatterjee; G. G. Sanwal

1993-01-01

82

SOD and catalase inactivation by singlet oxygen and peroxyl radicals  

Microsoft Academic Search

Both superoxide dismutase and catalase are readily deactivated by singlet oxygen and by the radicals produced in the pyrolysis of 2,2?-azo-bis-(2-amidinpropano) under aerobic conditions. The rate constant for the loss of enzymatic activity induced by singlet oxygen are 3.9 × 107 and 2.5 × 107 M?1 sec?1 for SOD and catalase, respectively. The similarity between these values implies that in

J. A. Escobar; M. A. Rubio; E. A. Lissi

1996-01-01

83

Differential Expression of Catalase Genes in Nicotiana plumbaginifolia (L.)  

Microsoft Academic Search

We have analyzed the expression of three catalase (Cat; EC 1.11.1.6) genes from Nicotiana plumbaginifolia by means of RNA blot and in situ hybridizations. Our data demonstrate that the expression of each catalase is associated with a particular H_2O_2-producing process. Cat1 appears to be specifically involved in the scavenging of photorespiratory H_2O_2 and is under control of a circadian rhythm,

Hilde Willekens; Christian Langebartels; Christine Tire; Marc van Montagu; Dirk Inze; Wim van Camp

1994-01-01

84

Cytochemical discrimination between catalases and peroxidases using diaminobenzidine  

Microsoft Academic Search

The influence on diaminobenzidine staining of four variables: prefixation in aldehyde, temperature and pH of incubation, and H2O2 concentration, was investigated in catalase-, as well as in peroxydase-containing material. Catalase from five different sources and five types of peroxidase were examine. It is conclude: (a) when cells are incubated without prior fixation, in a DAB medium at room temperature and

Frank Roels; Eddie Wisse; Betty Prest; Jannes Meulen

1975-01-01

85

Characterization of the oxidase activity in mammalian catalase.  

PubMed

Catalase is a highly conserved heme-containing antioxidant enzyme known for its ability to degrade hydrogen peroxide into water and oxygen. In low concentrations of hydrogen peroxide, the enzyme also exhibits peroxidase activity. We report that mammalian catalase also possesses oxidase activity. This activity, which is detected in purified catalases, cell lysates, and intact cells, requires oxygen and utilizes electron donor substrates in the absence of hydrogen peroxide or any added cofactors. Using purified bovine catalase and 10-acetyl-3,7-dihydroxyphenoxazine as the substrate, the oxidase activity was found to be temperature-dependent and displays a pH optimum of 7-9. The Km for the substrate is 2.4 x 10(-4) m, and Vmax is 4.7 x 10(-5) m/s. Endogenous substrates, including the tryptophan precursor indole, the neurotransmitter precursor beta-phenylethylamine, and a variety of peroxidase and laccase substrates, as well as carcinogenic benzidines, were found to be oxidized by catalase or to inhibit this activity. Several dietary plant micronutrients that inhibit carcinogenesis, including indole-3-carbinol, indole-3-carboxaldehyde, ferulic acid, vanillic acid, and epigallocatechin-3-gallate, were effective inhibitors of the activity of catalase oxidase. Difference spectroscopy revealed that catalase oxidase/substrate interactions involve the heme-iron; the resulting spectra show time-dependent decreases in the ferric heme of the enzyme with corresponding increases in the formation of an oxyferryl intermediate, potentially reflecting a compound II-like intermediate. These data suggest a mechanism of oxidase activity involving the formation of an oxygen-bound, substrate-facilitated reductive intermediate. Our results describe a novel function for catalase potentially important in metabolism of endogenous substrates and in the action of carcinogens and chemopreventative agents. PMID:16079130

Vetrano, Anna M; Heck, Diane E; Mariano, Thomas M; Mishin, Vladimir; Laskin, Debra L; Laskin, Jeffrey D

2005-08-02

86

Formulation and characterization of catalase in albumin microspheres.  

PubMed

Catalase in albumin microspheres were formulated for intravenous administration to antagonize the effects of over-production of reactive oxygenated species (ROS) such as hydrogen peroxide (H(2)O(2)) in septic shock. The aim was to increase effective half-life of catalase and take advantage of the phagocytic uptake of the encapsulated catalase by the vascular endothelium. Catalase microspheres were prepared by spray-drying. The microspheres were evaluated for particle size, particle shape and surface morphology by scanning electron microscopy (SEM), drug encapsulation efficiency, chemical stability, thermal stability and in vitro drug release characteristics. The microspheres had a mean particle size of 4.7 +/- 2 microm, optimal for phagocytic uptake, as demonstrated by Makino et al. SEM revealed that microspheres were spherical with smooth surface morphology. An encapsulation efficiency of 91.5 +/- 3% was achieved and the encapsulated catalase was chemically and thermally stable. Application of in vitro drug release data to the Higuchi kinetic equation indicated matrix diffusion-controlled catalase release from albumin microspheres. PMID:18821261

Siwale, Rodney C; Oettinger, Carl W; Pai, S Balakrishna; Addo, Richard; Uddin, Nasir; Siddig, Aladin; D'Souza, Martin J

2009-08-01

87

Pseudomonas syringae Catalases Are Collectively Required for Plant Pathogenesis  

PubMed Central

The bacterial pathogen Pseudomonas syringae pv. tomato DC3000 must detoxify plant-produced hydrogen peroxide (H2O2) in order to survive in its host plant. Candidate enzymes for this detoxification include the monofunctional catalases KatB and KatE and the bifunctional catalase-peroxidase KatG of DC3000. This study shows that KatG is the major housekeeping catalase of DC3000 and provides protection against menadione-generated endogenous H2O2. In contrast, KatB rapidly and substantially accumulates in response to exogenous H2O2. Furthermore, KatB and KatG have nonredundant roles in detoxifying exogenous H2O2 and are required for full virulence of DC3000 in Arabidopsis thaliana. Therefore, the nonredundant ability of KatB and KatG to detoxify plant-produced H2O2 is essential for the bacteria to survive in plants. Indeed, a DC3000 catalase triple mutant is severely compromised in its ability to grow in planta, and its growth can be partially rescued by the expression of katB, katE, or katG. Interestingly, our data demonstrate that although KatB and KatG are the major catalases involved in the virulence of DC3000, KatE can also provide some protection in planta. Thus, our results indicate that these catalases are virulence factors for DC3000 and are collectively required for pathogenesis.

Guo, Ming; Block, Anna; Bryan, Crystal D.; Becker, Donald F.

2012-01-01

88

Identification and expression studies of a catalase and a bifunctional catalase-peroxidase in Frankia strain R43  

Microsoft Academic Search

A monofunctional catalase and a bifunctional catalase-peroxidase were revealed by activity staining of non-denaturing PAGE in Frankia strain R43. Both enzymes were shown to be cytoplasmatic, growth regulated and expressed mainly during the stationary growth phase. Nevertheless, low levels of constitutive expression could also be detected during the early stages of growth. Immunoblot analyses using a polyclonal antibody raised against

Fernando Tavares; Lisandro Bernardo; Anita Sellstedt

2003-01-01

89

Purification and Characterization of a Catalase from the Facultatively Psychrophilic Bacterium Vibrio rumoiensis S-1T Exhibiting High Catalase Activity  

Microsoft Academic Search

Catalase from the facultatively psychrophilic bacterium Vibrio rumoiensis S-1 T , which was isolated from an environment exposed to H2O2 and exhibited high catalase activity, was purified and characterized, and its localization in the cell was determined. Its molecular mass was 230 kDa, and the molecule consisted of four identical subunits. The enzyme, which was not apparently reduced by dithionite,

ISAO YUMOTO; DAISEN ICHIHASHI; HIDEAKI IWATA; ANITA ISTOKOVICS; NOBUTOSHI ICHISE; HIDETOSHI MATSUYAMA; HIDETOSHI OKUYAMA; KOSEI KAWASAKI

2000-01-01

90

Embryonic catalase protects against ethanol-initiated DNA oxidation and teratogenesis in acatalasemic and transgenic human catalase-expressing mice.  

PubMed

Reactive oxygen species (ROS) are implicated in fetal alcohol spectrum disorders (FASD) caused by alcohol (ethanol, EtOH). Although catalase detoxifies hydrogen peroxide, embryonic catalase activity is only about 5% of maternal levels. To determine the roles of ROS and embryonic catalase in FASD, pregnant mice with enhanced (expressing human catalase, hCat) or deficient (acatalasemic, aCat) catalase activity, or their respective wild-type (WT) controls, were treated ip on gestational day 9 with 4 or 6g/kg EtOH or its saline vehicle, and embryos and fetuses were, respectively, evaluated for oxidatively damaged DNA and structural anomalies. Untreated hCat and aCat dams had, respectively, more and less offspring than their WT controls. hCat progenies were protected from all EtOH fetal anomalies at the low dose (p < .01) and from reduced head diameter and resorptions at the high dose (p < .001). Conversely, aCat progenies were more sensitive to dose-dependent EtOH fetal anomalies (p < .001) and exhibited a 50% increase in maternal lethality (p < .05) at the high dose. Maternal pretreatment of aCat mice with polyethylene glycol-conjugated catalase (PEG-Cat) reduced EtOH fetal anomalies (p < .001). EtOH-initiated embryonic DNA oxidation was reduced in hCat and WT mice pretreated with PEG-Cat and enhanced in aCat mice. Plasma concentrations of EtOH in catalase-altered mice were similar to controls, precluding a pharmacokinetic basis for altered EtOH teratogenesis. Endogenous embryonic catalase, despite its low level, is an important embryoprotective enzyme for EtOH teratogenesis and a likely determinant of individual risk. PMID:23733920

Miller, Lutfiya; Shapiro, Aaron M; Wells, Peter G

2013-06-02

91

Conversion of the synthetic catalase mimic precursor TAA-1 into the active catalase mimic in isolated hepatocytes.  

PubMed

In previous studies we reported on the catalase-like activity and antioxidative properties of a non-heme Fe(III)-tetraaza[14]annulene complex, 5,4-didehydro-5,9,14,18-tetraaza-di(2,2-dimethyl-[5,6]benzo[1,3]dioxolo)[a,h]cyclotetradecene--Fe(III) chloride (TAA-1/Fe). We proposed that intracellular application of the parent, iron-free tetraaza[14]annulene ligand, TAA-1, as precursor would allow antioxidative defense along two lines, i.e. by chelation of potentially toxic cellular iron ions and, subsequently, by catalase-mimic activity. We here set out to establish whether the active catalase mimic is indeed formed intracellularly when cells are loaded with the ligand. When isolated rat hepatocytes were preloaded with TAA-1, they were protected against iron-induced cell injury and oxidative stress elicited by exposure to the membrane-permeable iron complex Fe(III)/8-hydroxyquinoline. After lysis of the cells, followed by ultrafiltration to remove endogenous catalase, the lysate exhibited catalase-like activity, while lysates of control cells not treated with TAA-1 showed no catalase-like activity. By comparison with authentic TAA-1/Fe, an intracellular formation of 2.0 +/- 0.3 microm of the active catalase mimic in native hepatocytes exposed to TAA-1 and of 6.5 +/- 1.0 microm in hepatocytes exposed to both TAA-1 and iron ions was estimated. The intracellular formation of the active catalase mimic thus renders TAA-1 an attractive compound for protection against iron- and/or hydrogen peroxide-dependent cell injuries. PMID:19366358

Rauen, Ursula; Kettler-Thiel, Thorsten; de Groot, Herbert; Korth, Hans-Gert; Sustmann, Reiner

2009-05-01

92

The catalase activity of diiron adenine deaminase  

SciTech Connect

Adenine deaminase (ADE) from the amidohydrolase superfamily (AHS) of enzymes catalyzes the conversion of adenine to hypoxanthine and ammonia. Enzyme isolated from Escherichia coli was largely inactive toward the deamination of adenine. Molecular weight determinations by mass spectrometry provided evidence that multiple histidine and methionine residues were oxygenated. When iron was sequestered with a metal chelator and the growth medium supplemented with Mn{sup 2+} before induction, the post-translational modifications disappeared. Enzyme expressed and purified under these conditions was substantially more active for adenine deamination. Apo-enzyme was prepared and reconstituted with two equivalents of FeSO{sub 4}. Inductively coupled plasma mass spectrometry and Moessbauer spectroscopy demonstrated that this protein contained two high-spin ferrous ions per monomer of ADE. In addition to the adenine deaminase activity, [Fe{sup II}/Fe{sup II}]-ADE catalyzed the conversion of H{sub 2}O{sub 2} to O{sub 2} and H{sub 2}O. The values of k{sub cat} and k{sub cat}/K{sub m} for the catalase activity are 200 s{sup -1} and 2.4 x 10{sup 4} M{sup -1} s{sup -1}, respectively. [Fe{sup II}/Fe{sup II}]-ADE underwent more than 100 turnovers with H{sub 2}O{sub 2} before the enzyme was inactivated due to oxygenation of histidine residues critical for metal binding. The iron in the inactive enzyme was high-spin ferric with g{sub ave} = 4.3 EPR signal and no evidence of anti-ferromagnetic spin-coupling. A model is proposed for the disproportionation of H{sub 2}O{sub 2} by [Fe{sup II}/Fe{sup II}]-ADE that involves the cycling of the binuclear metal center between the di-ferric and di-ferrous oxidation states. Oxygenation of active site residues occurs via release of hydroxyl radicals. These findings represent the first report of redox reaction catalysis by any member of the AHS.

Kamat S. S.; Swaminathan S.; Holmes-Hampton, G. P.; Bagaria, A.; Kumaran, D.; Tichy, S. E.; Gheyi, T.; Zheng, X.; Bain, K.; Groshong, C.; Emtage, S.; Sauder, J. M.; Burley, S. K.; Lindahl, P. A.; Raushel, F. M.

2011-12-01

93

Embryoprotective role of endogenous catalase in acatalasemic and human catalase-expressing mouse embryos exposed in culture to developmental and phenytoin-enhanced oxidative stress.  

PubMed

Reactive oxygen species (ROS) are implicated in spontaneous and xenobiotic-enhanced embryopathies, and protein therapy with exogenous catalase suggests an embryoprotective role, although embryonic catalase activity is only about 5% of adult activity. Using mutant catalase-deficient (acatalasemic, aCat) mice and transgenic mice expressing human catalase (hCat, enhanced catalase activity) compared with a confirmed outbred CD-1 mouse model, we investigated the protective importance of constitutive embryonic catalase against endogenous ROS and the ROS-initiating teratogen phenytoin in embryo culture. Vehicle-exposed aCat and hCat embryos, respectively, exhibited reduced and enhanced catalase activity compared with wild-type (WT) controls, with conversely enhanced and reduced spontaneous embryopathies. Phenytoin was embryopathic in all strains without altering catalase activity but less so in the WT embryos for the aCat and hCat strains, which exhibited about half the catalase activity of CD-1 embryos. Phenytoin, respectively, enhanced and reduced embryopathies in aCat and hCat embryos. Among aCat embryos exposed to phenytoin, embryopathies increased with decreasing catalase activity and were completely blocked by addition of exogenous catalase, which increased embryonic catalase activity to WT levels. These results provide the first direct evidence that (1) the low level of constitutive embryonic catalase protects the conceptus from developmental and xenobiotic-enhanced oxidative stress and (2) embryonic variations in activity of this enzyme affect development. PMID:21252394

Abramov, Julia P; Wells, Peter G

2011-01-20

94

Central reinforcing effects of ethanol are blocked by catalase inhibition.  

PubMed

Recent studies have systematically indicated that newborn rats are highly sensitive to ethanol's positive reinforcing effects. Central administrations of ethanol (25-200mg %) associated with an olfactory conditioned stimulus (CS) promote subsequent conditioned approach to the CS as evaluated through the newborn's response to a surrogate nipple scented with the CS. It has been shown that ethanol's first metabolite, acetaldehyde, exerts significant reinforcing effects in the central nervous system. A significant amount of acetaldehyde is derived from ethanol metabolism via the catalase system. In newborn rats, catalase levels are particularly high in several brain structures. The present study tested the effect of catalase inhibition on central ethanol reinforcement. In the first experiment, pups experienced lemon odor either paired or unpaired with intracisternal (IC) administrations of 100mg% ethanol. Half of the animals corresponding to each learning condition were pretreated with IC administrations of either physiological saline or a catalase inhibitor (sodium-azide). Catalase inhibition completely suppressed ethanol reinforcement in paired groups without affecting responsiveness to the CS during conditioning or responding by unpaired control groups. A second experiment tested whether these effects were specific to ethanol reinforcement or due instead to general impairment in learning and expression capabilities. Central administration of an endogenous kappa opioid receptor agonist (dynorphin A-13) was used as an alternative source of reinforcement. Inhibition of the catalase system had no effect on the reinforcing properties of dynorphin. The present results support the hypothesis that ethanol metabolism regulated by the catalase system plays a critical role in determination of ethanol reinforcement in newborn rats. PMID:17980789

Nizhnikov, Michael E; Molina, Juan C; Spear, Norman E

2007-11-01

95

Multiple periplasmic catalases in phytopathogenic strains of Pseudomonas syringae.  

PubMed Central

Phytopathogenic strains of Pseudomonas syringae are exposed to plant-produced, detrimental levels of hydrogen peroxide during invasion and colonization of host plant tissue. When P. syringae strains were investigated for their capacity to resist H2O2, they were found to contain 10- to 100-fold-higher levels of total catalase activity than selected strains belonging to nonpathogenic related taxa (Pseudomonas fluorescens and Pseudomonas putida) or Escherichia coli. Multiple catalase activities were identified in both periplasmic and cytoplasmic fluids of exponential- and stationary-phase P. syringae cells. Two of these activities were unique to the periplasm of P. syringae pv. glycinea. During the stationary growth phase, the specific activity of cytoplasmic catalases increased four- to eightfold. The specific activities of catalases in both fluids from exponential-phase cells increased in response to treatment with 0.25 to 10 mM H2O2 but decreased when higher H2O2 concentrations were used. In stationary-growth phase cultures, the specific activities of cytoplasmic catalases increased remarkably after treatment with 0.25 to 50 mM H2O2. The growth of P. syringae into stationary phase and H2O2 treatment did not induce synthesis of additional catalase isozymes. Only the stationary-phase cultures of all of the P. syringae strains which we tested were capable of surviving high H2O2 stress at concentrations up to 50 mM. Our results are consistent with the involvement of multiple catalase isozymes in the reduction of oxidative stress during plant pathogenesis by these bacteria.

Klotz, M G; Hutcheson, S W

1992-01-01

96

Purification and biosynthesis of cottonseed (Gossypium hirsutum L.) catalase.  

PubMed Central

As part of our research on peroxisome biogenesis, catalase was purified from cotyledons of dark-grown cotton (Gossypium hirsutum L.) seedlings and monospecific antibodies were raised in rabbits. Purified catalase appeared as three distinct electrophoretic forms in non-denaturing gels and as a single protein band (with a subunit Mr of 57,000) on silver-stained SDS/polyacrylamide gels. Western blots of crude extracts and isolated peroxisomes from cotton revealed one immunoreactive polypeptide with the same Mr (57,000) as the purified enzyme, indicating that catalase did not undergo any detectable change in Mr during purification. Synthesis in vitro, directed by polyadenylated RNA isolated from either maturing seeds or cotyledons of dark-grown cotton seedlings, revealed a predominant immunoreactive translation product with a subunit Mr of 57,000 and an additional minor immunoreactive product with a subunit Mr of 64000. Labelling studies in vivo revealed newly synthesized monomers of both the 64000- and 57,000-Mr proteins present in the cytosol and incorporation of both proteins into the peroxisome without proteolytic processing. Within the peroxisome, the 57,000-Mr catalase was found as an 11S tetramer; whereas the 64,000-Mr protein was found as a relatively long-lived 20S aggregate (native Mr approx. 600,000-800,000). The results strongly indicate that the 64,000-Mr protein (catalase?) is not a precursor to the 57,000-Mr catalase and that cotton catalase is translated on cytosolic ribosomes without a cleavable transit or signal sequence. Images Fig. 1. Fig. 3. Fig. 4. Fig. 5. Fig. 6. Fig. 7. Fig. 8. Fig. 9. Fig. 10.

Kunce, C M; Trelease, R N; Turley, R B

1988-01-01

97

Synthesis and characterization of thermo-responsive poly( N-isopropylacrylamide)-bovine liver catalase bioconjugate  

Microsoft Academic Search

Thermo-responsive poly(N-isopropylacryalamide) (PNiPAAm) and polyacrylamide (PAAm)-bovine liver catalase bioconjugates were synthesized via copolymerization reaction between acylated catalase and polymeric monomers. The PNiPAAm bioconjugate behaved as a temperature responsive biocatalyst and did show temperature dependent phase transition whereas, polyacrylamide bioconjugate and unmodified catalase did not show such property. The synthesized PNiPAAm-catalase and PAAm-catalase bioconjugates have weight average molecular weight (Mw) of

Akhilesh Kumar Shakya; Poonam Sharma; Ashok Kumar

2010-01-01

98

The kinetic properties producing the perfunctory pH profiles of catalase-peroxidases  

Microsoft Academic Search

Many structure–function relationship studies performed on the catalase-peroxidase enzymes are based on limited kinetic data. To provide a more substantive understanding of catalase-peroxidase function, we undertook a more exhaustive evaluation of catalase-peroxidase catalysis as a function of pH. Kinetic parameters across a broad pH range for the catalase and peroxidase activities of E. coli catalase peroxidase (KatG) were obtained, including

Robert L. Moore; Luke J. Powell; Douglas C. Goodwin

2008-01-01

99

Pecam-directed immunotargeting of catalase: specific, rapid and transient protection against hydrogen peroxide  

Microsoft Academic Search

Vascular immunotargeting to Platelet-Endothelial Cell Adhesion Molecule-1 (PECAM) facilitates drug delivery to endothelium. We used human PECAM-transfected REN cells (REN\\/PECAM) as a model to compare targeting of antioxidant enzyme catalase conjugated with PECAM antibody (anti-PECAM\\/catalase) with adenoviral catalase delivery. Anti-PECAM\\/125I-catalase bound to REN\\/PECAM, but not to REN cells (70 vs. 1 ng\\/well vs. < 2 ng\\/well of unmodified catalase). At

Thomas D Sweitzer; Anu P Thomas; Rainer Wiewrodt; Marian T Nakada; Francisco Branco; Vladimir R Muzykantov

2003-01-01

100

Protandim attenuates intimal hyperplasia in human saphenous veins cultured ex vivo via a catalase-dependent pathway.  

PubMed

Human saphenous veins (HSVs) are widely used for bypass grafts despite their relatively low long-term patency. To evaluate the role of reactive oxygen species (ROS) signaling in intima hyperplasia (IH), an early stage pathology of vein-graft disease, and to explore the potential therapeutic effects of up-regulating endogenous antioxidant enzymes, we studied segments of HSV cultured ex vivo in an established ex vivo model of HSV IH. Results showed that HSV cultured ex vivo exhibit an ~3-fold increase in proliferation and ~3.6-fold increase in intimal area relative to freshly isolated HSV. Treatment of HSV during culture with Protandim, a nutritional supplement known to activate Nrf2 and increase the expression of antioxidant enzymes in several in vitro and in vivo models, blocks IH and reduces cellular proliferation to that of freshly isolated HSV. Protandim treatment increased the activity of SOD, HO-1, and catalase 3-, 7-, and 12-fold, respectively, and decreased the levels of superoxide (O(2)(•-)) and the lipid peroxidation product 4-HNE. Blocking catalase activity by cotreating with 3-amino-1,2,4-triazole abrogated the protective effect of Protandim on IH and proliferation. In conclusion, these results suggest that ROS-sensitive signaling mediates the observed IH in cultured HSV and that up-regulation of endogenous antioxidant enzymes can have a protective effect. PMID:21167278

Joddar, Binata; Reen, Rashmeet K; Firstenberg, Michael S; Varadharaj, Saradhadevi; McCord, Joe M; Zweier, Jay L; Gooch, Keith J

2010-12-15

101

Superoxide dismutase and catalase activities in Photobacterium damselae ssp. piscicida.  

PubMed

The ability of a set of Photobacterium damselae ssp. piscicida strains isolated from different fish species to produce different superoxide dismutase (SOD) and catalase enzymes was determined. Unlike other bacterial pathogens, P. damselae ssp. piscicida is not able to produce different isoforms of SOD or catalase containing different metal cofactors when cultured under oxidative stress induced by hydrogen peroxide or methyl viologen, or under iron depleted conditions. However, iron content of the growth medium influenced the levels of SOD and catalase activity in cells, these levels decreasing with iron availability of the medium. Comparison of virulent and non-virulent strains of P. damselae ssp. piscicida showed similar contents of SOD, but higher levels of catalase were detected in cells of the virulent strain. Incubation of bacteria with sole, Solea senegalensis (Kaup), phagocytes has shown that survival rates range from 19% to 62%, these rates being higher for the virulent strain. The increased levels of catalase activity detected in the virulent strain indicates a possible role for this enzyme in bacterial survival. PMID:16768716

Díaz-Rosales, P; Chabrillón, M; Arijo, S; Martinez-Manzanares, E; Moriñigo, M A; Balebona, M C

2006-06-01

102

A Simple Assay for Measuring Catalase Activity: A Visual Approach  

PubMed Central

In this study, an assay that combines the ease and simplicity of the qualitative approach for measuring catalase activity was developed. The assay reagents comprised only hydrogen peroxide and Triton X-100. The enzyme-generated oxygen bubbles trapped by Triton X-100 were visualized as foam, whose height was estimated. A calibration plot using the defined unit of catalase activity yielded the best linear fit over a range of 20–300 units (U) (y = 0.3794x ? 2.0909, r2 = 0.993). The assay precision and reproducibility at 100 U were 4.6% and 4.8%, respectively. The applicability of the assay for measuring the catalase activity of various samples was assessed using laboratory strains of Escherichia coli, catalase-deficient isogenic mutants, clinically isolated Shiga toxin-producing E. coli, and human cells. The assay generated reproducible results. In conclusion, this new assay can be used to measure the catalase activity of bacterial isolates and human cells.

Iwase, Tadayuki; Tajima, Akiko; Sugimoto, Shinya; Okuda, Ken-ichi; Hironaka, Ippei; Kamata, Yuko; Takada, Koji; Mizunoe, Yoshimitsu

2013-01-01

103

Purification and characterization of a catalase-peroxidase and a typical catalase from the bacterium Klebsiella pneumoniae.  

PubMed

The bacterium Klebsiella pneumoniae synthesizes three different types of catalase: a catalase-peroxidase, a typical catalase and an atypical catalase, designated KpCP, KpT and KpA, respectively (Goldberg, I. and Hochman, A. (1989) Arch. Biochem. Biophys. 268, 124-128). KpCP, but not the other two enzymes, in addition to the catalatic activity, catalyzes peroxidatic activities with artificial electron donors, as well as with NADH and NADPH. Both KpCP and KpT are tetramers, with heme IX as a prosthetic group, and they show a typical high-spin absorption spectrum which is converted to low-spin when a cyanide complex is formed. The addition of dithionite to KpCP causes a shift in the absorption maxima typical of ferrous heme IX. KpCP has a pH optimum of 6.3 for the catalatic activity and 5.2-5.7 for the peroxidatic activity, and relatively low 'Km' values: 6.5 mM and 0.65 H2O2 for the catalatic and peroxidatic activities, respectively. The activity of the catalase-peroxidase is inhibited by azide and cyanide, but not by 3-amino-1,2,4-triazole. KpT has wide pH optimum: 5-10.5 and a 'Km' of 50 mM H2O2, it is inhibited by incubation with 3-amino-1,2,4-triazole and by the acidic forms of cyanide and azide. A significant distinction between the typical catalase and the catalase-peroxidase is the stability of their proteins: KpT is more stable than KpCP to H2O2, temperature, pH and urea. PMID:2029529

Hochman, A; Goldberg, I

1991-04-29

104

Kinetics of hydrogen peroxide decomposition by catalase: hydroxylic solvent effects.  

PubMed

The effect of water-alcohol (methanol, ethanol, propan-1-ol, propan-2-ol, ethane-1,2-diol and propane-1,2,3-triol) binary mixtures on the kinetics of hydrogen peroxide decomposition in the presence of bovine liver catalase is investigated. In all solvents, the activity of catalase is smaller than in water. The results are discussed on the basis of a simple kinetic model. The kinetic constants for product formation through enzyme-substrate complex decomposition and for inactivation of catalase are estimated. The organic solvents are characterized by several physical properties: dielectric constant (D), hydrophobicity (log P), concentration of hydroxyl groups ([OH]), polarizability (?), Kamlet-Taft parameter (?) and Kosower parameter (Z). The relationships between the initial rate, kinetic constants and medium properties are analyzed by linear and multiple linear regression. PMID:22565543

Raducan, Adina; Cantemir, Anca Ruxandra; Puiu, Mihaela; Oancea, Dumitru

2012-05-08

105

The peroxisomal catalase gene in the methylotrophic yeast Pichia methanolica.  

PubMed

In this paper, we describe the CTA1 gene, which encodes a peroxisomal catalase in the methylotrophic yeast Pichia methanolica. The P. methanolica CTA1 gene (PmCTA1) comprises a 1,530-bp open reading frame corresponding to a protein of 510 amino acid residues, and its deduced amino acid sequence shows high similarity to those of Cta1ps from other methylotrophic yeasts (about 79%). Expression of PmCTA1 in a peroxisomal catalase-depleted (Cbcta1Delta) Candida boidinii strain restored the methylotrophic growth of the host strain, while the expression of PmCTA1-DeltaSRL, which lacks peroxisome targeting signal type 1, did not. In P. methanolica, expression of PmCTA1 was induced when cells were grown on peroxisome-inducing carbon sources, viz., methanol, oleate, and D-alanine. Taken together, these results indicate that PmCTA1 encodes a functional peroxisomal catalase in P. methanolica. PMID:20699560

Nakagawa, Tomoyuki; Yoshida, Kyoko; Takeuchi, Akihito; Ito, Takashi; Fujimura, Shuki; Matsufuji, Yoshimi; Tomizuka, Noboru; Yurimoto, Hiroya; Sakai, Yasuyoshi; Hayakawa, Takashi

2010-08-07

106

Determination of Catalase Activity at Physiological Hydrogen Peroxide Concentrations  

Microsoft Academic Search

A method for the determination of catalase activity (EC 1.11.1.6.) in homogenates and cell suspensions is described by following the decomposition of H2O2at physiological H2O2levels. This first chemiluminescence assay for catalase activity is based on the reaction of luminol (5-amino-2,3-dihydro-1,4-phthalazinedione) and NaOCl. The chemiluminescence of this reaction specifically depends on the H2O2concentration and shows fast kinetics of less than 2

Sebastian Mueller; Hans-Dieter Riedel; Wolfgang Stremmel

1997-01-01

107

Loading PEG-Catalase into Filamentous and Spherical Polymer Nanocarriers  

Microsoft Academic Search

Purpose  Based on a unique phase alignment that occurs during formulation, we postulated that PEG-ylation of the cargo enzyme would\\u000a enhance its encapsulation within diblock copolymer nanocarriers and thus resistance to proteases.\\u000a \\u000a \\u000a \\u000a Methods  A freeze–thaw modified double emulsion technique was utilized to encapsulate either the catalytically active enzyme catalase\\u000a (MW ?250 kDa) or PEG-catalase in PEG–PLA polymer nanocarriers (PNC). Spectrophotometer measurement of substrate

Eric A. Simone; Thomas D. Dziubla; Evguenia Arguiri; Vanessa Vardon; Vladimir V. Shuvaev; Melpo Christofidou-Solomidou; Vladimir R. Muzykantov

2009-01-01

108

Development of lyophilization cycle and effect of excipients on the stability of catalase during lyophilization  

PubMed Central

Introduction: The purpose of the present study was to screen excipients such as amino acids and non-aqueous solvents for their stabilizing effect on catalase, a model protein, for lyophilization. The present study also includes optimization of lyophilization cycle for catalase formulations, which is essential from the commercial point of view, since lyophilization is an extremely costly process. Materials and Methods: Activity of catalase was determined using catalase activity assay. Differential scanning calorimetry was used to determine eutectic melting temperature of the frozen catalase solution, which is essential for the optimization of lyophilization cycle. Results: When catalase was lyophilized without excipients, it was found that about 65-78% of the initial activity of catalase was lost during the lyophilization process in a concentration dependent manner. The maximum stability of catalase during lyophilization was observed at pH 7.0. Amino acids like alanine, glycine, lysine, serine and 4-hydroxy proline showed strong stabilizing effect on catalase during lyophilization by protecting catalase activity above 95%, whereas valine and cysteine hydrochloride showed destabilizing effect on catalase. Non-aqueous solvents such as dimethyl formamide, dimethyl sulphoxide, polyethylene glycol (PEG) 200, PEG 400, PEG 600 and ethylene glycol also showed destabilizing effect on catalase during lyophilization. Conclusions: In order to prevent loss of catalase activity during lyophilization of catalase, use of amino acids like alanine, glycine, lysine, serine and 4-hydroxy proline in optimum concentration is highly advisable.

Lale, Shantanu V; Goyal, Monu; Bansal, Arvind K

2011-01-01

109

Effects of peroxisomal catalase inhibition on mitochondrial function.  

PubMed

Peroxisomes produce hydrogen peroxide as a metabolic by-product of their many oxidase enzymes, but contain catalase that breaks down hydrogen peroxide in order to maintain the organelle's oxidative balance. It has been previously demonstrated that, as cells age, catalase is increasingly absent from the peroxisome, and resides instead as an unimported tetrameric molecule in the cell cytosol; an alteration that is coincident with increased cellular hydrogen peroxide levels. As this process begins in middle-passage cells, we sought to determine whether peroxisomal hydrogen peroxide could contribute to the oxidative damage observed in mitochondria in late-passage cells. Early-passage human fibroblasts (Hs27) treated with aminotriazole (3-AT), an irreversible catalase inhibitor, demonstrated decreased catalase activity, increased levels of cellular hydrogen peroxide, protein carbonyls, and peroxisomal numbers. This treatment increased mitochondrial reactive oxygen species levels, and decreased the mitochondrial aconitase activity by ?85% within 24?h. In addition, mitochondria from 3-AT treated cells show a decrease in inner membrane potential. These results demonstrate that peroxisome-derived oxidative imbalance may rapidly impair mitochondrial function, and considering that peroxisomal oxidative imbalance begins to occur in middle-passage cells, supports the hypothesis that peroxisomal oxidant release occurs upstream of, and contributes to, the mitochondrial damage observed in aging cells. PMID:22536190

Walton, Paul A; Pizzitelli, Michael

2012-04-23

110

A blue catalase screening test for pyuria and haematuria  

Microsoft Academic Search

The blue catalase test is easy to perform and economical of materials. In a series of 529 adult female hospital patients it appeared to be a good screening test for pyuria and haematuria, detecting all but one of the specimens examined with more than 20 red and white cells combined per cubic millimetre of urine and 95·2% of those with

Mair Thomas; Gillian Baldwin

1971-01-01

111

Electrochemical Method for Detecting Hydrogen Peroxide–Catalase-Treated Milk  

Microsoft Academic Search

The electrochemical determination of oxy- gen in milk provides a quick, practical, and simple means of detecting hydrogen per- oxide-catalase-treated milk. A fresh, raw milk containing more than 15 ppm oxygen should be viewed with suspicion. Severe agitation of milk or flushing with gases reduces the oxygen differential between treated and untreated milks, but under realistic field conditions agitation is

E. J. Siegenthaler; F. V. Kosikowski

1969-01-01

112

Effects of Peroxisomal Catalase Inhibition on Mitochondrial Function  

PubMed Central

Peroxisomes produce hydrogen peroxide as a metabolic by-product of their many oxidase enzymes, but contain catalase that breaks down hydrogen peroxide in order to maintain the organelle’s oxidative balance. It has been previously demonstrated that, as cells age, catalase is increasingly absent from the peroxisome, and resides instead as an unimported tetrameric molecule in the cell cytosol; an alteration that is coincident with increased cellular hydrogen peroxide levels. As this process begins in middle-passage cells, we sought to determine whether peroxisomal hydrogen peroxide could contribute to the oxidative damage observed in mitochondria in late-passage cells. Early-passage human fibroblasts (Hs27) treated with aminotriazole (3-AT), an irreversible catalase inhibitor, demonstrated decreased catalase activity, increased levels of cellular hydrogen peroxide, protein carbonyls, and peroxisomal numbers. This treatment increased mitochondrial reactive oxygen species levels, and decreased the mitochondrial aconitase activity by ?85% within 24?h. In addition, mitochondria from 3-AT treated cells show a decrease in inner membrane potential. These results demonstrate that peroxisome-derived oxidative imbalance may rapidly impair mitochondrial function, and considering that peroxisomal oxidative imbalance begins to occur in middle-passage cells, supports the hypothesis that peroxisomal oxidant release occurs upstream of, and contributes to, the mitochondrial damage observed in aging cells.

Walton, Paul A.; Pizzitelli, Michael

2012-01-01

113

Inhibition of Catalase by 3,3'-Diaminobenzidine.  

National Technical Information Service (NTIS)

3,3'-Diaminobenzidine strongly inhibits bovine liver catalase in two distinct ways. One of these was competitive with respect to H202, approached a limit of 100% inhibition and was rapidly reversed by dilution or by dialysis. The other was dependent upon ...

D. Darr I. Fridovich

1985-01-01

114

Activation of Catalase and Other Enzymes by Corn Oil Intake  

Microsoft Academic Search

The effects of linoleic acid intake on catalase and other enzymes were investigated by feeding 0, 1, 5 or 10% corn oil diet to rats previously fed a fat-free diet. Rats fed more than 1% corn oil for 2 weeks showed significant increases of glutathione peroxidase and Superoxide dismutase in liver cytosol when compared to the controls fed no corn

NOBUKO IRITANI; YUMIKO IKEDA

115

USE OF CATALASE FROM SPINACH FOR TESTING AT MOLECULAR LEVEL THE TOXICITY OF SOME IONIC LIQUIDS  

Microsoft Academic Search

SUMMARY The present work tries to evaluate catalase from spinach in order to introduce it into an ecotoxicological test battery. Previous to the determination of the influence of some ionic liquids on spinach catalase activity, the optimization of assay enzyme was performed. Optimum pH for spinach leaves catalase is between 7.5-8. Spinach catalase seems to not be inhibited by its

Ana-Maria Lacr; Laura Pope; Vasile Ostafe

116

Purification of three catalase isozymes from facultatively alkaliphilic Bacillus firmus OF4  

Microsoft Academic Search

Cell extracts of facultatively alkaliphilic B. firmus OF4 were assayed for catalase activity and their catalase isozyme content was analyzed on native polyacrylamide gels stained for catalase activity. pH-10.5-grown cells had about twice the specific catalase activity of pH-7.5-grown cells. The higher activity, however, did not confer resistance to exogenous hydrogen peroxide challenge relative to pH-7.5-grown cells and, in fact,

David B. Hicks

1995-01-01

117

Cloning, characterization and tissue expression of disk abalone ( Haliotis discus discus) catalase  

Microsoft Academic Search

Catalase is an antioxidant enzyme that plays a significant role in protection against oxidative stress by detoxification of hydrogen peroxide (H2O2). A gene coding for a putative catalase was isolated from the disk abalone (Haliotis discus discus) cDNA library and denoted as Ab-catalase. The full-length (2864bp) Ab-catalase cDNA contained 1,503bp open reading frame (ORF), encoding 501 amino acid residues with

Prashani Mudika Ekanayake; Mahanama De Zoysa; Hyun-Sil Kang; Qiang Wan; Youngheun Jee; Youn-Ho Lee; Sang-Jin Kim; Jehee Lee

2008-01-01

118

Immobilization of catalase by using Zr(IV)-modified collagen fiber as the supporting matrix  

Microsoft Academic Search

Collagen fiber (CF), an abundant natural material of biopolymer, was used as supporting matrix for immobilization of catalase. CF was firstly reacted with Zr(IV), then the catalase was immobilized on Zr(IV)-modified CF (Zr–CF) by adsorption. The structures and properties of Zr–CF and the Zr–CF immobilized catalase (Zr–CF-catalase) were characterized by means of DSC, SEM, FT-IR, etc. It was found that

Na Song; Shuang Chen; Xin Huang; Xuepin Liao; Bi Shi

2011-01-01

119

Detection of Hydrogen Peroxide and Glucose Based on Immobilized C60Catalase Enzyme  

Microsoft Academic Search

The interaction between fullerene C60 and catalase enzyme was studied with a fullerene C60-coated piezoelectric (PZ) quartz crystal sensor. The partially irreversible response of the C60-coated PZ crystal sensor for catalase was observed by the desorption study, which implied that C60 could chemically react with catalase. Thus, immobilized fullerene C60-catalase enzyme was synthesized and applied in deter- mining hydrogen peroxide

Chia-Wen Chuang; Li-Yung Luo; Ming-Sen Chang; Jeng-Shong Shih

2009-01-01

120

Catalase from the silkworm, Bombyx mori: Gene sequence, distribution, and overexpression  

Microsoft Academic Search

Living organisms require mechanisms regulating reactive oxygen species (ROS) such as hydrogen peroxide and superoxide anion. Catalase is one of the regulatory enzymes and facilitates the degradation of hydrogen peroxide to oxygen and water. Biochemical information on an insect catalase is, however, insufficient. Using mRNA from fat body of the silkworm, Bombyx mori, a cDNA encoding a putative catalase was

Kohji Yamamoto; Yutaka Banno; Hiroshi Fujii; Fumio Miake; Nobuhiro Kashige; Yoichi Aso

2005-01-01

121

A Simple Method for Demonstrating Enzyme Kinetics Using Catalase from Beef Liver Extract  

Microsoft Academic Search

This paper describes a simple visual method of demonstrating enzyme kinetics using beef liver catalase. A catalase solution is obtained by homogenizing beef liver in a phosphate buffer. In the demonstration, filter paper is saturated with beef liver extract and placed into a solution of hydrogen peroxide. The catalase in the extract decomposes the hydrogen peroxide to water and oxygen.

Kristin A. Johnson

2000-01-01

122

FSH induced stimulation of catalase activity in goat granulosa cells in vitro  

Microsoft Academic Search

Reactive oxygen species scavenging enzymes like catalase play diverse role in mammals. The presence of catalase in mammalian ovary is now well established. In the present investigation, changes in catalase activity in granulosa cells isolated from follicles at various stages of differentiation in response to FSH were studied. The follicles were dissected out from goat ovaries and classified as small

Rahul Behl; R. S. Pandey

2002-01-01

123

Catalase Activity During Muscular Activity in Birds (Aktivnost Katalazy V Protsesse Myshechnoi Deyatelnosti U Ptits).  

National Technical Information Service (NTIS)

The individual constant of catalase activity in the muscles of various pigeons is different. Expressing the catalase activity in milliliters of 0.1 N hydrogen peroxide decomposed by catalase, we find a minimum of 383.4 ml and a maximum of 874.0 ml, and an...

G. I. Rogachev

1969-01-01

124

Molecular cloning and sequence analysis of the Danio rerio catalase gene  

Microsoft Academic Search

Catalase is an antioxidant enzyme that plays a central role in the protection against oxidative stress through the metabolism of hydrogen peroxide. Catalase has been well studied in plants, bacteria, and mammals, but little work has been done in other vertebrate species. We have cloned the zebrafish (Danio rerio) catalase cDNA containing the complete coding region and analyzed expression by

Glenn S Gerhard; Elizabeth J Kauffman; Martin A Grundy

2000-01-01

125

Involvement of catalase in bacterial Blight disease development of rice caused by Xanthomonas oryzae pv. oryzae  

Microsoft Academic Search

We investigated the role of catalase in determining the virulence of Xanthomonas oryzae pv. oryzae isolates and the reaction of different rice cultivars to virulent isolates. Catalase, being an antioxidant enzyme, plays a major role in combating the toxic effect of reactive oxygen species (ROS) in plant cells. Among the 11 isolates studied, a variable level of catalase activity and

M. S. Choodamani; P. Hariprasad; M. K. Sateesh; S. Umesha

2009-01-01

126

Maternally transmitted milk containing recombinant human catalase provides protection against oxidation for mouse offspring during lactation  

Microsoft Academic Search

Catalase plays an important role in protecting organisms against oxidative damage caused by reactive oxygen species (ROS) by degrading surplus hydrogen peroxide. Addition of exogenous catalase can alleviate injuries caused by ROS. Thus, production of human catalase through genetic engineering will meet the increasing therapeutic demand for this enzyme. In this study, we successfully expressed the recombinant gene in mouse

Zuyong He; Shengli Yu; Gui Mei; Min Zheng; Meili Wang; Yunping Dai; Bo Tang; Ning Li

2008-01-01

127

Characterisation of the katA gene encoding a catalase and evidence for at least a second catalase activity in Staphylococcus xylosus, bacteria used in food fermentation  

Microsoft Academic Search

The catalase gene katA of Staphylococcus xylosus was cloned. It encodes a protein of 494 amino acids with a molecular mass of 56.9 kDa, closely related to monofunctional catalases. A katA mutant still showed a relatively high catalase activity demonstrating that S. xylosus possesses more than one enzyme. By Southern blot analysis using a katA probe, a second genetic locus

Charlotte Barrière; Reinhold Brückner; Delphine Centeno; Régine Talon

2002-01-01

128

Comparative immunological study of catalases in the genus Micrococcus.  

PubMed

Double immunodiffusion tests were performed with crude extracts from various Micrococcus species and antisera against catalase of Micrococcus luteus CCM 169. Cell-free extracts of M. lylae ATCC 27566 exhibited good cross-reaction. Cell-free extracts or catalase enriched preparations of M. varians reacted very weakly and no reaction has been found with preparation of M. kristinae, M. nishinomiyaensis, M. roseus and M. sedentarius. The quantitative microcomplement fixation assay also revealed a closer relationship between M. luteus and M. lylae than between M. luteus and M. varians. Strains of other Micrococcus species reacted in the microcomplement assay with M. luteus antiserum just a weakly as non-related strains, e.g. Staphylococcus aureus or Cellulomonas cartalyticum. PMID:71880

Rupprecht, M; Schleifer, K H

1977-07-26

129

The grid sectioning technique: a study of catalase platelets.  

PubMed Central

The grid sectioning technique has been used to obtain the two missing principal axis projections of orthorhombic catalase platelets and to measure directly the unit cell c-value. The negatively stained platelets have a unit cell c-dimension of half that proposed by Unwin (1975) from powder X-ray diffraction. The precision of the grid sectioning technique in positioning sections along a specimen axis shows that the growth fault lines usually observed on negatively stained catalase platelets are rows of missing molecules filled with stain. From these sections conclusions are drawn concerning the action of negative stain on a specimen, the microtomy process, and the specimen/supporting film interaction. Finally the value of microtomy for detailed structural analysis of biological objects is emphasized. Images Fig. 1. Fig. 2. Fig. 3. Fig. 4. Fig. 5. Fig. 6. Fig. 7.

Jesior, J C

1982-01-01

130

Catalase Test asan AidtotheIdentification of Enterobacteriace ae  

Microsoft Academic Search

Itwas further notedthat a widevariety of methods exist fortheexecution ofthecatalase test, thatthere isno universally accepted strength specified forthehydrogen peroxide, andthat no gradations forthevigor andspeed ofthereaction havebeenmentioned. Underthecondi- tions oftheclinical laboratory, we havedeveloped a simple, rapid, andaccu- ratemethodforthecatalase testthathasbeenofgreatvalue as an aidinthe identification oftheEnterobacteriaceae. With3%H202,itwas observed that Serratia, Proteus, andProvidencia were vigorous catalase reactors. OnlySal- monella andrareEscherichia, Enterobacter, andKlebsiella isolates were

WELTON I. TAYLOR

1972-01-01

131

Characterization of catalase from the seaweed Porphyra yezoensis  

Microsoft Academic Search

Catalase was partially purified from the marine red macroalga Porphyra yezoensis by sequential ammonium sulfate fractionation, ion-exchange and hydrophobic interaction chromatography. Extraction from frozen and powdered material under liquid nitrogen was more efficient than that from fresh or freeze-dried material. The maximal activity of the enzyme was observed in the pH range 6.0–11.0, but the activity rapidly decreased below pH

Toshiki Nakano; Masumi Watanabe; Minoru Sato; Masaaki Takeuchi

1995-01-01

132

Genes Important for Catalase Activity in Enterococcus faecalis  

Microsoft Academic Search

Little in general is known about how heme proteins are assembled from their constituents in cells. The Gram-positive bacterium Enterococcus faecalis cannot synthesize heme and does not depend on it for growth. However, when supplied with heme in the growth medium the cells can synthesize two heme proteins; catalase (KatA) and cytochrome bd (CydAB). To identify novel factors important for

Michael Baureder; Lars Hederstedt

2012-01-01

133

Progeric effects of catalase inactivation in human cells  

SciTech Connect

Peroxisomes generate hydrogen peroxide, a reactive oxygen species, as part of their normal metabolism. A number of pathological situations exist in which the organelle's capacity to degrade the potentially toxic oxidant is compromised. It is the peroxidase, catalase, which largely determines the functional antioxidant capacity of the organelle, and it is this enzyme that is affected in aging, in certain diseases, and in response to exposure to specific chemical agents. To more tightly control the enzymatic activity of peroxisomal catalase and carefully document the effects of its impaired action on human cells, we employed the inhibitor 3-amino-1,2,4-triazole. We show that by chronically reducing catalase activity to approximately 38% of normal, cells respond in a dramatic manner, displaying a cascade of accelerated aging reactions. Hydrogen peroxide and related reactive oxygen species are produced, protein and DNA are oxidatively damaged, import into peroxisomes and organelle biogenesis is corrupted, and matrix metalloproteinases are hyper-secreted from cells. In addition, mitochondria are functionally impaired, losing their ability to maintain a membrane potential and synthesize reactive oxygen species themselves. These latter results suggest an important redox-regulated connection between the two organelle systems, a topic of considerable interest for future study.

Koepke, Jay I.; Wood, Christopher S.; Terlecky, Laura J. [Department of Pharmacology, Wayne State University School of Medicine, 540 E. Canfield Avenue, Detroit, Michigan, 48201 (United States); Walton, Paul A. [Department of Anatomy and Cell Biology, University of Western Ontario, London, Ontario (Canada); Terlecky, Stanley R. [Department of Pharmacology, Wayne State University School of Medicine, 540 E. Canfield Avenue, Detroit, Michigan, 48201 (United States)], E-mail: srterlecky@med.wayne.edu

2008-10-01

134

Internal Catalase Protects Herpes Simplex Virus from Inactivation by Hydrogen Peroxide  

PubMed Central

Herpes simplex virus 1 (HSV-1) was shown to contain catalase, an enzyme able to detoxify hydrogen peroxide by converting it to water and oxygen. Studies with a catalase inhibitor indicated that virus-associated catalase can have a role in protecting the virus from oxidative inactivation. HSV-1 was found to be more sensitive to killing by hydrogen peroxide in the presence of a catalase inhibitor than in its absence. The results suggest a protective role for catalase during the time HSV-1 spends in the oxidizing environment outside a host cell.

Newcomb, William W.

2012-01-01

135

Histone H4 deacetylation down-regulates catalase gene expression in doxorubicin-resistant AML subline.  

PubMed

We explored if epigenetic mechanisms could be involved in the down-regulated expression of catalase gene (CAT) in the doxorubicin-resistant acute myelogenous leukemia (AML)-2/DX100 cells. Down-regulated CAT expression in AML-2/DX100 cells was completely recovered after treatment of hydrogen peroxide (H(2)O(2)) and histone deacetylase inhibitor, trichostatin A (TSA) but was increased slightly by the treatment of DNA methylation inhibitor, 5-aza-2'-deoxycytidine (5-AdC). Bisulfite-sequencing PCR revealed that a CpG island of CAT was not methylated in AML-2/DX100 cells. Chromatin immunoprecipitation assay confirmed that acetylation of histone H4 in AML-2/DX100 cells significantly decreased as compared with that in AML-2/WT cells, which was significantly increased by TSA more than 5-AdC. Meanwhile, overexpression of other up-regulated peroxidase genes appears to make compensation for decreased H(2)O(2)-scavenging activity for the down-regulated CAT expression in AML-2/DX100 cells. These results suggest that histone H4 deacetylation is responsible for the down-regulated CAT expression in AML-2/DX100 cells, which are well adapted to oxidative stress. PMID:21968610

Lee, Tae-Bum; Moon, Young-Sook; Choi, Cheol-Hee

2011-10-05

136

Structure–Function Relationships in Fungal Large-Subunit Catalases  

SciTech Connect

Neurospora crassa has two large-subunit catalases, CAT-1 and CAT-3. CAT-1 is associated with non-growing cells and accumulates particularly in asexual spores; CAT-3 is associated with growing cells and is induced under different stress conditions. It is our interest to elucidate the structure-function relationships in large-subunit catalases. Here we have determined the CAT-3 crystal structure and compared it with the previously determined CAT-1 structure. Similar to CAT-1, CAT-3 hydrogen peroxide (H{sub 2}O{sub 2}) saturation kinetics exhibited two components, consistent with the existence of two active sites: one saturated in the millimolar range and the other in the molar range. In the CAT-1 structure, we found three interesting features related to its unusual kinetics: (a) a constriction in the channel that conveys H{sub 2}O{sub 2} to the active site; (b) a covalent bond between the tyrosine, which forms the fifth coordination bound to the iron of the heme, and a vicinal cysteine; (c) oxidation of the pyrrole ring III to form a cis-hydroxyl group in C5 and a cis-{gamma}-spirolactone in C6. The site of heme oxidation marks the starts of the central channel that communicates to the central cavity and the shortest way products can exit the active site. CAT-3 has a similar constriction in its major channel, which could function as a gating system regulated by the H{sub 2}O{sub 2} concentration before the gate. CAT-3 functional tyrosine is not covalently bonded, but has instead the electron relay mechanism described for the human catalase to divert electrons from it. Pyrrole ring III in CAT-3 is not oxidized as it is in other large-subunit catalases whose structure has been determined. Different in CAT-3 from these enzymes is an occupied central cavity. Results presented here indicate that CAT-3 and CAT-1 enzymes represent a functional group of catalases with distinctive structural characteristics that determine similar kinetics.

Diaz, A.; Valdez, V; Rudino-Pinera, E; Horjales, E; Hansberg, W

2009-01-01

137

Oxidation of human catalase by singlet oxygen in myeloid leukemia cells.  

PubMed

Catalases are oxidized by singlet oxygen giving rise to more acidic conformers detected in zymograms after electrophoresis in polyacrylamide gels. This shift in catalase mobility can be indicative of singlet oxygen production in vivo. Catalase from human cells, as from many organisms, is susceptible to in vitro modification by singlet oxygen. Human myeloid leukemia (U937) cells were treated under different stress conditions and catalase activity and its electrophoretic mobility was monitored. The U937 cells were found to have high levels of catalase activity, as compared to cultured fibroblasts, and to be very resistant to oxidative stress. Hydrogen peroxide did not modify the electrophoretic mobility of catalase, even at doses that produced cell damage. Conditions that primarily generate superoxide, such as treatment with paraquat or heat shock, also failed to modify the enzyme. In contrast, photosensitization reactions using rose Bengal gave rise to a more acidic conformer of catalase. Singlet oxygen quenchers prevented catalase modification by rose Bengal and light. The growth medium had a photosensitizing activity. Catalase was not modified in cells illuminated in phosphate buffer but was modified in cells illuminated in phosphate buffer containing riboflavin. Intense light per se also generated a slight shift in the electrophoretic mobility of catalase. Ultraviolet light (350 or 366 nm) did cause a change in catalase, but to a less acidic catalase conformer, indicating other modifications of the enzyme. The main effect of photosensitization with methylene blue was crosslinking of the enzyme, although some shift to acidic conformers was observed at a low concentration of the photoactive compound. Results indicate that catalase can be modified by singlet oxygen generated intracellularly, even though the enzyme is predominantly inside peroxisomes. Under some photosensitization conditions, catalase modification can be used as a marker to detect intracellular singlet oxygen. PMID:10628300

Lledías, F; Hansberg, W

1999-12-01

138

Isolation of catalase-deficient Escherichia coli mutants and genetic mapping of katE, a locus that affects catalase activity.  

PubMed

A number of catalase-deficient mutants of Escherichia coli which exhibit no assayable catalase activity were isolated. The only physiological difference between the catalase mutants and their parents was a 50- to 60-fold greater sensitivity to killing by hydrogen peroxide. For comparison, mutations in the xthA and recA genes of the same strains increased the sensitivity of the mutants to hydrogen peroxide by seven- and fivefold, respectively, showing that catalase was the primary defense against hydrogen peroxide. One class of mutants named katE was localized between pfkB and xthA at 37.8 min on the E. coli genome. A second class of catalase mutants was found which did not map in this region. PMID:6319370

Loewen, P C

1984-02-01

139

Wood utilization is dependent on catalase activities in the filamentous fungus Podospora anserina.  

PubMed

Catalases are enzymes that play critical roles in protecting cells against the toxic effects of hydrogen peroxide. They are implicated in various physiological and pathological conditions but some of their functions remain unclear. In order to decipher the role(s) of catalases during the life cycle of Podospora anserina, we analyzed the role of the four monofunctional catalases and one bifunctional catalase-peroxidase genes present in its genome. The five genes were deleted and the phenotypes of each single and all multiple mutants were investigated. Intriguingly, although the genes are differently expressed during the life cycle, catalase activity is dispensable during both vegetative growth and sexual reproduction in laboratory conditions. Catalases are also not essential for cellulose or fatty acid assimilation. In contrast, they are strictly required for efficient utilization of more complex biomass like wood shavings by allowing growth in the presence of lignin. The secreted CATB and cytosolic CAT2 are the major catalases implicated in peroxide resistance, while CAT2 is the major player during complex biomass assimilation. Our results suggest that P. anserina produces external H(2)O(2) to assimilate complex biomass and that catalases are necessary to protect the cells during this process. In addition, the phenotypes of strains lacking only one catalase gene suggest that a decrease of catalase activity improves the capacity of the fungus to degrade complex biomass. PMID:22558065

Bourdais, Anne; Bidard, Frederique; Zickler, Denise; Berteaux-Lecellier, Veronique; Silar, Philippe; Espagne, Eric

2012-04-27

140

Catalase degradation in sunflower cotyledons during peroxisome transition from glyoxysomal to leaf peroxisomal function. [Helianthus annuus  

SciTech Connect

First order rate constant for the degradation (degradation constants) of catalase in the cotyledons of sunflower (Helianthus annuus L.) were determined by measuring the loss of catalase containing /sup 14/C-labeled heme. During greening of the cotyledons, a period when peroxisomes change from glyoxysomal to leaf peroxisomal function, the degradation of glyoxysomal catalase is significantly slower than during all other stages of cotyledon development in light or darkness. The degradation constant during the transition stage of peroxisome function amounts to 0.205 day/sup -1/ in contrast to the constants ranging from 0.304 day/sup -1/ to 0.515 day/sup -1/ during the other developmental stages. Density labeling experiments comprising labeling of catalase with /sup 2/H/sub 2/O and its isopycnic centrifugation on CsCl gradients demonstrated that the determinations of the degradation constants were not substantially affected by reutilization of /sup 14/C-labeled compounds for catalase synthesis. The degradation constants for both glyoxysomal catalase and catalase synthesized during the transition of peroxisome function do not differ. This was shown by labeling the catalases with different isotopes and measuring the isotope ratio during the development of the cotyledons. The results are inconsistent with the concept that an accelerated and selective degradation of glyoxysomes underlies the change in peroxisome function. The data suggest that catalase degradation is at least partially due to an individual turnover of catalase and does not only result from a turnover of the whole peroxisomes.

Eising, R.; Gerhardt, B.

1987-06-01

141

Catalase activity of different Candida species after exposition to specific antiserum  

PubMed Central

Antisera were developed in rabbits after challenge with intracellular antigens of Candida albicans, C. tropicalis and C. parapsilosis. Microorganism catalase has been correlated with virulence, resistance to drugs and immunogenicity. The intracellular catalase is consistently present in strains of Candida and in this paper, the enzyme activity was analysed by PAGE after exposition to antisera. The catalases of C. albicans, C. parapsilosis and C. tropicalis were immunogenic and differed in their binding to specific antibodies raised in rabbits. Tests of cross-reactivity between different Candida species showed that when antiserum from C. albicans immunized rabbit was incubated with intracellular extracts of these three Candida species, the catalases activities were abolished. However, the antisera from C. parapsilosis or C. tropicalis immunized rabbits did not affect the catalase activity of C. albicans; the enzyme of C. albicans was inactivated only by the antiserum to the catalase of own C. albicans. The antiserum to the catalase of C. tropicalis was species-specific and did not cross-react with catalases of C. albicans and C. parapsilosis. The activities of Aspergillus niger and bovine catalases were not affected by the antiserum from any Candida immunized rabbits. This report is a preliminary study of specific antisera that react against intracellular catalase of Candida sp. and neutralize the enzymatic activity. Further study is necessary to develop species-specific antibody once differences in the susceptibility of the Candida species to commonly used antifungal drugs make identification to the species level important.

Miyasaka, Natalia R.S.; Unterkircher, Carmelinda S.; Shimizu, Mario T.

2008-01-01

142

Glyoxylic acid production using immobilized glycolate oxidase and catalase.  

PubMed

A variety of methods for the immobilization of glycolate oxidase have been examined for the preparation of a catalyst for the oxidation of glycolic acid to glyoxylic acid. The co-immobilization of glycolate oxidase and catalase on oxirane acrylic beads produced a catalyst which was stable to the reaction conditions used for the oxidation, where glycolic acid and oxygen are reacted in aqueous solution in the presence of the immobilized enzyme catalyst and ethylenediamine. Under optimum reaction conditions, 99% yields of glyoxylic acid were obtained at greater than 99% conversion of glycolic acid, and the recovery and reuse of the co-immobilized enzyme catalyst was demonstrated. PMID:8000856

Seip, J E; Fager, S K; Gavagan, J E; Anton, D L; Di Cosimo, R

1994-06-01

143

Kinetic evaluation of catalase and peroxygenase activities of tyrosinase.  

PubMed

Tyrosinase is a copper monooxygenase containing a coupled dinuclear copper active site (type-3 copper), which catalyzes oxygenation of phenols (phenolase activity) as well as dehydrogenation of catechols (catecholase activity) using O(2) as the oxidant. In this study, catalase activity (conversion of H(2)O(2) to (1/2)O(2) and H(2)O) and peroxygenase activity (H(2)O(2)-dependent oxygenation of substrates) of mushroom tyrosinase have been examined kinetically by using amperometric O(2) and H(2)O(2) sensors. The catalase activity has been examined by monitoring the initial rate of O(2) production from H(2)O(2) in the presence of a catalytic amount of tyrosinase in 0.1 M phosphate buffer (pH 7.0) at 25 degrees C under initially anaerobic conditions. It has been found that the catalase activity of mushroom tyrosinase is three-order of magnitude greater than that of mollusk hemocyanin. The higher catalase activity of tyrosinase could be attributed to easier accessibility of H(2)O(2) to the dinuclear copper site of tyrosinase. Mushroom tyrosinase has also been demonstrated for the first time to catalyze oxygenation reaction of phenols with H(2)O(2) (peroxygenase activity). The reaction has been investigated kinetically by monitoring the H(2)O(2) consumption rate in 0.5 M borate buffer (pH 7.0) under aerobic conditions. Similarity of the substituent effects of a series of p-substituted phenols in the peroxygenase reaction with H(2)O(2) to those in the phenolase reaction with O(2) as well as the absence of kinetic deuterium isotope effect with a perdeuterated substrate (p-Cl-C(6)D(4)OH vs p-Cl-C(6)H(4)OH) clearly demonstrated that the oxygenation mechanisms of phenols in both systems are the same, that is, the electrophilic aromatic substitution reaction by a (micro-eta(2):eta(2)-peroxo)dicopper(II) intermediate of oxy-tyrosinase. PMID:15350140

Yamazaki, Shin-ichi; Morioka, Chiyuki; Itoh, Shinobu

2004-09-14

144

Pretreatment with interferon-gamma protects microglia from oxidative stress via up-regulation of Mn-SOD.  

PubMed

Microglial cells, resident macrophage-like immune cells in the brain, are exposed to intense oxidative stress under various pathophysiological conditions. For self-defense against oxidative injuries, microglial cells must be equipped with antioxidative mechanisms. In this study, we investigated the regulation of antioxidant enzyme systems in microglial cells by interferon-gamma (IFN-gamma) and found that pretreatment with IFN-gamma for 20 h protected microglial cells from the toxicity of various reactive species such as hydrogen peroxide (H(2)O(2)), superoxide anion, 4-hydroxy-2(E)-nonenal, and peroxynitrite. The cytoprotective effect of IFN-gamma pretreatment was abolished by the protein synthesis inhibitor cycloheximide. In addition, treatment of microglial cells with both IFN-gamma and H(2)O(2) together did not protect them from the H(2)O(2)-evoked toxicity. These results imply that protein synthesis is required for the protection by IFN-gamma. Among various antioxidant enzymes such as manganese or copper/zinc superoxide dismutase (Mn-SOD or Cu/Zn-SOD), catalase, and glutathione peroxidase (GPx), only Mn-SOD was up-regulated in IFN-gamma-pretreated microglial cells. Transfection with siRNA of Mn-SOD abolished both up-regulation of Mn-SOD expression and protection from H(2)O(2) toxicity by IFN-gamma pretreatment. Furthermore, whereas the activities of Mn-SOD and catalase were up-regulated by IFN-gamma pretreatment, those of Cu/Zn-SOD and GPx were not. These results indicate that IFN-gamma pretreatment protects microglial cells from oxidative stress via selective up-regulation of the level of Mn-SOD and activity of Mn-SOD and catalase. PMID:19439213

Chen, Xia; Choi, In Young; Chang, Tong-Shin; Noh, You Hyun; Shin, Chan Young; Wu, Chun-Fu; Ko, Kwang Ho; Kim, Won-Ki

2009-02-09

145

High Conformational Stability of Secreted Eukaryotic Catalase-peroxidases  

PubMed Central

Catalase-peroxidases (KatGs) are bifunctional heme enzymes widely spread in archaea, bacteria, and lower eukaryotes. Here we present the first crystal structure (1.55 Å resolution) of an eukaryotic KatG, the extracellular or secreted enzyme from the phytopathogenic fungus Magnaporthe grisea. The heme cavity of the homodimeric enzyme is similar to prokaryotic KatGs including the unique distal +Met-Tyr-Trp adduct (where the Trp is further modified by peroxidation) and its associated mobile arginine. The structure also revealed several conspicuous peculiarities that are fully conserved in all secreted eukaryotic KatGs. Peculiarities include the wrapping at the dimer interface of the N-terminal elongations from the two subunits and cysteine residues that cross-link the two subunits. Differential scanning calorimetry and temperature- and urea-mediated unfolding followed by UV-visible, circular dichroism, and fluorescence spectroscopy combined with site-directed mutagenesis demonstrated that secreted eukaryotic KatGs have a significantly higher conformational stability as well as a different unfolding pattern when compared with intracellular eukaryotic and prokaryotic catalase-peroxidases. We discuss these properties with respect to the structure as well as the postulated roles of this metalloenzyme in host-pathogen interactions.

Zamocky, Marcel; Garcia-Fernandez, Queralt; Gasselhuber, Bernhard; Jakopitsch, Christa; Furtmuller, Paul G.; Loewen, Peter C.; Fita, Ignacio; Obinger, Christian; Carpena, Xavi

2012-01-01

146

Selection of bovine catalase aptamers using non-SELEX.  

PubMed

In this research, we used the non-SELEX method to successfully select an aptamer that binds to the protein target (bovine catalase) with a K(D) value in the low micro molar range. The time window was determined for the target and aptamer library by optimizing the buffer conditions using 3 × Tris-glycine-potassium phosphate (TGK) buffer as the run buffer and 1× TGK as the selection buffer to give the biggest complex peak. Fractions were collected by multistep nonequilibrium capillary electrophoresis of equilibrium mixtures (NECEEM)-based partitioning for three rounds of selection. The fractions from each round were enriched using PCR and the progress of selection was monitored using bulk affinity analysis. Fraction 2 was determined to have the optimal bulk affinity (0.75 ?M) and this enriched library was cloned and sequenced giving four aptamer sequences. These sequences were verified using affinity capillary electrophoresis (CAT 1 0.237 ?M) and fluorescence intensity measurements (CAT 1 0.430 ?M). The specificity of the aptamer was also determined by fluorescence intensity measurements. The results showed that the aptamer with the highest binding affinity showed at least a 100-fold decrease in affinity toward four other proteins (i.e. lysozyme, trypsinogen, chymotrypsinogen A, and myoglobin) tested and this confirmed that the aptamer exhibited a distinct specificity toward bovine catalase. This aptamer will be useful in biosensing, Western blot, and biomarker identification. PMID:22965726

Ashley, Jon; Ji, Kaili; Li, Sam F Y

2012-09-01

147

Purification and characterization of an intracellular catalase-peroxidase from Penicillium simplicissimum  

Microsoft Academic Search

The first dimeric catalase-peroxidase of eucaryotic origin, an intracellular hydroperoxidase from Penicillium simplicissimum which exhibited both catalase and peroxidase activities, has been isolated. The enzyme has an apparent molecular mass of about 170 kDa and is composed of two identical subunits. The purified protein has a pH optimum for catalase activity at 6.4 and for peroxidase at 5.4. Both activities

Willem J. H. van Berkel; Wilfred R. Hagen; Hanno P. Roubroeks; Marco W. Fraaije

1996-01-01

148

Levels of dna damage are unaltered in mice overexpressing human catalase in nuclei  

Microsoft Academic Search

Two types of transgenic mice were generated to evaluate the role of hydrogen peroxide in the formation of nuclear DNA damage. One set of lines overexpresses wild-type human catalase cDNA, which is localized to peroxisomes. The other set overexpresses a human catalase construct that is targeted to the nucleus. Expression of the wild-type human catalase transgene was found in liver,

Samuel E Schriner; Charles E Ogburn; Annette C Smith; Terry G Newcomb; Warren C Ladiges; Martijn E. T Dollé; Jan Vijg; Ken-Ichiro Fukuchi; George M Martin

2000-01-01

149

Distribution of oxidase enzymes in potato tubers relative to blackspot susceptibility II. Peroxidase and Catalase  

Microsoft Academic Search

Peroxidase and catalase activities in selected potato tuber tissue were studied for differences and possible association with\\u000a resistance or susceptibility to blackspot. Unbruised stem-end tissue had significantly greater peroxidase activity than did\\u000a unbruised bud-end tissue. However, there was no significant difference between catalase activity at either end of the tuber;\\u000a between blackspot susceptibility and peroxidase or catalase activity; and between

M. L. Weaver; E. Hautala; R. M. Reeve

1971-01-01

150

Cloning and Heterologous Expression of Hematin-Dependent Catalase Produced by Lactobacillus plantarum CNRZ 1228  

PubMed Central

Lactobacillus plantarum CNRZ 1228 exhibited heme-dependent catalase activity under environmental conditions similar to those encountered during sausage fermentation. The 1,455-bp catalase gene (katL) was cloned and encoded a protein of 484 amino acids. Expression of katL in a heterologous host showed that katL encodes a functional catalase. PCR screening of selected strains of lactic acid bacteria for katL indicated the presence of similar genes in other strains of lactobacilli.

Abriouel, Hikmate; Herrmann, Anette; Starke, Joachim; Yousif, Nuha M. K.; Wijaya, Agus; Tauscher, Bernhard; Holzapfel, Wilhelm; Franz, Charles M. A. P.

2004-01-01

151

Immobilization of catalase via adsorption onto l-histidine grafted functional pHEMA based membrane  

Microsoft Academic Search

Poly(2-hydroxyethylmethacrylate) (pHEMA) based flat sheet membrane was prepared by UV-initiated photopolymerization technique. The membrane was then grafted with l-histidine. Catalase immobilization onto the membrane from aqueous solutions containing different amounts of catalase at different pH was investigated in a batch system. The maximum catalase immobilization capacity of the pHEMA–histidine membrane was 86?gcm?2. The activity yield was decreased with the increase

Sinan Akgöl; Yasemin Kaçar; Serpil Özkara; Handan Yavuz; Adil Denizli; M. Yakup Arica

2001-01-01

152

INHIBITION OF CATALASE IN MESENCEPHALIC CULTURES BY l-DOPA AND DOPAMINE  

Microsoft Academic Search

Catalase activity in cell cultures of fetal rat mesencephalon was decreased by 42 and 50%, respectively, after exposure to l-3,4-dihydroxyphenylalanine (l-DOPA, 100 ?M) or dopamine (100 ?M) for 48 h. Catalase activity was also decreased 21% by 10 ?M hydroquinone. Ascorbic acid (200 ?M), an agent that suppresses the autoxidation of l-DOPA and dopamine, blocked the anti-catalase effect of l-DOPA,

SHAN-KUO HAN; GERALD COHEN

1996-01-01

153

Comparison of Catalase in Diploid and Haploid Rana rugosa Using Heat and Chemical Inactivation Techniques  

Microsoft Academic Search

The present study examines differences in the hydrogen peroxide (H2O2) detoxifying enzyme, catalase, found in the tails and livers of diploid and haploid Rana rugosa. Investigative techniques include measurement of catalase activity and tests for temperature stability and chemical inhibition. Catalase from the tails of pre-climactic (stage XXIII) haploids was found to be over three times as H2O2 destructive as

Akihiko Kashiwagi; Keiko Kashiwagi; Minoru Takase; Hideki Hanada; Masahisa Nakamura

1997-01-01

154

The Catalase Inhibitor Sodium Azide Reduces Ethanol-Induced Locomotor Activity  

Microsoft Academic Search

SANCHIS-SEGURA, C., M. MIQUEL, M. CORREA AND C. M. G. ARAGON. The catalase inhibitor sodium azide reduces ethanol-induced locomotor activity. ALCOHOL 19(1) 37–42, 1999.—The involvement of brain catalase in modulating the psychopharmacological effects of ethanol was investigated by examining ethanol-induced locomotor activity in sodium azide-treated mice. Mice were pretreated with IP injections of the catalase inhibitor sodium azide (5, 10,

Carles Sanchis-Segura; Marta Miquel; Mercè Correa; Carlos M. G Aragon

1999-01-01

155

Molecular cloning of Daphnia magna catalase and its biomarker potential against oxidative stresses  

Microsoft Academic Search

Catalase (EC 1.11.1.6) is an important antioxidant enzyme that protects aerobic organisms against oxidative damage by degrading hydrogen peroxide to oxygen and water. Catalase mRNAs have been cloned from many species and employed as useful biomarkers of oxidative stress. In the present study, we cloned the cDNA from the catalase gene in Daphnia magna, analyzed its catalytic properties, and investigated

Jungkon Kim; Sunmi Kim; Kwang Wook An; Cheol Young Choi; Sungkyu Lee; Kyungho Choi

2010-01-01

156

Layer-by-layer self-assembly immobilization of catalases on wool fabrics.  

PubMed

A new immobilization strategy of catalases on natural fibers was reported in this paper. Catalase (CAT) from Bacillus subtilis was assembled into multiple layers together with poly(diallyldimethylammonium chloride) (PDDA) on wool fabrics via layer-by-layer (LBL) electrostatic self-assembly deposition. The mechanism and structural evaluation of LBL electrostatic self-assembly were studied in terms of scanning electron microscopy (SEM), surface zeta potential, and apparent color depth (K/S). The SEM pictures showed obvious deposits absorbed on the wool surfaces after LBL self-assembly. The surface zeta potential and dyeing depth of CAT/PDDA-assembled wool fabrics presented a regular layer-by-layer alternating trend along with the change of deposited materials, revealing the multilayer structure of the wool fiber immobilized catalases. The V(max) values were found to be 2,500±238 U/mg protein for the free catalase and 1,000±102 U/mg protein for the immobilized catalase. The K(m) value of free catalase (11.25±2.3 mM) was found to be lower than that of the immobilized catalase (222.2±36.5 mM). The immobilized catalase remained high enzymatic activity and showed a measureable amount of reusability, which proved that LBL electrostatic self-assembly deposition is a promising approach to immobilize catalases. PMID:23420488

Liu, J; Wang, Q; Fan, X R; Sun, X J; Huang, P H

2013-02-19

157

High concentrations of ascorbic acid induces apoptosis of human gastric cancer cell by p38MAP kinase-dependent up-regulation of transferrin receptor  

Microsoft Academic Search

We investigated the molecular mechanism by which ascorbic acid (AA) induces apoptosis in human gastric cancer cells, AGS cells. High concentration (more than 5mM) of AA increased cellular iron uptake by increasing transferrin receptor (TfR) expression and induced AGS cell apoptosis which was inhibited by catalase. Interestingly, p38 mitogen-activated protein kinase (MAPK) inhibitor inhibited the upregulation of TfR and increased

Yu Mi Ha; Min Kyu Park; Hye Jung Kim; Han Geuk Seo; Jae Heun Lee; Ki Churl Chang

2009-01-01

158

Regulation of catalase activity in leaves of Nicotiana sylvestris by high CO sub 2  

SciTech Connect

The effect of high CO{sub 2} (1% CO{sub 2}/21% O{sub 2}) on the activity of specific forms of catalase (CAT-1, -2, and -3) in seedling leaves of tobacco (Nicotiana sylvestris, Nicotiana tabacum) was examined. In high CO{sub 2} total catalase activity decreased by 50% in the first 2 days, followed by a more gradual decline in the next 4 days. The loss of total activity resulted primarily from a decrease in CAT-1 catalase. In contrast, the activity of CAT-3 catalase, a form with enhanced peroxidatic activity, increased 3-fold in high CO{sub 2} relative to air controls after 4 days. Short-term exposure to high CO{sub 2} indicated that the 50% loss of total activity occurs in the firs 12 hours. Catalase levels increased to normal within 12 hours after seedlings were returned to air. When seedlings were transferred to air after prolonged exposure to high CO{sub 2} (13 days), the levels of CAT-1 catalase were partially restored while CAT-3 remained at its elevated level. Levels of superoxide dismutase activity and those of several peroxisomal enzymes were not affected by high CO{sub 2}. Total catalase levels did not decline when seedlings were exposed to atmospheres of 0.04% CO{sub 2}/5% O{sub 2} or 0.04% CO{sub 2}/1% O{sub 2}, indicating that regulation of catalase in high CO{sub 2} is not related directly to suppression of photorespiration. Antibodies prepared against CAT-1 catalase from N. tabacum reacted strongly against CAT-1 catalase from both N. sylvestris and N. tabacum but not against CAT-3 catalase from either species.

Havir, E.A.; McHale, N.A. (Connecticut Agricultural Experiment Station, New Haven (USA))

1989-03-01

159

Isolation and characterization of catalase from Penicillium chrysogenum.  

PubMed

Catalase from a crude preparation of Penicillium chrysogenum was isolated in a single chromatographic step by immobilized metal ion affinity chromatography (IMAC) on Cu(II)-Chelating Sepharose Fast Flow. A chromatographically and electrophoretically homogeneous enzyme was obtained in 89% yield. IMAC was found to be superior to ion-exchange, hydrophobic interaction, size-exclusion and concanavalin A affinity chromatography. Analytical and preparative chromatography gave essentially the same chromatograms. Isoelectric point, molecular weight (by ultracentrifugation), amino acid composition, carbohydrate content and subunit organization were determined. The apparent Michaelis-Menten constant, KM, and the azide competitor constant, Ki, were calculated and found to be 59 microM and 6.1 microM, respectively. PMID:1639925

Chaga, G S; Medin, A S; Chaga, S G; Porath, J O

1992-06-26

160

Effect of nitrate and incubation conditions on the production of catalase and nitrate reductase by staphylococci  

Microsoft Academic Search

The objective of this work was to study the production of catalase and nitrate reductase by staphylococci in order to understand their role in lipid oxidation during sausage manufacturing. Catalase and nitrate reductase were measured in resting cells and supernatants of staphylococci grown in different conditions. All staphylococci (except S. warneri) synthetized nitrate reductase. In static condition, the synthesis was

R Talon; D Walter; S Chartier; C Barrière; M. C Montel

1999-01-01

161

Serum antibodies to Aspergillus fumigatus catalase in patients with cystic fibrosis  

Microsoft Academic Search

Seven to ten percent of patients with cystic fibrosis had serum antibodies to the catalase antigen ofAspergillus fumigatus in three cross-sectional surveys between 1977 and 1984. A total of 208 patients participated at least once, and the cumulated frequency of catalase antibodies in 94 patients included in all three surveys was 16 %. The titer range was 1 to 16.

H. Schønheyder; T. Jensen; I. H. LaessCe; N. Høiby; C. Koch

1988-01-01

162

Inhibition of catalase activity by oxidative stress and its relationship to salicylic acid accumulation in plants  

Microsoft Academic Search

The decrease in catalase activity and its relationship to change in salicylic acid content were investigated in rice, wheat, and cucumber seedlings exposed to oxidative stresses. A decrease in chlorophyll fluorescence (?F\\/Fm'), measured as an indicator of the oxidative stress, and a drop in catalase activity were observed following treatment with NaCl in all plant seedlings tested . Furthermore, such

Ie-Sung Shim; Yukie Momose; Akihiro Yamamoto; Dea-Wook Kim; Kenji Usui

2003-01-01

163

Immobilization of catalases from Bacillus SF on alumina for the treatment of textile bleaching effluents  

Microsoft Academic Search

A catalase preparation from a newly isolated Bacillus sp. was covalently immobilized on silanized alumina using glutaraldehyde as crosslinking agent. The effect of the coupling time of the enzyme-support reaction was determined in terms of protein recovery and immobilization yield and a certain balance point was found after which the activity recovery decreased. The activity profile of the immobilized catalase

Silgia A. Costa; Tzanko Tzanov; Andreas Paar; Marinka Gudelj; Georg M. Gübitz; Artur Cavaco-Paulo

2001-01-01

164

Tumor Necrosis Factor\\/Cachectin Decreases Catalase Activity of Rat Liver1  

Microsoft Academic Search

Tumor bearing hosts and animals treated with endotoxin commonly show a decrease in the catalase activity of the liver and kidney. Since tumor necrosis factor (TNF)\\/cachectin may play a significant role in these conditions, we investigated its effects on the catalatic and peroxi- datic activity of catalase in the liver and kidney of the rat. The activities of glucose-6-phosphate dehydrogenase

Walid G. Yasmineh; Janet L. Parkin; I. Caspers; Athanasios Theologides

165

Age-associated changes of superoxide dismutase and catalase activities in the rat brain  

Microsoft Academic Search

Oxygen free radicals have been proposed to be involved in the process of aging. Superoxide dismutase (SOD) and catalase are important for antioxidative defense. In this study, profiles of SOD, catalase, and their mRNA levels were investigated in the frontal, parietal, temporal and occipital lobes, subcortex and cerebellum of male Wistar rats at ages 1–21 months. The total SOD and

Huey-Jen Tsay; Pei Wang; Shyang-Long Wang; Hung-Hai Ku

2000-01-01

166

Inhibiting catalase activity sensitizes 36B10 rat glioma cells to oxidative stress  

Microsoft Academic Search

Gliomas are extremely resistant to anticancer therapies resulting in poor patient survival, due, in part, to altered expression of antioxidant enzymes. The primary antioxidant enzyme, catalase, is elevated constitutively in gliomas compared to normal astrocytes. We hypothesized that downregulating catalase in glioma cells would sensitize these cells to oxidative stress. To test this hypothesis, we implemented two approaches. The first,

Pameeka S. Smith; Weiling Zhao; Douglas R. Spitz; Mike E. Robbins

2007-01-01

167

Properties of erythrocyte catalase from homozygotes and heterozygotes for Swiss-type acatalasemia  

Microsoft Academic Search

The unstable catalase variant found in the blood of individuals homozygous for Swiss-type acatalasemia and the enzyme species present in heterozygous carriers of this rare defect have been further characterized. The mutant enzyme isolated from acatalasemic red cells is considerably more heat labile and differs in electrophoretic mobility from the normal enzyme. Catalase preparations obtained from heterozygotes consist of an

H. Aebi; Sonja R. Wyss; B. Scherz; J. Gross

1976-01-01

168

UVA-Irradiated Pheomelanin Alters the Structure of Catalase and Decreases Its Activity in Human Skin  

Microsoft Academic Search

More than 40 years ago Aronoff showed that catalase structure and activity is seriously affected by photo-oxidation of its own substrate, hydrogen peroxide, owing to cleavage of its porphyrin active site. Here we support the results of Maresca et al. (in this issue) and expand on them by using structural modeling of native catalase and its photo-oxidation product, where both

John M Wood; Karin U Schallreuter

2006-01-01

169

Effect of Butylated Hydroxyanisole on Catalase Activity and Malondialdehyde Content in Aging Zaprionus paravittiger (Diptera)  

Microsoft Academic Search

Catalase activity and malondialdehyde (MDA) content were measured in whole body and mitochondrial homogenates of the banana fruit fly, Zaprionus paravittiger, fed on control and butylated hydroxyanisole (BHA, 10 mM) mixed diets. Catalase activity increased during the reproductive period and decreased thereafter with age. However, the MDA content increased with advancing age in both sexes. In general, females exhibited higher

J. S. Bains; S. K. Garg; S. P. Sharma

1998-01-01

170

A biosensor based on catalase for determination of highly toxic chemical azide in fruit juices  

Microsoft Academic Search

In this work, an amperometric biosensor based on catalase enzyme was developed for the determination of azide. The principle of the measurements was based on the determination of the decrease in the differentiation of oxygen level which had been caused by the inhibition of catalase in the bioactive layer of the biosensor by azide.Firstly, the optimum conditions for the inhibitor

Mustafa Kemal Sezgintürk; Tüge Göktu?; Erhan Dinçkaya

2005-01-01

171

Characterization of Catalase Activities in a Root-Colonizing Isolate of 'Pseudomonas putida' (Revised).  

National Technical Information Service (NTIS)

Pseudomonas putida, a saprophytic root-colonizing bacterium, produces multiple forms of catalase. Catalase A, which increases in specific activity during growth phase and after treatment with H2O2, is located in the cytoplasm and is inhibited by 3-amino-1...

J. Katsuwon A. J. Anderson

1991-01-01

172

THE USE OF BEEF LIVER CATALASE AS A PROTEIN TRACER FOR ELECTRON MICROSCOPY  

Microsoft Academic Search

Beef liver catalase was injected intravenously into mice, and its distribution in the kidney, myocardium, and liver was studied with the electron microscope .A specific and relatively sensitive method was developed for its ultrastructural localization, based on the peroxidatic activity of catalase and employing a modified Graham and Karnovsky incubation medium. The main features of the medium were a higher

M. A. VENKATACHALAM; H. DARIUSH FAHIMI

2009-01-01

173

CHARACTERIZATION OF CATALASE ACTIVITIES IN A ROOT-CLEANING ISOLATE OF PSEUDOMONAS PUTIDA  

EPA Science Inventory

Psuedomonas putida, a saprophytic root-colonizing bacterium, produces multiple forms of catalase Catalase A which increases in specific activity during growth phase and after treatment with H2O2, is located in the and is inhibited by 3-amino-1,2-4-triazole, EDTA, and cyanide, but...

174

Development of a catalase based biosensor for alcohol determination in beer samples  

Microsoft Academic Search

An amperometric biosensor based on catalase enzyme for alcohol determination was developed. To construct the biosensor catalase was immobilized by using gelatin and glutaraldehyde on a Clark type dissolved oxygen (DO) probe covered with a teflon membrane which is sensitive for oxygen. The working principle of the biosensor depends on two reactions, which one is related to another, catalyzed by

Erol Akyilmaz; Erhan Dinçkaya

2003-01-01

175

Determination of calcium in milk and water samples by using catalase enzyme electrode  

Microsoft Academic Search

A biosensor based on catalase enzyme was developed for the investigation of the effect of calcium ions on the activity of the enzyme. Calcium plays an activator role for the catalase enzyme that catalyses the degradation of hydrogen peroxide to O2 and H2O. Determination method of the effect of calcium ion on the activity of the enzyme was based on

Erol Akyilmaz; Ozge Kozgus

2009-01-01

176

Activation?Based Catalase Enzyme Electrode and its Usage for Glucose Determination  

Microsoft Academic Search

In this study, a novel type amperometric biosensor, which is based on the activation of catalase enzyme by glucose, was developed and used for the sensitive determination of glucose. For the preparation of the biosensor catalase enzyme was immobilized in gelatin by using cross?linking agent glutaraldehyde and fixed on a pretreated teflon membrane of a dissolved oxygen probe. Glucose was

Pinar Akbayirli; Erol Akyilmaz

2007-01-01

177

Posttranscriptional Control Mediates Cell Type-Specific Localization of Catalase A during Aspergillus nidulans Development  

Microsoft Academic Search

Two differentially regulated catalase genes have been identified in the fungus Aspergillus nidulans. The catA gene belongs to a class whose transcripts are specifically induced during asexual sporulation (conidiation) and encodes a catalase accumulated in conidia. Using a developmental mutant affected in the brlA gene, which is unable to form conidia but capable of producing sexual spores (ascospores), we demonstrated

ROSA E. NAVARRO; JESUS AGUIRRE

1998-01-01

178

Differential Accumulation of Salicylic Acid and Salicylic Acid-Sensitive Catalase in Different Rice Tissues1  

Microsoft Academic Search

We previously proposed that salicylic acid (SA)-sensitive cata- lases serve as biological targets of SA in plant defense responses. To further examine the role of SA-sensitive catalases, we have analyzed the relationship between SA levels and SA sensitivity of catalases in different rice (Oryza saliva) tissues. We show here that, whereas rice shoots contain extremely high levels of free SA,

Zhixiang Chen; Allan Caplan; Daniel F. Klessig; Baofang Fan

1997-01-01

179

[Soil catalase activity of main plant communities in Leymus chinensis grassland in northeast China].  

PubMed

The seasonal dynamics of soil catalase activity of three different plants communities in Leymus chinensis grassland in northeast China were in a parabolas shape. The seasonal variation of Chloris virgata community was greater than those of Leymus chinensis community and Puccinellia tenuiflora community, and "seed effect" might be the main reason. The correlation between the activity of soil catalase in different soil layers and environmental factors were analyzed. The results showed that the activity of soil catalase was decreased gradually with depth of soil layer. The activity of soil catalase was closely correlated with rainfall and air temperature, and it was affected by soil temperature, soil moisture, and their interactions. The correlation between the activity and aboveground vegetation was very significant, and the growing condition of plant communities could be reflected by the activity of soil catalase. PMID:12216391

Lu, Ping; Guo, Jixun; Zhu, Li

2002-06-01

180

LESION SIMULATING DISEASE1 Interacts with Catalases to Regulate Hypersensitive Cell Death in Arabidopsis.  

PubMed

LESION SIMULATING DISEASE1 (lsd1) is an important negative regulator of programmed cell death (PCD) in Arabidopsis (Arabidopsis thaliana). The loss-of-function mutations in lsd1 cause runaway cell death triggered by reactive oxygen species. lsd1 encodes a novel zinc finger protein with unknown biochemical activities. Here, we report the identification of CATALASE3 (CAT3) as an lsd1-interacting protein by affinity purification and mass spectrometry-based proteomic analysis. The Arabidopsis genome contains three homologous catalase genes (CAT1, CAT2, and CAT3). Yeast two-hybrid and coimmunoprecipitation analyses demonstrated that lsd1 interacted with all three catalases both in vitro and in vivo, and the interaction required the zinc fingers of lsd1. We found that the catalase enzymatic activity was reduced in the lsd1 mutant, indicating that the catalase enzyme activity was partially dependent on lsd1. Consistently, the lsd1 mutant was more sensitive to the catalase inhibitor 3-amino-1,2,4-triazole than the wild type, suggesting that the interaction between lsd1 and catalases is involved in the regulation of the reactive oxygen species generated in the peroxisome. Genetic studies revealed that lsd1 interacted with CATALASE genes to regulate light-dependent runaway cell death and hypersensitive-type cell death. Moreover, the accumulation of salicylic acid was required for PCD regulated by the interaction between lsd1 and catalases. These results suggest that the lsd1-catalase interaction plays an important role in regulating PCD in Arabidopsis. PMID:23958864

Li, Yansha; Chen, Lichao; Mu, Jinye; Zuo, Jianru

2013-08-19

181

The relevance of the non-canonical PTS1 of peroxisomal catalase.  

PubMed

Catalase is sorted to peroxisomes via a C-terminal peroxisomal targeting signal 1 (PTS1), which binds to the receptor protein Pex5. Analysis of the C-terminal sequences of peroxisomal catalases from various species indicated that catalase never contains the typical C-terminal PTS1 tripeptide-SKL, but invariably is sorted to peroxisomes via a non-canonical sorting sequence. We analyzed the relevance of the non-canonical PTS1 of catalase of the yeast Hansenula polymorpha (-SKI). Using isothermal titration microcalorimetry, we show that the affinity of H. polymorpha Pex5 for a peptide containing -SKI at the C-terminus is 8-fold lower relative to a peptide that has a C-terminal -SKL. Fluorescence microscopy indicated that green fluorescent protein containing the -SKI tripeptide (GFP-SKI) has a prolonged residence time in the cytosol compared to GFP containing -SKL. Replacing the -SKI sequence of catalase into -SKL resulted in reduced levels of enzymatically active catalase in whole cell lysates together with the occurrence of catalase protein aggregates in the peroxisomal matrix. Moreover, the cultures showed a reduced growth yield in methanol-limited chemostats. Finally, we show that a mutant catalase variant that is unable to properly fold mislocalizes in protein aggregates in the cytosol. However, by replacing the PTS1 into -SKL the mutant variant accumulates in protein aggregates inside peroxisomes. Based on our findings we propose that the relatively weak PTS1 of catalase is important to allow proper folding of the enzyme prior to import into peroxisomes, thereby preventing the accumulation of catalase protein aggregates in the organelle matrix. PMID:22546606

Williams, Chris; Bener Aksam, Eda; Gunkel, Katja; Veenhuis, Marten; van der Klei, Ida J

2012-04-21

182

Loss of catalase activity in Tn1545-induced mutants does not reduce growth of Listeria monocytogenes in vivo.  

PubMed Central

Two catalase-negative mutants of Listeria monocytogenes were obtained by chromosomal insertions of the conjugative transposon Tn1545. The loss of catalase activity did not reduce the level of virulence of these mutants in mice. Indeed, both mutants were capable of growing in host tissues at the same rate as the parental catalase-positive strain. These results favor the view that catalase does not play a critical role in the resistance of L. monocytogenes to macrophage killing.

Leblond-Francillard, M; Gaillard, J L; Berche, P

1989-01-01

183

Kinetic Characterization of Extracellular Catalases from Penicillium piceum F-648 and Its Hydrogen Peroxide-Adapted Variants  

Microsoft Academic Search

A comparative kinetic study of extracellular catalases produced by Penicillium piceum F-648 and their variants adapted to H2O2 was performed in culture liquid filtrates. The specific activity of catalase, the maximum rate of catalase-induced H2O2 degradation (Vmax), Vmax\\/KM ratio, and the catalase inactivation rate constant in the enzymatic reaction (kin, s–1) were estimated in phosphate buffer (pH 7.4) at 30°C.

A. N. Eremin; D. I. Metelitsa; I. V. Moroz; Zh. I. Pavlovskaya; R. V. Mikhailova

2002-01-01

184

Klotho upregulation contributes to the neuroprotection of ligustilide in an Alzheimer's disease mouse model.  

PubMed

Klotho, an aging-suppressor gene, encodes a protein that potentially acts as a neuroprotective factor by modulating insulin-like growth factor 1 signaling and oxidative stress. In the present study, we investigated the potential role of Klotho in the therapeutic effect of ligustilide against Alzheimer's disease (AD)-like neuropathologies and memory impairment in aged senescence-accelerated mouse prone-8 (SAMP8) mice. Ligustilide treatment (10 and 40 mg/kg for 8 weeks, intragastrically) in 10-month-old SAMP8 mice reduced memory deficits, amyloid-?1-42 accumulation, tau phosphorylation, and neuron loss, increased mitochondrial manganese-superoxide dismutase and catalase expression and activity, and decreased malondialdehyde, protein carbonyl, and 8-hydroxydesoxyguanosine levels in the brain. Ligustilide upregulated Klotho expression in the cerebral choroid plexus and serum, decreased Akt and Forkhead box class O1 phosphorylation. Moreover, ligustilide inhibited the insulin-like growth factor 1 pathway and induced Forkhead box class O1 activation in 293T cells along with Klotho upregulation. An inverse correlation was found between Klotho expression and the AD phenotype, suggesting that Klotho might be a novel therapeutic target for age-related AD, and Klotho upregulation might contribute to the neuroprotective effect of ligustilide against AD. PMID:23973442

Kuang, Xi; Chen, Ya-Shu; Wang, Liang-Fen; Li, Yong-Jie; Liu, Ke; Zhang, Meng-Xue; Li, Ling-Jiao; Chen, Chu; He, Qian; Wang, Yu; Du, Jun-Rong

2013-08-21

185

Selective sensitization of bacteria to peroxide damage associated with fluoride inhibition of catalase and pseudocatalase.  

PubMed

Fluoride and sulfide are known inhibitors of heme catalases in acid environments. Staphylococcus aureus H cells were found to be sensitized by fluoride or sulfide to H2O2 killing at acid pH values in the range of 3.5 to 4.0, and catalase activity was reduced concomitantly. In contrast, fluoride had little effect on H2O2 killing of Streptococcus mutans GS-5, which has fluoride-insensitive peroxidase activity, but still is more sensitive to H2O2 than is S. aureus in the absence of fluoride. Fluoride but not sulfide was inhibitory also for the Mn-containing, non-heme pseudocatalase of Lactobacillus plantarum ATCC 14431 over a wide pH range, and this inhibitory effect was reflected in enhanced H2O2 killing in the presence of fluoride. In addition, we found that catalase-positive S. aureus or Neisseria sicca could protect catalase-negative S. mutans against killing by H2O2 in mixed suspensions, but protection was compromised by fluoride or sulfide under acid conditions. Thus, catalase-positive organisms could protect a catalase-negative organism against peroxide damage, but inhibition of catalase reduced protection. These findings are pertinent to the widespread use of fluoride and peroxide in oral health care products. PMID:11169136

Phan, T N; Kirsch, A M; Marquis, R E

2001-02-01

186

Maternally transmitted milk containing recombinant human catalase provides protection against oxidation for mouse offspring during lactation.  

PubMed

Catalase plays an important role in protecting organisms against oxidative damage caused by reactive oxygen species (ROS) by degrading surplus hydrogen peroxide. Addition of exogenous catalase can alleviate injuries caused by ROS. Thus, production of human catalase through genetic engineering will meet the increasing therapeutic demand for this enzyme. In this study, we successfully expressed the recombinant gene in mouse mammary gland, and biologically active human catalase was secreted into the milk of the transgenic mice. The peroxisomal targeting sequence (PTS) within the catalase gene had no significant negative effect on the secretion of the recombinant protein. Intake of the transgenic milk by the pups was found to decrease lipid peroxidation, increase the total superoxide dismutase (T-SOD) activity in the brain, and enhance the total antioxidative capacity (T-AOC) of brain, liver, and serum. To our knowledge, this is the first example of efficient production of biologically active human catalase in the milk of transgenic animals. Our study suggests that scaled-up production in transgenic farm animals would yield sufficient human catalase for biomedical research and clinical therapies. PMID:18722522

He, Zuyong; Yu, Shengli; Mei, Gui; Zheng, Min; Wang, Meili; Dai, Yunping; Tang, Bo; Li, Ning

2008-07-30

187

Comparison of the California Mastitis Test, Catalase Test, and pH Readings on Quarter Milk Samples  

Microsoft Academic Search

Three representative groups from 611 quarter samples of aseptically collected milk were compared for catalase, pH, and California mastitis test readings. Statistical analysis (determination of correlation coefficient) was applied to 102 of the 611 quarter samples. It was found that the correlation coefficient for catalase and pH reading was more significant than the correlation coefficient of the catalase and CMT

C. T. Raby; P. L. Hubbard; R. H. Cobbins

1967-01-01

188

Maturation of Catalase Precursor Proceeds to a Different Extent in Glyoxysomes and Leaf Peroxisomes of Pumpkin Cotyledons  

Microsoft Academic Search

As an approach to study the mechanism of the microbody transition (glyoxysomes to leaf peroxisomes) in greening pumpkin cotyledons, catalase molecules were purified from the two different types of microbody and their structural properties were compared. The purified glyoxysomal catalase was found to consist of four identical subunits (55 kDa), whereas the leaf peroxisomal catalase contains two different forms of

Junji Yamaguchi; Mikio Nishimura; Takashi Akazawa

1984-01-01

189

Hydroperoxide determination by a catalase OPEE: application to the study of extra virgin olive oil rancidification process  

Microsoft Academic Search

A new application to authentic matrices of a catalase organic phase enzyme electrode (OPEE) recently developed by the present authors is described in this communication. This biosensor was obtained by coupling an amperometric gas diffusion electrode for the oxygen, made of teflon, and the catalase enzyme immobilised in kappa-carrageenan gel.The response of the catalase biosensor to cumene hydroperoxide and to

L Campanella; M. P Sammartino; M Tomassetti; S Zannella

2001-01-01

190

Red-Cell Catalase and the Production of Methaemoglobin, Heinz Bodies and Changes in Osmotic Fragility due to Drugs  

Microsoft Academic Search

Heinz bodies were produced in vitroin normal human red cells by incubation with ascorbic acid, menadione, sodium azide, primaquine diphosphate, acetyl phenylhydrazine, potassium chlorate, sodium nitrite and p-phenetidine. All compounds causing Heinz body formation also produced methaemoglobin, and most led to reduction in catalase activity; sodium nitrite and p-phenetidine caused no inhibition of catalase. Catalase inhibition was not found with

G. R. Tudhope; Sandra P. Leece

1971-01-01

191

Enhanced stability of catalase covalently immobilized on functionalized titania submicrospheres.  

PubMed

In this study, a novel approach combing the chelation and covalent binding was explored for facile and efficient enzyme immobilization. The unique capability of titania to chelate with catecholic derivatives at ambient conditions was utilized for titania surface functionalization. The functionalized titania was then used for enzyme immobilization. Titania submicrospheres (500-600 nm) were synthesized by a modified sol-gel method and functionalized with carboxylic acid groups through a facile chelation method by using 3-(3,4-dihydroxyphenyl) propionic acid as the chelating agent. Then, catalase (CAT) was covalently immobilized on these functionalized titania submicrospheres through 1-ethyl-3-[3-dimethylaminopropyl] carbodiimide hydrochloride/N-hydroxysuccinimide (EDC/NHS) coupling reaction. The immobilized CAT retained 65% of its free form activity with a loading capacity of 100-150 mg/g titania. The pH stability, thermostability, recycling stability and storage stability of the immobilized CAT were evaluated. A remarkable enhancement in enzyme stability was achieved. The immobilized CAT retained 90% and 76% of its initial activity after 10 and 16 successive cycles of decomposition of hydrogen peroxide, respectively. Both the Km and the Vmax values of the immobilized CAT (27.4 mM, 13.36 mM/min) were close to those of the free CAT (25.7 mM, 13.46 mM/min). PMID:23827593

Wu, Hong; Liang, Yanpeng; Shi, Jiafu; Wang, Xiaoli; Yang, Dong; Jiang, Zhongyi

2012-12-22

192

The Genetics of Catalase in Drosophila Melanogaster: Isolation and Characterization of Acatalasemic Mutants  

PubMed Central

Activated oxygen species have been demonstrated to be the important agents in oxygen toxicity by disrupting the structural and functional integrity of cells through lipid peroxidation events, DNA damage and protein inactivation. The biological consequences of free radical damage have long been hypothesized to be a causal agent in many aging-related diseases. Catalase (H(2)O(2):H(2)O(2) oxidoreductase; EC 1.15.1.1) is one of several enzymes involved in the scavenging of oxygen free radicals and free radical derivatives. The structural gene for catalase in Drosophila melanogaster has been localized to region 75D1-76A on chromosome 3L by dosage responses to segmental aneuploidy. This study reports the isolation of a stable deficiency, Df(3L)Cat(DH104)(75C1-2;75F1), that uncovers the catalase locus and the subsequent isolation of six acatalasemic mutants. All catalase mutants are viable under standard culture conditions and recessive lethal mutations within the 75C1-F1 interval have been shown not to affect catalase activity. Two catalase mutations are amorphic while four are hypomorphic alleles of the Cat(+) locus. The lack of intergenic complementation between the six catalase mutations strongly suggests that there is only one functional gene in Drosophila. One acatalesemic mutation was mapped to position 3-47.0 which resides within the catalase dosage sensitive region. While complete loss of catalase activity confers a severe viability effect, residual levels are sufficient to restore viability to wild type levels. These results suggest a threshold effect for viability and offer an explanation for the general lack of phenotypic effects associated with the known mammalian acatalasemics.

Mackay, W. J.; Bewley, G. C.

1989-01-01

193

Adsorption Kinetics of Catalase to Thin-Films of Carbon Nanotubes  

PubMed Central

The adsorption conditions used to immobilize catalase onto thin-films of carbon nanotubes were investigated to elucidate the conditions that produced films with maximum amounts of active catalase. The adsorption kinetics were monitored by spectroscopic ellipsometry and the immobilized catalase films were then assayed for catalytic activity. The development of a volumetric optical model used to interpret the ellipsometric data is discussed. According to the results herein discussed, not only the adsorbed amount but also the initial adsorption rates determine the final catalytic activity of the adsorbed layer. The results described in the manuscript have direct implications on the rational design and analytical performance of enzymatic biosensors.

Felhofer, Jessica L.; Caranto, Jonathan D.; Garcia, Carlos D.

2010-01-01

194

Serological, Taxonomic, and Kinetic Studies of the T and M Classes of Mycobacterial Catalase  

Microsoft Academic Search

Two types of catalase may be found in extracts of mycobacteria, the heat-labile T class and the heat-stable M class. The T-catalase is resistant to 3-amino-1,2,4- triazole and has a Michaelis constant in the range of 3.1 to 6.8 mM H202, whereas the M-catalase is inhibited by 3-amino-l,2,4-triazole and has a Michaelis constant in the range of 143 to 156

LAWRENCE G. WAYNE; GILBERT A. DIAZ

195

Reversible immobilization of catalase on fibrous polymer grafted and metal chelated chitosan membrane  

Microsoft Academic Search

Poly(itaconic acid) grafted and\\/or Fe(III) ions incorporated chitosan membranes were used for reversible immobilization of catalase (from bovine liver) via adsorption. The influences of pH and initial catalase concentration on the immobilization capacities of the CH-g-poly(IA) and CH-g-poly(IA)-Fe(III) membranes have been investigated in a batch system. Maximum catalase adsorption onto CH-g-poly(IA) and CH-g-poly(IA)-Fe(III) membrane were found to be 6.3 and

Gulay Bayramoglu; M. Yakup Arica

2010-01-01

196

Thermal stability of catalases active in dormant saffron (Crocus sativus L.) corms.  

PubMed

Catalase activity was detected in crude extract prepared from dormant saffron (Crocus sativus L.) corms. The activity was independent of pH in the range 6.0-11.0. Thermostability studies suggested the presence of three isoenzymes with transition temperatures of 30 degrees C, 45 degrees C and 60 degrees C, respectively, as given by Arrhenius plots. When stained for catalase activity gel electropherograms of extract revealed 3 distinct bands with apparent molecular weight of 323,000, 295,000 and 268,000, respectively. Thus it appeared that at least three isoenzymes of catalase were present in dormant saffron corms. PMID:12241041

Keyhani, J; Keyhani, E; Kamali, J

2002-01-01

197

Rapid formation of compound II and a tyrosyl radical in the Y229F mutant of Mycobacterium tuberculosis catalase-peroxidase disrupts catalase but not peroxidase function.  

PubMed

Catalase-peroxidases (KatG), which belong to Class I heme peroxidase enzymes, have high catalase activity and substantial peroxidase activity. The Y229F mutant of Mycobacterium tuberculosis KatG was prepared and characterized to investigate the functional role of this conserved residue unique to KatG enzymes. Purified, overexpressed KatG[Y229F] exhibited severely reduced steady-state catalase activity while the peroxidase activity was enhanced. Optical stopped-flow experiments showed rapid formation of Compound (Cmpd) II (oxyferryl heme intermediate) in the reaction of resting KatG[Y229F] with peroxyacetic acid or chloroperoxybenzoic acid, without detectable accumulation of Cmpd I (oxyferryl heme pi-cation radical intermediate), the latter being readily observed in the wild-type enzyme under similar conditions. Facile formation of Cmpd III (oxyferrous enzyme) also occurred in the mutant in the presence of micromolar hydrogen peroxide. Thus, the lost catalase function may be explained in part because of formation of intermediates that do not participate in catalatic turnover. The source of the reducing equivalent required for generation of Cmpd II from Cmpd I was shown by rapid freeze-quench electron paramagnetic resonance spectroscopy to be a tyrosine residue, just as in wild-type KatG. The kinetic coupling of radical generation and Cmpd II formation was shown in KatG[Y229F]. Residue Y229, which is a component of a newly defined three amino acid adduct in catalase-peroxidases, is critically important for protecting the catalase activity of KatG. PMID:12944408

Yu, Shengwei; Girotto, Stefania; Zhao, Xiangbo; Magliozzo, Richard S

2003-08-27

198

High resistance to oxidative damage in the Antarctic midge Belgica antarctica, and developmentally linked expression of genes encoding superoxide dismutase, catalase and heat shock proteins.  

PubMed

Intense ultraviolet radiation, coupled with frequent bouts of freezing-thawing and anoxia, have the potential to generate high levels of oxidative stress in Antarctic organisms. In this study, we examined mechanisms used by the Antarctic midge, Belgica antarctica, to counter oxidative stress. We cloned genes encoding two key antioxidant enzymes, superoxide dismutase (SOD) and catalase (Cat), and showed that SOD mRNA was expressed continuously and at very high levels in larvae, but not in adults, while Cat mRNA was expressed in both larvae and adults but at a somewhat reduced level. SOD mRNA was expressed at even higher levels in larvae that were exposed to direct sunlight. Catalase, a small heat shock protein, Hsp70 and Hsp90 mRNAs were also strongly upregulated in response to sunlight. Total antioxidant capacity of the adults was higher than that of the larvae, but levels in both stages of the midge were much higher than observed in a freeze-tolerant, temperate zone insect, the gall fly Eurosta solidaginis. Assays to measure oxidative damage (lipid peroxidation TBARS and carbonyl proteins) demonstrated that the Antarctic midge is highly resistant to oxidative stress. PMID:18625403

Lopez-Martinez, Giancarlo; Elnitsky, Michael A; Benoit, Joshua B; Lee, Richard E; Denlinger, David L

2008-07-02

199

A synthetic superoxide dismutase/catalase mimetic EUK-207 mitigates radiation dermatitis and promotes wound healing in irradiated rat skin.  

PubMed

In the event of a radionuclear attack or nuclear accident, the skin would be the first barrier exposed to radiation, though skin injury can progress over days to years following exposure. Chronic oxidative stress has been implicated as being a potential contributor to the progression of delayed radiation-induced injury to skin and other organs. To examine the causative role of oxidative stress in delayed radiation-induced skin injury, including impaired wound healing, we tested a synthetic superoxide dismutase (SOD)/catalase mimetic, EUK-207, in a rat model of combined skin irradiation and wound injury. Administered systemically, beginning 48?hours after irradiation, EUK-207 mitigated radiation dermatitis, suppressed indicators of tissue oxidative stress, and enhanced wound healing. Evaluation of gene expression in irradiated skin at 30 days after exposure revealed a significant upregulation of several key genes involved in detoxication of reactive oxygen and nitrogen species. This gene expression pattern was primarily reversed by EUK-207 therapy. These results demonstrate that oxidative stress has a critical role in the progression of radiation-induced skin injury, and that the injury can be mitigated by appropriate antioxidant compounds administered 48?hours after exposure. PMID:23190879

Doctrow, Susan R; Lopez, Argelia; Schock, Ashley M; Duncan, Nathan E; Jourdan, Megan M; Olasz, Edit B; Moulder, John E; Fish, Brian L; Mäder, Marylou; Lazar, Jozef; Lazarova, Zelmira

2012-11-29

200

A synthetic superoxide dismutase/catalase mimetic EUK-207 mitigates radiation dermatitis and promotes wound healing in irradiated rat skin  

PubMed Central

In the event of a radionuclear attack or nuclear accident, the skin would be the first barrier exposed to radiation, though skin injury can progress over days to years following exposure. Chronic oxidative stress has been implicated as being a potential contributor to the progression of delayed radiation-induced injury to skin and other organs. To examine the causative role of oxidative stress in delayed radiation-induced skin injury, including impaired wound healing, we tested a synthetic superoxide dismutase (SOD)/catalase mimetic, EUK-207, in a rat model of combined skin irradiation and wound injury. Administered systemically, beginning 48 h after irradiation, EUK-207 mitigated radiation dermatitis, suppressed indicators of tissue oxidative stress, and enhanced wound healing. Evaluation of gene expression in irradiated skin at 30 days after exposure revealed a significant upregulation of several key genes involved in detoxication of reactive oxygen and nitrogen species. This gene expression pattern was primarily reversed by EUK-207 therapy. These results demonstrate that oxidative stress plays a critical role in the progression of radiation-induced skin injury, and that the injury can be mitigated by appropriate antioxidant compounds administered 48 h after exposure.

Doctrow, Susan R.; Lopez, Argelia; Schock, Ashley M.; Duncan, Nathan E.; Jourdan, Megan M.; Olasz, Edit B.; Moulder, John E.; Fish, Brian L.; Mader, Marylou; Lazar, Jozef; Lazarova, Zelmira

2012-01-01

201

Serum adenosine deaminase, catalase and carbonic anhydrase activities in patients with bladder cancer  

PubMed Central

OBJECTIVES: The relationship between adenosine deaminase and various cancers has been investigated in several studies. However, serum adenosine deaminase activity and carbonic anhydrase and catalase activities in patients with bladder cancer have not previously been reported. Therefore, the aim of this study was to measure serum adenosine deaminase, carbonic anhydrase and catalase activities in patients with bladder cancer. MATERIALS AND METHODS: Forty patients with bladder cancer and 30 healthy controls were enrolled in the study. Serum adenosine deaminase, carbonic anhydrase and catalase activities were measured spectrophotometrically. RESULTS: Serum adenosine deaminase, carbonic anhydrase and catalase activities were significantly higher in patients with bladder cancer than controls (all significant, p<0.001). CONCLUSIONS: These markers might be a potentially important finding as an additional diagnostic biochemical tool for bladder cancer.

Pirincci, Necip; Gecit, Ilhan; Gunes, Mustafa; Bilgehan Y?ksel, Mehmet; Kaba, Mehmet; Tan?k, Serhat; Demir, Halit; Aslan, Mehmet

2012-01-01

202

Studies of Peroxide Deactivation and Glucose Removal with Immobilized Glucose Oxidase and Catalase.  

National Technical Information Service (NTIS)

A series of studies using immobilized glucose oxidase and catalase in a continuous flow, tubular, packed bed reactor have been performed. The studies were aimed at developing an immobilized enzyme system for the desugaring of eggs. Quantitative expression...

R. E. Altomare

1974-01-01

203

A Simple Method for Demonstrating Enzyme Kinetics Using Catalase from Beef Liver Extract  

NASA Astrophysics Data System (ADS)

This paper describes a simple visual method of demonstrating enzyme kinetics using beef liver catalase. A catalase solution is obtained by homogenizing beef liver in a phosphate buffer. In the demonstration, filter paper is saturated with beef liver extract and placed into a solution of hydrogen peroxide. The catalase in the extract decomposes the hydrogen peroxide to water and oxygen. Oxygen forms on the filter paper, and the filter paper rises to the top of the beaker. Catalase activity is measured by timing the rise of the enzyme-soaked filter paper to the top of beakers containing different concentrations of hydrogen peroxide. The data are plotted as a Lineweaver-Burk double-reciprocal plot, and the Km and Vmax for the reaction are calculated.

Johnson, Kristin A.

2000-11-01

204

Catalase and Superoxide Dismutase of Root-Colonizing Saprophytic Fluorescent Pseudomonads.  

National Technical Information Service (NTIS)

Increased specific activities of catalase but not superoxide dismutase were observed during growth of these bacteria on components washed from root surfaces. The specific activities of both enzymes were also regulated during contact of these bacteria with...

J. Katsuwon A. J. Anderson

1990-01-01

205

Occurrence of High Catalase-containing Acinetobacter in Spacecraft Assembly Facilities  

NASA Astrophysics Data System (ADS)

In summary, the measurement of high catalase specific activity values for spacecraft-associated Acinetobacter strains is potentially the result of adaptation towards the harsh conditions of the clean rooms and assembly process.

McCoy, K. B.; Derecho, I.; La Duc, M. T.; Vaishampayan, P.; Venkateswaran, K. J.; Mogul, R.

2010-04-01

206

Spectroscopic study on the interaction of catalase with bifendate and analogs  

NASA Astrophysics Data System (ADS)

The interactions of bifendate (DDB) or analogs (Bicyclol, I, II and III) with catalase are analyzed by spectrophotometric methods. The fluorescence spectra results show the intrinsic fluorescence of catalase is strongly quenched by DDB or analogs with a static quenching procedure. The binding constants are obtained at three temperatures. The thermodynamics parameters (?H, ?S, ?G) indicate the hydrophobic and electrostatic interactions play a major role in the interaction. The results of synchronous fluorescence, UV-vis absorption and three-dimensional fluorescence spectra demonstrate that the microenvironments of Trp residue of catalase are disturbed by the analogs. Thermodynamic results showed that DDB is the strongest quencher and bind to catalase with the highest affinity among five compounds.

Wang, Ruiqiang; Zhang, Lu; Wang, Rui; Dou, Huanjing; Li, Hua; Wang, Yi; Pu, Juanjuan; Wang, Ruiyong

2013-02-01

207

Effects of Inflammation on Peroxisomal Enzyme Activity, Catalase Synthesis and Lipid Metabolism.  

National Technical Information Service (NTIS)

The activity of hepatic peroxisomal enzymes, catalase, urate oxidase, D-amino acid oxidase, hydroxy acid oxidase, and carnitine acetyltransferase were serially measured following a turpentine-induced sterile inflammatory lesion in rats. The ensuing depres...

P. G. Canonico W. Rill E. Ayala

1977-01-01

208

Two divergent catalase genes are differentially regulated during Aspergillus nidulans development and oxidative stress.  

PubMed

Catalases are ubiquitous hydrogen peroxide-detoxifying enzymes that are central to the cellular antioxidant response. Of two catalase activities detected in the fungus Aspergillus nidulans, the catA gene encodes the spore-specific catalase A (CatA). Here we characterize a second catalase gene, identified after probing a genomic library with catA, and demonstrate that it encodes catalase B. This gene, designated catB, predicts a 721-amino-acid polypeptide (CatB) showing 78% identity to an Aspergillus fumigatus catalase and 61% identity to Aspergillus niger CatR. Notably, similar levels of identity are found when comparing CatB to Escherichia coli catalase HPII (43%), A. nidulans CatA (40%), and the predicted peptide of a presumed catA homolog from A. fumigatus (38%). In contrast, the last two peptides share a 79% identity. The catalase B activity was barely detectable in asexual spores (conidia), disappeared after germination, and started to accumulate 10 h after spore inoculation, throughout growth and conidiation. The catB mRNA was absent from conidia, and its accumulation correlated with catalase activity, suggesting that catB expression is regulated at the transcription level. In contrast, the high CatA activity found in spores was lost gradually during germination and growth. In addition to its developmental regulation, CatB was induced by H2O2, heat shock, paraquat, or uric acid catabolism but not by osmotic stress. This pattern of regulation and the protective role against H2O2 offered by CatA and CatB, at different stages of the A. nidulans life cycle, suggest that catalase gene redundancy performs the function of satisfying catalase demand at the two different stages of metabolic and genetic regulation represented by growing hyphae versus spores. Alternative H2O2 detoxification pathways in A. nidulans were indicated by the fact that catA/catB double mutants were able to grow in substrates whose catabolism generates H2O2. PMID:9150225

Kawasaki, L; Wysong, D; Diamond, R; Aguirre, J

1997-05-01

209

Expression and functional characterization of Helicobacter pylori catalase from baculovirus-infected insect cells  

Microsoft Academic Search

The catalase katA gene of Helicobacter pylori encodes an antioxidant enzyme to protect the bacteria from environmental toxic oxygen species. In this study, the baculovirus-insect cell expression system was used to express the full-length katA gene from the Taiwanese H. pylori TW-34 strain. Three lipidopteran insect cell lines (Sf9, Sf21, High5) were evaluated to produce the recombinant catalase (KatA) using

Suh-Chin Wu; Haimei Huang; Chih-Chien Lin

2004-01-01

210

Effect of dose and dose rate of gamma radiation on catalytic activity of catalase  

Microsoft Academic Search

Catalytic activity of gamma irradiated catalase from bovine liver was studied for hydrogen peroxide decomposition at constant\\u000a temperature and pressure. The measurement was performed at temperatures 27, 32, 37, 42 and 47 °C. Solutions containing 1 and\\u000a 0.01 g dm?3 of catalase in phosphate buffer were used for the study. Repeatability of both sample preparation and kinetics measurement\\u000a was experimentally verified. Rate

Václav ?uba; Tereza Pavelková; Viliam Mú?ka

2010-01-01

211

Brain catalase activity is highly correlated with ethanol-induced locomotor activity in mice  

Microsoft Academic Search

It has been demonstrated that acute administration of lead to mice enhances brain catalase activity and ethanol-induced locomotion. These effects of lead seem to be related, since they show similar time courses and occur at similar doses. In the present study, in an attempt to further evaluate the relation between brain catalase activity and lead-induced changes in ethanol-stimulated locomotion, the

Mercè Correa; Carles Sanchis-Segura; Carlos M. G. Aragon

2001-01-01

212

Catalase deficiency reduces survival and pleiotropically affects agronomic performance in field-grown barley progeny  

Microsoft Academic Search

Field-grown plants of the catalase-deficient mutant RPr79\\/4 show necrotic lesions in leaves and preferentially die. Initially, necrotic lesions exhibited by RPr79\\/4 were used to indirectly assess the role of distinct levels of catalase on the survival and agronomic performance of field-grown barley progeny. The segregation of three control traits was also analyzed to eliminate the influence of any obvious meiotic

Alberto Acevedo; Antonio D??az Paleo; Mar??a Laura Federico

2001-01-01

213

Use of a simple catalase assay for assessment of aerobic microbial contamination on vegetables  

Microsoft Academic Search

This paper presents a rapid catalase test for monitoring the aerobic microbial contamination associated with vegetables. The\\u000a microbial loads of celery, bell pepper and ready-to-eat salad were serially tested over a 2-week period under common storage\\u000a conditions. At each time point, samples were surface-sampled for catalase activity with a Pasteur pipette method in 5 min.\\u000a Simultaneously, the aerobic viable microbial counts

Rebecca J. Ye; Vivian C. H. Wu

2011-01-01

214

The circadian clock gates expression of two Arabidopsis catalase genes to distinct and opposite circadian phases  

Microsoft Academic Search

InArabidopsis thaliana, catalase is encoded by a small gene family. We have characterized cDNA and genomic clones containing theArabidopsis catalase geneCAT3, present as a single copy in the nuclear genome. Six introns were identified in theCAT3 coding region and two transcription start sites have been been mapped by primer extension. The deduced amino acid sequence of CAT3 is highly similar

H. H. Zhong; C. R. McClung

1996-01-01

215

Layer-by-layer assembled multilayers using catalase-encapsulated gold nanoparticles  

Microsoft Academic Search

We introduce a novel and versatile approach for the preparation of multilayers, based on catalase-encapsulated gold nanoparticles (CAT-AuNP), allowing electrostatic charge reversal and structural transformation through pH adjustment. CAT-AuNP, which are synthesized directly from CAT stabilizer, can be electrostatically assembled with anionic and cationic PEs as a result of the charge reversal of the catalase stabilizers through pH control. In

Sungwoo Kim; Jinhan Cho

2010-01-01

216

Separation and characterization of two catalase activities isolated from the yeast Trigonopsis variabilis  

Microsoft Academic Search

Two different catalases present in cell-free extracts of the yeast Trigonopsis variabilis have been separated by dye-binding chromatography. Both enzymes, named TvC-I and TvC-II, behave as members of the “typical catalases” family: they have a broad pH activity profile and do not possess peroxidase activity, are quite stable when treated with ethanol\\/chloroform mixtures, are inhibited by azide and cyanide at

Daniela Monti; Eva Baldaro; Sergio Riva

2003-01-01

217

Purification and Characterization of a Homodimeric Catalase-Peroxidase from the Cyanobacterium Anacystis nidulans  

Microsoft Academic Search

Cytosolic extracts of the cyanobacteriumAnacystis nidulansexhibit both catalase and o-dianisidine peroxidase activity. Native polyacrylamide gel electrophoresis demonstrates one distinct enzyme, which has been purified to essential homogeneity and found to be composed of two identical subunits of equal size (80.5 kDa). The isoelectric point is at pH 4.7. It is a very efficient catalase with a broad pH optimum between

C. Obinger; G. Regelsberger; G. Strasser; U. Burner; G. A. Peschek

1997-01-01

218

Ethanol intake and motor sensitization: the role of brain catalase activity in mice with different genotypes  

Microsoft Academic Search

The C57BL\\/6J strain of inbred mice shows a characteristic pattern of ethanol-induced behaviors: very weak acute locomotor stimulation, a lack of locomotor-sensitizing effect of ethanol, and a high level of ethanol intake. This strain has relatively low levels of activity of the ethanol metabolizing enzyme catalase, and it has been proposed that brain catalase plays a role in the modulation

M. Correa; C. Sanchis-Segura; R. Pastor; C. M. G. Aragon

2004-01-01

219

Selection of biochemical mutants of Aspergillus niger with enhanced catalase production  

Microsoft Academic Search

The production of extracellular catalase in a submerged culture by a number of biochemical mutants has been evaluated. Eight\\u000a of these mutants showed increased extracellular catalase, the level of which ranged widely in individual cases from 44% to\\u000a over 94% in comparison with the parental strain. Studies of the relationship between a criterion of selection and the frequency\\u000a of mutation

J. Fiedurek; A. Gromada

1997-01-01

220

Catalase inhibition in the Arcuate nucleus blocks ethanol effects on the locomotor activity of rats  

Microsoft Academic Search

Previous studies have demonstrated that there is a bidirectional modulation of ethanol-induced locomotion produced by drugs that regulate brain catalase activity. In the present study we have assessed the effect in rats of intraperitoneal, intraventricular or intracraneal administration of the catalase inhibitor sodium azide in the locomotor changes observed after ethanol (1g\\/kg) administration. Our results show that sodium azide prevents

Carles Sanchis-Segura; Mercé Correa; Marta Miquel; Carlos M. G. Aragon

2005-01-01

221

Effects of autogamy in Paramecium tetraurelia on catalase activity and on radiosensitivity to natural ionizing radiations  

SciTech Connect

Catalase activity of Paramecium tetraurelia decreased during autogamy and recovered to normal 5 days later. Autogamy also caused changes in the ciliate's sensitivity sensitivity to natural ionizing radiations - the decrease in cell growth rate previously described in shielded cultures did not occur when autogamous cells were used. Maximum effect of shielding was observed in 11-day-old postautogamous cells. The role of the catalase in the mechanism of natural irradiation effect is discussed.

Croute, F.; Dupouy, D.; Charley, J.P.; Soleilhavoup, J.P.; Planel, H.

1980-02-01

222

Impact of sodium cyanide on catalase activity in the freshwater exotic carp, Cyprinus carpio (Linnaeus)  

Microsoft Academic Search

The Cyprinus carpio fingerlings on exposure to lethal (1mg\\/L) and sub lethal concentrations (0.066mg\\/L) of sodium cyanide showed inhibition in the activity of catalase. The disruption of catalase activity in freshwater fish, C. carpio is demonstrated in the present study using UV–visible spectrophotometer at 240nm using hydrogen peroxide as a substrate. It suggests toxic effects of sodium cyanide and consequent

Muniswamy David; Vadingadu Munaswamy; Ramesh Halappa; Shambangouda R. Marigoudar

2008-01-01

223

Transient Overexpression of Catalase Does Not Inhibit TNF or PMA-Induced NF-?B Activation  

Microsoft Academic Search

H2O2 has been proposed as a second messenger involved in cell signaling for NF-?B activation. In the present study, this hypothesis was tested by transiently overexpressing catalase, a specific scavenger of H2O2, in COS-1 cells. A mammalian expression vector was constructed by incorporating catalase gene from pCAT10 clone into the unique EcoRI site of the pSG5 vector which contains the

Y. J. Suzuki; M. Mizuno; L. Packer

1995-01-01

224

Cardiac overexpression of antioxidant catalase attenuates aging-induced cardiomyocyte relaxation dysfunction  

Microsoft Academic Search

Catalase, an enzyme which detoxifies H2O2, may interfere with cardiac aging. To test this hypothesis, contractile and intracellular Ca2+ properties were evaluated in cardiomyocytes from young (3–4 months) and old (26–28 months) FVB and transgenic mice with cardiac overexpression of catalase. Contractile indices analyzed included peak shortening (PS), time-to-90% PS (TPS90), time-to-90% relengthening (TR90), half-width duration (HWD), maximal velocity of

Jun Ren; Qun Li; Shan Wu; Shi-Yan Li; Sara A. Babcock

2007-01-01

225

Utilization of methanol by a catalase-negative mutant of Hansenula polymorpha  

Microsoft Academic Search

In methanol-utilizing yeasts, catalase is an essential enzyme for the destruction of hydrogen peroxide generated by methanol oxidase (E.C. 1.1.3.13). It was found however that a catalase-negative mutant of Hansenula polymorpha is able to consume methanol in the presence of glucose in continuous cultures. At a dilution rate of 0.1 h-1, stable continuous cultures could be obtained during growth on

Marco L. F. Giuseppin; Hendrikus M. J. van Eijk; Annemieke Bos; Cornelis Verduyn

1988-01-01

226

Promoter Variant in the Catalase Gene Is Associated with Vitiligo in Chinese People  

Microsoft Academic Search

Vitiligo is an acquired depigmentation disorder, and reactive oxygen species have an important role in the physiology of cell damage. Reduced catalase enzyme activity and accumulation of excessive hydrogen peroxide have been observed in vitiligo. In a hospital-based case–control study of vitiligo patients (n=749) and age- and sex-matched healthy controls (n=763), we investigated three catalase (CAT) gene polymorphisms (?89A>T, 389C>T,

Ling Liu; Chunying Li; Jian Gao; Kai Li; Rui Zhang; Gang Wang; Chenxin Li; Tianwen Gao

2010-01-01

227

Immunocytochemical investigation of catalase and peroxisomal lipid ?-oxidation enzymes in human hepatocellular tumors and liver cirrhosis  

Microsoft Academic Search

A significant reduction of catalase activity, a peroxisomal marker enzyme, occurs in human hepatic neoplasias, but no information\\u000a is available on other peroxisomal proteins. We have studied by means of immunohistochemistry four specific proteins of peroxisomes\\u000a (catalase and three enzymes of lipid ?-oxidation) in human hepatocellular tumors of various differentiation grades from adenoma\\u000a to anaplastic carcinoma. In all tumors, except

Jan A. Litwin; Konstantin Beier; Alfred Völkl; Walter J. Hofmann; H. Dariush Fahimi

1999-01-01

228

Effect of the embryo axis on catalase in the endosperm of germinating castor bean seeds  

Microsoft Academic Search

The effect of the embryo axis on the activity of the glyoxysomal enzyme catalase (EC 1.11.1.6) in the endosperm of germinating castor bean (Ricinus communis L. cv. Hale) seeds was examined. The presence of the embryo axis was required for maximum levels of catalase enzyme activity and protein levels in cell-free extracts of endosperms from germinated seeds. In contrast, RNA

Robert T Mullen; David J Gifford

1995-01-01

229

Catalase: A Tetrameric Enzyme with Four Tightly Bound Molecules of NADPH  

Microsoft Academic Search

Catalases (H2O2:H2O2 oxidoreductase, EC 1.11.1.6) from many species are known to be tetramers of 60,000-dalton subunits, with four heme groups per tetramer. Previous authors have determined the amino acid sequence and three-dimensional structure of bovine liver catalase. Studies of the regulation of the pentose phosphate pathway led the present authors to a search for proteins that bind NADP+ and NADPH

Henry N. Kirkman; Gian F. Gaetani

1984-01-01

230

Purification, characterization, and identification of a novel bifunctional catalase-phenol oxidase from Scytalidium thermophilum.  

PubMed

A novel bifunctional catalase with an additional phenol oxidase activity was isolated from a thermophilic fungus, Scytalidium thermophilum. This extracellular enzyme was purified ca. 10-fold with 46% yield and was biochemically characterized. The enzyme contains heme and has a molecular weight of 320 kDa with four 80 kDa subunits and an isoelectric point of 5.0. Catalase and phenol oxidase activities were most stable at pH 7.0. The activation energies of catalase and phenol oxidase activities of the enzyme were found to be 2.7 +/- 0.2 and 10.1 +/- 0.4 kcal/mol, respectively. The pure enzyme can oxidize o-diphenols such as catechol, caffeic acid, and L-DOPA in the absence of hydrogen peroxide and the highest oxidase activity is observed against catechol. No activity is detected against tyrosine and common laccase substrates such as ABTS and syringaldazine with the exception of weak activity with p-hydroquinone. Common catechol oxidase inhibitors, salicylhydroxamic acid and p-coumaric acid, inhibit the oxidase activity. Catechol oxidation activity was also detected in three other catalases tested, from Aspergillus niger, human erythrocyte, and bovine liver, suggesting that this dual catalase-phenol oxidase activity may be a common feature of catalases. PMID:18369615

Sutay Kocabas, Didem; Bakir, Ufuk; Phillips, Simon E V; McPherson, Michael J; Ogel, Zumrut B

2008-03-28

231

Redundant catalases detoxify phagocyte reactive oxygen and facilitate Histoplasma capsulatum pathogenesis.  

PubMed

Histoplasma capsulatum is a respiratory pathogen that infects phagocytic cells. The mechanisms allowing Histoplasma to overcome toxic reactive oxygen molecules produced by the innate immune system are an integral part of Histoplasma's ability to survive during infection. To probe the contribution of Histoplasma catalases in oxidative stress defense, we created and analyzed the virulence defects of mutants lacking CatB and CatP, which are responsible for extracellular and intracellular catalase activities, respectively. Both CatB and CatP protected Histoplasma from peroxide challenge in vitro and from antimicrobial reactive oxygen produced by human neutrophils and activated macrophages. Optimal protection required both catalases, as the survival of a double mutant lacking both CatB and CatP was lower than that of single-catalase-deficient cells. Although CatB contributed to reactive oxygen species defenses in vitro, CatB was dispensable for lung infection and extrapulmonary dissemination in vivo. Loss of CatB from a strain also lacking superoxide dismutase (Sod3) did not further reduce the survival of Histoplasma yeasts. Nevertheless, some catalase function was required for pathogenesis since simultaneous loss of both CatB and CatP attenuated Histoplasma virulence in vivo. These results demonstrate that Histoplasma's dual catalases comprise a system that enables Histoplasma to efficiently overcome the reactive oxygen produced by the innate immune system. PMID:23589579

Holbrook, Eric D; Smolnycki, Katherine A; Youseff, Brian H; Rappleye, Chad A

2013-04-15

232

Double antisense plants lacking ascorbate peroxidase and catalase are less sensitive to oxidative stress than single antisense plants lacking ascorbate peroxidase or catalase  

Microsoft Academic Search

Summary The plant genome is a highly redundant and dynamic genome. Here, we show that double antisense plants lacking the two major hydrogen peroxide-detoxifying enzymes, ascorbate peroxidase (APX) and catalase (CAT), activate an alternative\\/redundant defense mechanism that compensates for the lack of APX and CAT. A similar mechanism was not activated in single antisense plants that lacked APX or CAT,

Ludmila Rizhsky; Elza Hallak-Herr; Frank Van Breusegem; Shimon Rachmilevitch; Jason E. Barr; Steven Rodermel; Dirk Inzé; Ron Mittler

2002-01-01

233

[Kinetics of catalase inactivation induced by ultrasonic cavitation].  

PubMed

Kinetic patterns of sonication-induced inactivation of bovine liver catalase (CAT) were studied in buffer solutions (pH 4-11) within the temperature range from 36 to 55 degrees C. Solutions of CAT were exposed to low-frequency (20.8 kHz) ultrasound (specific power, 48-62 W/cm2). The kinetics of CAT inactivation was characterized by effective first-order rate constants (s-1) of total inactivation (kin), thermal inactivation (*kin), and ultrasonic inactivation (kin(us)). In all cases, the following inequality was valid: kin > *kin. The value of kin(us) increased with the ultrasound power (range, 48-62 W/cm2) and exhibited a strong dependence on pH of the medium. On increasing the initial concentration of CAT (0.4-4.0 nM), kin(us) decreased. The three rate constants were minimum within the range of pH 6.5-8; their values increased considerably at pH < 6 and pH > 9. At 36-55 degrees C, temperature dependence of kin(us) was characterized by an activation energy (Eact) of 19.7 kcal/mol, whereas the value of Eact for CAT thermoinactivation was equal to 44.2 kcal/mol. Bovine serum and human serum albumins (BSA and HSA, respectively) inhibited sonication-induced CAT inactivation; complete prevention was observed at concentrations above 2.5 micrograms/ml. Dimethyl formamide (DMFA), a scavenger of hydroxyl radicals (HO.), prevented sonication-induced CAT inactivation at 10% (kin and *kin increased with the content of DMFA at concentrations in excess of 3%). The results obtained indicate that free radicals generated in the field of ultrasonic cavitation play a decisive role in the inactivation of CAT, which takes place when its solutions are exposed to low-frequency ultrasound. However, the efficiency of CAT inactivation by the radicals is determined by (1) the degree of association between the enzyme molecules in the reaction medium and (2) the composition thereof. PMID:12722648

Potapovich, M V; Eremin, A N; Metelitsa, D I

234

Purification and Characterization of a Novel Thermo-Alkali-Stable Catalase from Thermus brockianus  

SciTech Connect

A novel thermo-alkali-stable catalase from Thermus brockianus was purified and characterized. The protein was purified from a T. brockianus cell extract in a three-step procedure that resulted in 65-fold purification to a specific activity of 5300 U/mg. The enzyme consisted of four identical subunits of 42.5 kDa as determined by SDS-PAGE and a total molecular mass measured by gel filtration of 178 kDa. The catalase was active over a temperature range from 30 to 94 C and a pH range from 6 to 10, with optimum activity occurring at 90 C and pH 8. At pH 8, the enzyme was extremely stable at elevated temperatures with half-lives of 330 h at 80 C and 3 h at 90 C. The enzyme also demonstrated excellent stability at 70 C and alkaline pH with measured half-lives of 510 h and 360 h at pHs of 9 and 10, respectively. The enzyme had an unusual pyridine hemochrome spectrum and appears to utilize eight molecules of heme c per tetramer rather than protoheme IX present in the majority of catalases studied to date. The absorption spectrum suggested that the heme iron of the catalase was in a 6-coordinate low spin state rather than the typical 5-coordinate high spin state. A Km of 35.5 mM and a Vmax of 20.3 mM/min·mg protein for hydrogen peroxide was measured, and the enzyme was not inhibited by hydrogen peroxide at concentrations up to 450 mM. The enzyme was strongly inhibited by cyanide and the traditional catalase inhibitor 3-amino-1,2,4-triazole. The enzyme also showed no peroxidase activity to peroxidase substrates o-dianisidine and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), a trait of typical monofunctional catalases. However, unlike traditional monofunctional catalases, the T. brockianus catalase was easily reduced by dithionite, a characteristic of catalase-peroxidases. The above properties indicate that this catalase has potential for applications in industrial bleaching processes to remove residual hydrogen peroxide from process streams.

Thompson, Vicki Sue; Schaller, Kastli Dianne; Apel, William Arnold

2003-10-01

235

Tumour suppressor PTEN enhanced enzyme activity of GPx, SOD and catalase by suppression of PI3K/AKT pathway in non-small cell lung cancer cell lines.  

PubMed

Phosphates and tensin homologue deleted on chromosome 10 (PTEN) is a tumour suppressor gene which dephosphorilates phosphoinositol 3,4,5 triphosphates. Therefore PTEN can regulate PI3K/AKT pathway in cells. Because of promoter methylation or gene deletion, PTEN expression is commonly decreased or lost in non-small cell lung cancer (NSCLC) cell lines. Therefore, we hypothesized that PTEN could regulate the activity of superoxide dismutase (CuZnSOD), glutathione peroxidase (GPx) and catalase. We first recreated PTENwt, G129R and G129E expressions in lung cell lines, in which endogenous PTEN expression was not detected. Then, we showed that PTEN could suppress AKT activity by its lipid phosphatase domain. We then examined the effect of recreated PTEN expressions in NSCLC cells. While PTENwt expression caused enhanced activity of SOD, GPx and catalase in transfected cells lines, neither G129R nor G129E expression effected enzyme activities. These results suggest that PTEN can up-regulate SOD, GPx and catalase activity by inhibition of PI3K/AKT pathway in NSCLC cell lines. PMID:22299584

Akca, Hakan; Demiray, Aydin; Aslan, Mutay; Acikbas, Ibrahim; Tokgun, Onur

2012-02-03

236

Transgelin Up-Regulation in Obstructive Nephropathy  

PubMed Central

Fibrosis is a complex and multifactorial process, affecting the structure and compromising the function of several organs. Among those, renal fibrosis is an important pathological change, eventually leading to renal failure. Proteomic analysis of the renal parenchyma in the well-established rat model of unilateral ureteral obstruction (UUO model) suggested that transgelin was up-regulated during the development of fibrosis. Transgelin up-regulation was confirmed both at the protein and at the mRNA level. It was observed that at early stages of fibrosis transgelin was mainly expressed in the interstitial compartment and, more specifically, in cells surrounding the glomeruli. Subsequently, it was confirmed that transgelin expressing cells were activated fibroblasts, based on their extensive co-expression of ?-SMA and their complete lack of co-distribution with markers of other cell types (endothelial, epithelial and cells of the immune system). These periglomerular fibroblasts exhibited staining for transgelin mainly cytoplasmic but occasionally nuclear as well. In addition, transgelin expression in periglomerular fibroblasts was absent in renal fibrosis developed in a hypertensive model, compared to the UUO model. Promoter analysis indicated that there are several conserved motifs for transcription factor binding. Among those, Kruppel-like factor 6 was found to be up-regulated in transgelin positive periglomerular activated fibroblasts, suggesting a possible involvement in the mechanism of transgelin up-regulation. These data strongly suggest that transgelin is up-regulated in the obstructive nephropathy and could be used as a novel marker for renal fibrosis in the future.

Karagianni, Fani; Prakoura, Niki; Kaltsa, Garyfallia; Politis, Panagiotis; Arvaniti, Elena; Kaltezioti, Valeria; Psarras, Stelios; Pagakis, Stamatis; Katsimboulas, Michalis; Abed, Ahmed; Chatziantoniou, Christos; Charonis, Aristidis

2013-01-01

237

Protection of Bacillus larvae from Oxygen Toxicity with Emphasis on the Role of Catalase  

PubMed Central

Sporulation of Bacillus larvae NRRL B-3650 occurred only at aeration rates lower than those used for cultivation of most Bacillus species. One possible explanation for the requirement for a low level of aeration in B. larvae is that toxic forms of oxygen such as H2O2 and superoxide are involved. The superoxide dismutase levels of strain B-3650 were similar to those of Bacillus subtilis 168 during sporulation, and no NADH peroxidase was present. Catalase activity was absent during exponential growth and first appeared near the start of the stationary phase. The catalase activity was 2,700 times less than that in B. subtilis 168 at the same stage of development. Therefore, the relative deficiency of catalase (and NADH peroxidase) might be the cause of the apparent O2 toxicity. It was postulated that B. larvae might accumulate H2O2 in the medium and exhibit more than normal sensitivity to H2O2. Experimental results did not verify either postulate, but the possibilities of intracellular accumulation of H2O2 and unusual sensitivity to endogenous H2O2 were not excluded. The catalase present in early-stationary-phase cells was soluble, heat labile, and inhibited by cyanide, azide, and hydroxylamine. An increase in catalase activity also occurred at the time of appearance of refractile spores in both B. larvae NRRL B-3650 and B. subtilis 168. The level of catalase activity in strain B-3650 was 5,400 times less than that in B. subtilis 168 at this stage. In B. larvae, this second increase occurred primarily within the developing endospore. The activity in spore extracts was particulate, heat stable, and inhibited by hydroxylamine but not by azide or cyanide. Synthesis of catalase in B. larvae was unaffected by H2O2, O2, or glucose.

Dingman, D. W.; Stahly, Donald P.

1984-01-01

238

Cardiac-Specific Overexpression of Catalase Attenuates Lipopolysaccharide-Induced Myocardial Contractile Dysfunction: Role of Autophagy  

PubMed Central

Lipopolysaccharide (LPS) from Gram-negative bacteria is a major initiator of sepsis, leading to cardiovascular collapse. Accumulating evidence has indicated a role of reactive oxygen species (ROS) in cardiovascular complication in sepsis. This study was designed to examine the effect of cardiac-specific overexpression of catalase in LPS-induced cardiac contractile dysfunction and the underlying mechanism(s) with a focus on autophagy. Catalase transgenic and wild-type FVB mice were challenged with LPS (6 mg/kg) and cardiac function was evaluated. Levels of oxidative stress, autophagy, apoptosis and protein damage were examined using fluorescence microscopy, Western blot, TUNEL assay, caspase-3 activity and carbonyl formation. Kaplan-Meier curve was constructed for survival following LPS treatment. Our results revealed a lower mortality in catalase mice compared with FVB mice following LPS challenge. LPS injection led to depressed cardiac contractile capacity as evidenced by echocardiography and cardiomyocyte contractile function, the effect of which was ablated by catalase overexpression. LPS treatment induced elevated TNF-? level, autophagy, apoptosis (TUNEL, caspase-3 activation, cleaved caspase-3), production of ROS and O2?, and protein carbonyl formation, the effects of which were significantly attenuated by catalase overexpression. Electron microscopy revealed focal myocardial damage characterized by mitochondrial injury following LPS treatment, which was less severe in catalase mice. Interestingly, LPS-induced cardiomyocyte contractile dysfunction was prevented by antioxidant NAC and the autophagy inhibitor 3-methyladenine. Taken together, our data revealed that catalase protects against LPS-induced cardiac dysfunction and mortality, which may be associated with inhibition of oxidative stress and autophagy.

Turdi, Subat; Han, Xuefeng; Huff, Anna F.; Roe, Nathan D.; Hu, Nan; Gao, Feng; Ren, Jun

2012-01-01

239

Cardiac Overexpression of Antioxidant Catalase Attenuates Aging-Induced Cardiomyocyte Relaxation Dysfunction  

PubMed Central

Catalase, an enzyme which detoxifies H2O2, may interfere with cardiac aging. To test this hypothesis, contractile and intracellular Ca2+ properties were evaluated in cardiomyocytes from young (3–4 mo) and old (26–28 mo) FVB and transgenic mice with cardiac overexpression of catalase. Contractile indices analyzed included peak shortening (PS), time-to-90% PS (TPS90), time-to-90% relengthening (TR90), half-width duration (HWD), maximal velocity of shortening/relengthening (± dL/dt) and intracellular Ca2+ levels or decay rate. Levels of advanced glycation endproduct (AGE), Na+/Ca2+ exchanger (NCX), sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA2a), phospholamban (PLB), myosin heavy chain (MHC), membrane Ca2+ and K+ channels were measured by western blot. Catalase transgene prolonged survival while did not alter myocyte function by itself. Aging depressed ± dL/dt, prolonged HWD, TR90 and intracellular Ca2+ decay without affecting other indices in FVB myocytes. Aged FVB myocytes exhibited a stepper decline in PS in response to elevated stimulus or a dampened rise in PS in response to elevated extracellular Ca2+ levels. Interestingly, aging-induced defects were nullified or significantly attenuated by catalase. AGE level was elevated by 5-fold in aged FVB compared with young FVB mice, which was reduced by catalase. Expression of SERCA2a, NCX and Kv1.2 K+ channel was significantly reduced although levels of PLB, L-type Ca2+ channel dihydropyridine receptor and ?-MHC isozyme remained unchanged in aged FVB hearts. Catalase restored NCX and Kv1.2 K+ channel but not SERCA2a level in aged mice. In summary, our data suggested that catalase protects cardiomyocytes from aging-induced contractile defect possibly via improved intracellular Ca2+ handling.

Ren, Jun; Li, Qun; Wu, Shan; Li, Shi-Yan; Babcock, Sara A.

2007-01-01

240

Cardiac overexpression of antioxidant catalase attenuates aging-induced cardiomyocyte relaxation dysfunction.  

PubMed

Catalase, an enzyme which detoxifies H2O2, may interfere with cardiac aging. To test this hypothesis, contractile and intracellular Ca2+ properties were evaluated in cardiomyocytes from young (3-4 months) and old (26-28 months) FVB and transgenic mice with cardiac overexpression of catalase. Contractile indices analyzed included peak shortening (PS), time-to-90% PS (TPS90), time-to-90% relengthening (TR90), half-width duration (HWD), maximal velocity of shortening/relengthening (+/-dL/dt) and intracellular Ca2+ levels or decay rate. Levels of advanced glycation endproduct (AGE), Na+/Ca2+ exchanger (NCX), sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA2a), phospholamban (PLB), myosin heavy chain (MHC), membrane Ca2+ and K+ channels were measured by western blot. Catalase transgene prolonged survival while did not alter myocyte function by itself. Aging depressed+/-dL/dt, prolonged HWD, TR90 and intracellular Ca2+ decay without affecting other indices in FVB myocytes. Aged FVB myocytes exhibited a stepper decline in PS in response to elevated stimulus or a dampened rise in PS in response to elevated extracellular Ca2+ levels. Interestingly, aging-induced defects were nullified or significantly attenuated by catalase. AGE level was elevated by 5-fold in aged FVB compared with young FVB mice, which was reduced by catalase. Expression of SERCA2a, NCX and Kv1.2 K+ channel was significantly reduced although levels of PLB, L-type Ca2+ channel dihydropyridine receptor and beta-MHC isozyme remained unchanged in aged FVB hearts. Catalase restored NCX and Kv1.2 K+ channel but not SERCA2a level in aged mice. In summary, our data suggested that catalase protects cardiomyocytes from aging-induced contractile defect possibly via improved intracellular Ca2+ handling. PMID:17250874

Ren, Jun; Li, Qun; Wu, Shan; Li, Shi-Yan; Babcock, Sara A

2006-12-27

241

Spectroscopic description of an unusual protonated ferryl species in the catalase from Proteus mirabilis and density functional theory calculations on related models. Consequences for the ferryl protonation state in catalase, peroxidase and chloroperoxidase  

Microsoft Academic Search

The catalase from Proteus mirabilis peroxide-resistant bacteria is one of the most efficient heme-containing catalases. It forms a relatively stable compound\\u000a II. We were able to prepare samples of compound II from P. mirabilis catalase enriched in 57Fe and to study them by spectroscopic methods. Two different forms of compound II, namely, low-pH compound II (LpH II) and\\u000a high-pH compound II

O. Horner; J. M. Mouesca; P. L. Solari; M. Orio; J. L. Oddou; P. Bonville; H. M. Jouve

2007-01-01

242

Genetic Variation Affecting the Expression of Catalase in DROSOPHILA MELANOGASTER: Correlations with Rates of Enzyme Synthesis and Degradation  

PubMed Central

Both second and third chromosome substitution lines isolated from natural populations of Drosophila melanogaster affect the expression of catalase (EC 1.11.1.6) at both the larval and adult stages of development. In each case, the level of catalase activity is strongly related to the level of catalase-specific cross-reacting material. Turnover studies employing the catalase inhibitor 3-amino-1,2,4-triazole were conducted on a selected number of lines. Although the variation in steady state levels of catalase protein was highly significant among lines, variation in intracellular degradation rate was not. These results suggest that the different steady state levels observed among lines largely reflect different rates of catalase synthesis.

Bewley, Glenn C.; Laurie-Ahlberg, Cathy C.

1984-01-01

243

Characterization of a Facultatively Psychrophilic Bacterium, Vibrio rumoiensis sp. nov., That Exhibits High Catalase Activity  

PubMed Central

A novel facultatively psychrophilic bacterium, strain S-1, which exhibits extraordinarily high catalase activity was isolated from the drain pool of a fish product processing plant that uses H2O2 as a bleaching and microbicidal agent. The catalase activity of the isolate was 1 or 2 orders of magnitude higher than those of Corynebacterium glutamicum, Staphylococcus aureus, Pseudomonas fluorescens, and five other species tested in this study. The strain seemed to possess only one kind of catalase, according to the results of polyacrylamide gel electrophoresis of the cell extract. The optimum temperature for catalase activity was about 30°C, which was about 20°C lower than that for bovine catalase activity. Electron microscopic observation revealed that the surface of the microorganism was covered by blebs. Although the isolate was nonflagellated, its taxonomic position on the basis of physiological and biochemical characteristics and analysis of 16S rRNA sequence and DNA-DNA relatedness data indicated that strain S-1 is a new species belonging to the genus Vibrio. Accordingly, we propose the name Vibrio rumoiensis. The type strain is S-1 (FERM P-14531).

Yumoto, Isao; Iwata, Hideaki; Sawabe, Tomoo; Ueno, Keisuke; Ichise, Nobutoshi; Matsuyama, Hidetoshi; Okuyama, Hidetoshi; Kawasaki, Kosei

1999-01-01

244

Production of catalases by Aspergillus niger isolates as a response to pollutant stress by heavy metals  

SciTech Connect

Isolates of Aspergillus niger, selected from the coal dust of a mine containing arsenic (As; 400 mg/kg) and from the river sediment of mine surroundings (As, 1651 mg/kg, Sb, 362 mg/kg), growing in minimal nitrate medium in the phase of hyphal development and spore formation, exhibited much higher levels of total catalase activity than the same species from the culture collection or a culture adapted to soil contaminated with As (5 mg/L). Electrophoretic resolution of catalases in cell-free extracts revealed three isozymes of catalases and production of individual isozymes was not significantly affected by stress environments. Exogenously added stressors (As{sup 5+}, Cd{sup 2+}, Cu{sup 2+}) at final concentrations of 25 and 50 mg/L and H{sub 2}O{sub 2} (20 or 40 m(M)) mostly stimulated production of catalases only in isolates from mines surroundings, and H{sub 2}O{sub 2} and Hg{sup 2+} caused the disappearance of the smallest catalase I. Isolates exhibited a higher tolerance of the toxic effects of heavy metals and H{sub 2}O{sub 2}, as monitored by growth, than did the strain from the culture collection.

Buckova, M.; Godocikova, J.; Simonovicova, A.; Polek, B. [Slovakian Academy of Science, Bratislava (Slovakia)

2005-04-15

245

The oxidation of chiral alcohols catalyzed by catalase in organic solvents  

SciTech Connect

The catalytic properties of bovine liver catalase have been investigated in organic solvents. In tetrahydrofuran, dioxane, and acetone (all containing 1% to 3% of water), the enzyme breaks down tert-butyl hydroperoxide several fold faster than in pure water. Furthermore, the rate of catalase-catalyzed production of tert-butanol from tert-butyl hydroperoxide increases more than 400-fold upon transition from aqueous buffer to ethanol as the reaction medium. The mechanistic rationale for this striking effect is that in aqueous buffer the rate-limiting step of the enzymatic process involves the reduction of catalase`s compound 1 by tert-butyl hydroperoxide. In ethanol, an additional step in the reaction scheme becomes available in which ethanol, greatly outcompeting the hydroperoxide, is oxidized by compound 1 regenerating the free enzyme. In solvents, such as acetonitrile or tetrahydrofuran, which themselves are not oxidizable by compound 1, catalase catalyzes the oxidation of numerous primary and secondary alcohols with tert-butyl hydroperoxide to the corresponding aldehydes or ketones. The enzymatic oxidation of some chiral alcohols (2,3-butanediol, citronellol, and menthol) under these conditions occurs enantioselectively. Examination of the enantioselectivity for the oxidation of 2,3-butanediol in a series of organic solvents reveals a considerable solvent dependence.

Magner, E.; Klibanov, A.M. [Massachusetts Inst. of Tech., Cambridge, MA (United States). Dept. of Chemistry

1995-04-20

246

Relationship between uptake of mercury vapor by mushrooms and its catalase activity  

SciTech Connect

The uptake of mercury vapor by mushrooms (Shiitake) artifically grown on an oak tree and the uptake in vitro by catalase extracts prepared from mushroom Hay Bacillus and spinach are reported. Mushrooms were exposed to 1.4 mg/Hg/cu m for 11 days. Measurement of total mercury was as previously described (Ogata et al. 1978, 1979). Levels in mushrooms ranged from 0.4 +/- 0.1 ..mu..g/g at 0.5 days to 4.6 +/- 0.2 ..mu..g/g at 10.5 days and steady-state thereafter. In in vitro studies Hy uptake by mushroom catalase extract was estimated by the perborate method. Uptake was found to parallel catalase activity and was inhibited by potassium cyanide, sodium azide, and 3-amino-1,2,4-triazole. Similar results were obtained with Hay Bacillus and spinach catalase extracts. Results suggest that the level of mercury in the mushroom can be used as an indicator of mercury pollution in the environment. It is also suggested that catalase has an important role in uptake of mercury vapor in the plant. 2 tables (JMT)

Ogata, M.; Kenmotsu, K.; Hirota, N.; Naito, M.

1981-12-01

247

Purification and characterization of catalase from sprouted black gram (Vigna mungo) seeds.  

PubMed

Black gram (Vigna mungo) is a legume which belongs to Fabaceae family. It is a rich source of protein. It has been known to have interesting small molecule antioxidant activity. However, its enzymatic antioxidant properties have not been explored much. In the present work we studied catalase, a principal antioxidant enzyme from black gram seeds. Day four sprouted black gram seeds were found to have a significant catalase content approximately of 15,240 U/g seeds. IMAC (Seph 4B-IDA-Zn(II)) was used for purifying this catalase, a purification fold of 106 and a high specific activity of 25,704 U/mg was obtained. The K(m) and V(max) of the purified catalase were found to be 16.2 mM and 2.5 ?mol/min. The effect of inhibitors like Sodium azide (NaN(3)) and EDTA and different metal ions on catalase activity were studied. NaN(3), Fe(3+)and Cu(2+) were found to have profound inhibitory effects on the enzyme activity. Other metal ions like Ni(2+), Ca(2+), Mg(2+) and Mn(2+) had both enhancing and inhibitory effects. The enzyme showed optimal activity at a temperature of 40°C and pH 7.0. It was stable over a broad range of pH 6.0-10.0 and had a half life of 7h 30 min at 50°C. PMID:22341355

Kandukuri, Sai Srikar; Noor, Ayesha; Ranjini, S Shiva; Vijayalakshmi, M A

2012-02-02

248

Inhibition of Catalase Activity with 3AminoTriazole Enhances the Cytotoxicity of the Alzheimer’s Amyloid-? Peptide  

Microsoft Academic Search

Amyloid-? (A?) is a cytotoxic peptide implicated in the pathology of Alzheimer’s disease. The antioxidant enzyme catalase has been suggested to protect against A? cytotoxicity in both neuronal and non-neuronal cell types. Inhibition of endogenous catalase using 3-amino-1,2,4-triazole (3AT) in neuronal (NT-2) and myeloma (SP2\\/0-Ag-14) cell lines increases A? toxicity, suggesting that any protective role for endogenous catalase requires active

Nathaniel G. N. Milton

2001-01-01

249

Layer-by-layer assembled multilayers using catalase-encapsulated gold nanoparticles  

NASA Astrophysics Data System (ADS)

We introduce a novel and versatile approach for the preparation of multilayers, based on catalase-encapsulated gold nanoparticles (CAT-AuNP), allowing electrostatic charge reversal and structural transformation through pH adjustment. CAT-AuNP, which are synthesized directly from CAT stabilizer, can be electrostatically assembled with anionic and cationic PEs as a result of the charge reversal of the catalase stabilizers through pH control. In particular, at pH 5.2, near the pI of catalase, dispersed CAT-AuNP are structurally transformed into colloidal or network CAT-AuNP nanocomposites. Furthermore, we demonstrate that the layer-by-layer assembled multilayers composed of PEs and CAT-AuNP induce an effective electron transfer between CAT and the electrode as well as a high loading of CAT and AuNP, and resultantly exhibit a highly catalytic activity toward H2O2.

Kim, Sungwoo; Park, Jeongju; Cho, Jinhan

2010-09-01

250

Influence of Catalase and Superoxide Dismutase on Ozone Inactivation of Listeria monocytogenes  

PubMed Central

The effects of ozone at 0.25, 0.40, and 1.00 ppm on Listeria monocytogenes were evaluated in distilled water and phosphate-buffered saline. Differences in sensitivity to ozone were found to exist among the six strains examined. Greater cell death was found following exposure at lower temperatures. Early stationary-phase cells were less sensitive to ozone than mid-exponential- and late stationary-phase cells. Ozonation at 1.00 ppm of cabbage inoculated with L. monocytogenes effectively inactivated all cells after 5 min. The abilities of in vivo catalase and superoxide dismutase to protect the cells from ozone were also examined. Three listerial test strains were inactivated rapidly upon exposure to ozone. Both catalase and superoxide dismutase were found to protect listerial cells from ozone attack, with superoxide dismutase being more important than catalase in this protection.

Fisher, Christopher W.; Lee, Dongha; Dodge, Beth-Anne; Hamman, Kristen M.; Robbins, Justin B.; Martin, Scott E.

2000-01-01

251

Exposure of erythrocytes to methylene blue shows the active role of catalase in removing hydrogen peroxide.  

PubMed

Methylene blue (MB) is a powerful reducing agent that is widely used in clinical practice as well as for metabolic studies of the erythrocyte. We have investigated the role of catalase as a specific enzyme for the removal of hydrogen peroxide by measuring the in vitro effects of MB on human red cells. In the presence of MB, catalase underwent inactivation even with the co-existence of active generation of NADPH, leaving the glutathione concentration unaffected. The data obtained in the present investigation show, using a different tool (MB), that catalase is the active enzyme in H2O2 detoxification and that its integrity is largely dependent on an adequate generation of NADPH. PMID:12437668

Gaetani, Gian Franco; Rapezzi, Davide; Mangerini, Rosa; Racchi, Omar; Rolfo, Michela; Ferraris, Anna Maria

2002-12-01

252

Cloning and Characterization of katA , Encoding the Major Monofunctional Catalase from Xanthomonas campestris pv. phaseoli and Characterization of the Encoded Catalase KatA  

Microsoft Academic Search

The first cloning and characterization of the gene katA, encoding the major catalase (KatA), from Xanthomonas is reported. A reverse genetic approach using a synthesized katA-specific DNA probe to screen a X. campestris pv. phaseoli genomic library was employed. A positively hybridizing clone designated pKat29 that contained a full-length\\u000a katA was isolated. Analysis of the nucleotide sequence revealed an open

Nopmanee Chauvatcharin; Paiboon Vattanaviboon; Jack Switala; Peter C. Loewen; Skorn Mongkolsuk

2003-01-01

253

Vascular endothelium-specific overexpression of human catalase in cloned pigs.  

PubMed

The objective of this study was to develop transgenic Yucatan minipigs that overexpress human catalase (hCat) in an endothelial-specific manner. Catalase metabolizes hydrogen peroxide (H(2)O(2)), an important regulator of vascular tone that contributes to diseases such as atherosclerosis and preeclampsia. A large animal model to study reduced endothelium-derived H(2)O(2) would therefore generate valuable translational data on vascular regulation in health and disease. Yucatan minipig fetal fibroblasts stably co-transfected with human catalase (Tie2-hCat) and eGFP expression constructs were isolated into single-cell populations. The presence of the Tie2-hCat transgene in individual colonies of fibroblasts was determined by PCR. Transgenic fibroblasts were used for nuclear transfer into enucleated oocytes by electrofusion. A minimum of 140 cloned embryos were transferred per surrogate sow (n = 4). All four surrogates maintained pregnancies and piglets were delivered by cesarean section. Nine male piglets from three of the four litters carried the Tie2-hCat transgene. Expression of human catalase mRNA and overall elevated catalase protein in isolated umbilical endothelial cells from transgenic piglets were verified by RT-PCR and western blot, respectively, and endothelial localization was confirmed by immunohistochemistry. Increased enzymatic activity of catalase in transgenic versus wild-type endothelial cells was inferred based on significantly reduced levels of H(2)O(2) in culture. The similarities in swine and human cardiovascular anatomy and physiology will make this pig model a valuable source of information on the putative role of endothelium-derived H(2)O(2) in vasodilation and in the mechanisms underlying vascular health and disease. PMID:21170678

Whyte, J J; Samuel, M; Mahan, E; Padilla, J; Simmons, G H; Arce-Esquivel, A A; Bender, S B; Whitworth, K M; Hao, Y H; Murphy, C N; Walters, E M; Prather, R S; Laughlin, M H

2010-12-18

254

Diminution of mouse epidermal superoxide dismutase and catalase activities by tumor promotors  

SciTech Connect

The effects of phorbol ester tumor promoters and related compounds on superoxide dismutase (SOD) and catalase were examined. The treatment of adult mouse skin with 2 ..mu..g 12-0-tetradecanoylphorbol-13-acetate (TPA) resulted in a sustained decrease in the basal levels of both SOD and catalase activities in the epidermis. A decline in SOD activity occurred within 2 h after application and the maximum effect was seen at 16-17 h. The decrease in SOD activity was always accompanied by a similar decline in the epidermal catalase activity. The alterations in both enzymes occurred against a high background of enhanced protein synthesis which indicates that the effect of TPA is selective for SOD and catalase. Other tumor promoters such as phorbol 12,13-dibutyrate and the non-phorbol tumor promoter anthraline also lowered the activities of both the enzymes. Mezerein, a resiniferonol derivative with weak promoting activity but a potent stage-II promoter, appeared to be more potent than TPA in lowering the basal levels. These results indicate that damage which favors neoplastic progression would occur in TPA-treated mouse skin due to the accumulation of free radicals resulting from low levels of SOD and catalase activity. In addition, the TPA-caused decrease in the levels of SOD and catalase was not prevented by either retinoic acid, fluocinolone acetonide, tosyl amino-2-phenylethyl chloromethyl ketone, or butylated hydroxytoluene, suggesting that inhibition of tumor promotion by these agents is not mediated through alterations in the levels of enzymatic activities which decrease free radical concentrations.

Solanki, V. (Oak Ridge National Lab., TN); Rana, R.S.; Slaga, T.J.

1981-01-01

255

Synthesis and activity of Helicobacter pylori urease and catalase at low pH.  

PubMed Central

BACKGROUND: Helicobacter pylori produces large amounts of urease presumably to be prepared for the rare event of a sudden acid exposure. The hypothesis that H pylori is acid sensitive and protein production is inhibited by low pH was examined. METHODS: H pylori or its soluble enzymes were incubated buffered or unbuffered at a pH ranging from 2-7 in the presence of 5 mM urea for 30 minutes. After exposure, urease and catalase activities of whole cells, supernatants, and soluble enzyme preparations were measured at pH 6.8. Newly synthesised enzyme was quantified by immunoprecipitation of [35S]-methionine labelled protein. RESULTS: Exposure to buffer below pH 4 resulted in loss of intracellular urease activity. In soluble enzyme preparations and supernatant, no urease activity was measurable after incubation at pH < 5. In contrast, catalase in whole cells, supernatant, and soluble enzyme preparations remained active after exposure to pH > or = 3. Exposure below pH 5 inhibited synthesis of total protein including nascent urease and catalase. At pH 6 or 7, urease represented 10% of total protein, catalase 1.5%. Exposure of H pylori to unbuffered HCl (pH > 2) resulted in an immediate neutralisation; urease and catalase activities and synthesis were unchanged. CONCLUSION: Low surrounding pH reduces activity of urease and synthesis of nascent urease, catalase, and presumably of most other proteins. This suggests that H pylori is not acidophilic although it tolerates short-term exposure to low pH.

Bauerfeind, P; Garner, R; Dunn, B E; Mobley, H L

1997-01-01

256

[Activity catalase and superoxide dismutase of Staphylococcus aureus during its persistence in the body].  

PubMed

The dynamics of the level of catalase and superoxidedismutase (SOD) expression by S. aureus isolated in persistent experimental kidney infection is described. A rise in the activity of the staphylococci under study during transition of the infectious process from the alteration to persistence stage. Changes in the expression of SOD and catalase were observed simultaneously with a decrease in hemolytic, fibrinolytic and protease activity, as well as in the presence of more pronounced clumping and an increase in the production of protein A, the antilysozyme and anticomplement activity of staphylococcal clones obtained from kidney tissue. The significance of all above-mentioned phenomena in the persistence of microorganisms is discussed. PMID:11548249

Brudastov, Iu A; Sborets, T S; Deriabin, D G

257

Effect of helium-neon laser on activity and optical properties of catalase  

Microsoft Academic Search

The effects of laser (632.8 nm) on functional and spectral properties of catalase at pH 6.0–7.4 were studied. Laser irradiation\\u000a led to photoactivation of the enzyme at pH 7.1–7.4. Changes in the spectral properties of photomodified hemoprotein were found\\u000a in the absorption spectrum of the protein component: apoenzyme displayed protective effects in relation to ferroporphyrin.\\u000a Structural modifications of catalase induced

V. G. Artyukhov; O. V. Basharina; A. A. Pantak; L. S. Sveklo

2000-01-01

258

Cyanamide reduces brain catalase and ethanol-induced locomotor activity: is there a functional link?  

Microsoft Academic Search

The present study was designed in an attempt to assess a previously suggested role of brain catalase activity in ethanol-induced\\u000a behaviour by examining ethanol-induced locomotor activity in cyanamide-treated mice. Mice were pretreated with IP injections\\u000a of the catalase inhibitor cyanamide (3.75, 7.5, 15, 30 or 45?mg\\/kg) or saline. Following this treatment, animals in each group\\u000a received IP injections of ethanol

Carles Sanchis-Segura; Marta Miquel; Mercè Correa; Carlos M. G. Aragon

1999-01-01

259

Catalase activity as a potential indicator of the reducer component of small closed ecosystems  

NASA Astrophysics Data System (ADS)

Dynamics of catalase activity has been shown to reflect the growth curve of microorganisms in batch cultivation (celluloselythic bacteria Bacillus acidocaldarius and bacteria of the associated microflora Chlorella vulgaris). Gas and substrate closure of the three component ecosystems with spatially separated components ``producer-consumer-reducer'' (Chl. vulgaris-Paramecium caudatum-B. acidocaldarius, two bacterial strains isolated from the associated microflora Chl. vulgaris) demonstrated that the functioning of the reducer component can be estimated by the catalase activity of microorganisms of this component.

Sarangova, A. B.; Somova, L. A.; Pisman, T. I.

1997-01-01

260

The effect of intracellular antioxidant delivery (catalase) on hydrogen peroxide and proinflammatory cytokine synthesis: a new therapeutic horizon.  

PubMed

Reactive oxygen species synthesized by endothelial cells may be responsible for cell damage and altered physiologic function. After endotoxin stimulation, free radicals including H(2)O(2) are produced. We have developed a method of intracellular drug delivery using albumin microcapsules. Catalase would be an excellent compound to alter H(2)O(2) production. However, the large molecular size of catalase limits cellular penetration. Endothelial cells have been previously shown to readily phagocytoze albumin microcapsules. Methods: Catalase was added to an albumin solution to form a 10% solution of catalase. Microspheres from 2 to 7 microm in size were formed using a Bucchi spray dryer. Human endothelial cells were incubated with varying concentrations of microencapsulated catalase. The cells were then exposed to Escherichia coli endotoxin to determine if increased intracellular penetration of catalase would inhibit H(2)O(2), nitrate, and cytokine synthesis. Results: There was a 7.2-fold increase in endothelial intracellular catalase after 48 h incubation. H(2)O(2) was inhibited by 72%, nitrate 96%, TNF 90%, IL1 21%, IL6 42%. Conclusions: These results demonstrate that inhibition of H(2)O(2) as a result of increased intracellular delivery of catalase inhibits proinflammatory cytokine synthesis after endotoxin exposure. PMID:19845487

Siwale, Rodney C; Yeboah, George K; Addo, Richard; Oettinger, Carl W; D'Souza, Martin J

2009-11-01

261

Mitochondrial Targeting of a Catalase Transgene Product by Plasmid Liposomes Increases Radioresistance In Vitro and In Vivo  

PubMed Central

To determine whether increased mitochondrially localized catalase was radioprotective, a human catalase transgene was cloned into a small pSVZeo plasmid and localized to the mitochondria of 32D cl 3 cells by adding the mitochondrial localization sequence of MnSOD (mt-catalase). The cell lines 32D-Cat and 32D-mt-Cat had increased catalase biochemical activity as confirmed by Western blot analysis compared to the 32D cl 3 parent cells. The MnSOD-overexpressing 32D cl 3 cell line, 2C6, had decreased baseline catalase activity that was increased in 2C6-Cat and 2C6-mt-Cat subclonal cell lines. 32D-mt-Cat cells were more radioresistant than 32D-Cat cells, but both were radioresistant relative to 32D cl 3 cells. 2C6-mt-Cat cells but not 2C6-Cat cells were radioresistant compared to 2C6 cells. Intratracheal injection of the mt-catalase-plasmid liposome complex (mt-Cat-PL) but not the catalase-plasmid liposome complex (Cat-PL) increased the resistance of C57BL/6NHsd female mice to 20 Gy thoracic irradiation compared to MnSOD-plasmid liposomes. Thus mitochondrially targeted overexpression of the catalase transgene is radioprotective in vitro and in vivo.

Epperly, Michael W.; Melendez, J. A.; Zhang, Xichen; Nie, Suhua; Pearce, Linda; Peterson, James; Franicola, Darcy; Dixon, Tracy; Greenberger, Benjamin A.; Komanduri, Paavani; Wang, Hong; Greenberger, Joel S.

2009-01-01

262

POTENTIATING ACTION OF THE CATALASE POISON AMINOTRIAZOLE ON HYDROGEN PEROXIDE TOXICITY. SIGNIFICANCE FOR THE BIOLOGICAL EFFECTS OF IONIZING RADIATION  

Microsoft Academic Search

In mice, aminotriazole induced marked decreases in both tissue (liver) ; catalase activity and the dose (LDââ) of hydrogen peroxide (HâOâ; ) required to induce death. Both effects were counteracted by ethanol. These ; findings, coupled with a consideration of pertinent literature, indicate that: a) ; tissue catalase plays an important role in detoxication of hydrogen peroxide ; formed in

L. V. Beck; S. Ch. Kalser; V. R. Alexander

1959-01-01

263

Direct electrochemistry and electrocatalytic activity of catalase immobilized onto electrodeposited nano-scale islands of nickel oxide  

Microsoft Academic Search

Cyclic voltammetry was used for simultaneous formation and immobilization of nickel oxide nano-scale islands and catalase on glassy carbon electrode. Electrodeposited nickel oxide may be a promising material for enzyme immobilization owing to its high biocompatibility and large surface. The catalase films assembled on nickel oxide exhibited a pair of well defined, stable and nearly reversible CV peaks at about

Abdollah Salimi; Ensiyeh Sharifi; Abdollah Noorbakhsh; Saied Soltanian

2007-01-01

264

Conversion of methanol to formic acid through the coupling of the enzyme reactions of alcohol oxidase, catalase and formaldehyde dismutase  

Microsoft Academic Search

Summary A novel process for the production of formic acid from methanol has been developed that involves the coupled reactions of the three enzymes, alcohol oxidase, catalase and formaldehyde dismutase. In this process, methanol is oxidized to formaldehyde by alcohol oxidase and catalase, followed by the formaldehyde dismutase reaction that leads to the formation of methanol and formic acid. Ultimately,

Sumiko Mizuno; Yukio Imada

1986-01-01

265

Cloning, characterization, and targeted disruption of cpcat1, coding for an in planta secreted catalase of Claviceps purpurea.  

PubMed

Claviceps purpurea has been shown to secrete catalases in axenic and parasitic culture. In order to determine the importance of these enzymes in the host-parasite interaction, especially their role in overcoming oxidative stress imposed on the pathogen by the plant's defense system, the catR gene from A. niger was used to isolate a putative catalase gene from a genomic library of C. purpurea, cpcat1 consists of an open reading frame of 2,148 bp that is interrupted by five introns. Its derived gene product shows significant homology to fungal catalases and contains a putative signal peptide of 19 amino acids and three putative N-glycosylation sites, which indicates that CPCAT1 is a secreted catalase. Disruption of the gene by a gene replacement approach resulted in the loss of two catalase isoforms, CATC and CATD, strongly suggesting that they are both encoded by cpcat1. CATD is the major secreted catalase of C. purpurea and is furthermore the only catalase present in the honeydew of infected rye ears. Deletion mutants of cpcat1 were inoculated on rye plants and showed no significant reduction in virulence. Ovarian tissue and honeydew of plants inoculated with the mutants lacked CATD, confirming that this catalase is not essential for colonization of the host tissue by C. purpurea. PMID:9675893

Garre, V; Müller, U; Tudzynski, P

1998-08-01

266

Catalase deficiency in Staphylococcus aureus subsp. anaerobius is associated with natural loss-of-function mutations within the structural gene  

Microsoft Academic Search

Degenerate oligonucleotide primers based on internal peptide sequences obtained by HPLC from purified Staphylococcus aureus catalase were used to locate the S. aureus and S. aureus subsp. anaerobius kat regions by PCR. Southern hybridization analysis with a probe derived from a 1<1 kb PCR- amplified fragment showed that a single copy of the putative catalase gene was present in the

Rosario Sanz; Irma Mari; Jose A. Ruiz-Santa-Quiteria; Jose A. Orden; Dolores Cid; Rosa M. Diez; K. Souad Silhadi; Ricardo Amils; Ricardo de la Fuente

267

Structure, recombinant expression and mutagenesis studies of the catalase with oxidase activity from Scytalidium thermophilum.  

PubMed

Scytalidium thermophilum produces a catalase with phenol oxidase activity (CATPO) that catalyses the decomposition of hydrogen peroxide into oxygen and water and also oxidizes various phenolic compounds. A codon-optimized catpo gene was cloned and expressed in Escherichia coli. The crystal structures of native and recombinant S. thermophilum CATPO and two variants, H82N and V123F, were determined at resolutions of 2.7, 1.4, 1.5 and 1.9?Å, respectively. The structure of CATPO reveals a homotetramer with 698 residues per subunit and with strong structural similarity to Penicillium vitale catalase. The haem component is cis-hydroxychlorin ?-spirolactone, which is rotated 180° with respect to small-subunit catalases. The haem-binding pocket contains two highly conserved water molecules on the distal side. The H82N mutation resulted in conversion of the native d-type haem to a b-type haem. Kinetic studies of the H82N and V123F mutants indicate that both activities are likely to be associated with the haem centre and suggest that the secondary oxidase activity may be a general feature of catalases in the absence of hydrogen peroxide. PMID:23519415

Yuzugullu, Yonca; Trinh, Chi H; Smith, Mark A; Pearson, Arwen R; Phillips, Simon E V; Sutay Kocabas, Didem; Bakir, Ufuk; Ogel, Zumrut B; McPherson, Michael J

2013-02-16

268

Catalase overexpression reduces UVB-induced apoptosis in a human xeroderma pigmentosum reconstructed epidermis  

Microsoft Academic Search

Xeroderma pigmentosum type C (XPC) is a rare autosomal recessive disorder that occurs due to inactivation of the XPC protein, an important DNA damage recognition protein involved in DNA nucleotide excision repair (NER). This defect, which prevents removal of a wide array of direct and indirect DNA lesions, is associated with a decrease in catalase activity. To test the hypothesis

H R Rezvani; C Ged; B Bouadjar; H de Verneuil; A Taïeb

2008-01-01

269

Catalase Test for Abnormal Milk. I. Techniques and Factors Affecting the Test1  

Microsoft Academic Search

This study was made to compare techniques for testing milk for catalase activity, and to determine the effects of certain experimental variables on the reaction. In the inverted tube test, calibrated centrifuge tubes with outlets of straight glass tubing were most satisfactory. Increase in substrate concentration above 1 ml 3% H~O~ did not significantly increase O~ production at room tem-

G. Nageswararao; H. Blobel; J. B. Derbyshire

1965-01-01

270

Assembly of catalase-based bioconjugates for enhanced anticancer efficiency of photodynamic therapy in vitro.  

PubMed

An oxygen generation core-shell structure uploading rose bengal has been fabricated by covalent assembly of catalase and alginate dialdehyde via Schiff's base. The composite can catalyze the decomposition of intracellular H2O2 to increase the concentration of O2, which effectively enhances the anticancer efficiency of photodynamic therapy in vitro. PMID:24104860

Zhao, Jie; Fei, Jinbo; Du, Cuiling; Cui, Wei; Ma, Hongchao; Li, Junbai

2013-10-22

271

Structural and functional alterations of catalase induced by acriflavine, a compound causing apoptosis and necrosis.  

PubMed

Acriflavine is an antiseptic agent causing both apoptosis and necrosis in yeast. In this work, its effect on the structure and function of catalase, a vital enzyme actively involved in protection against oxidative stress, was investigated. In vitro kinetic studies showed that acriflavine inhibited the enzymatic activity in a competitive manner. The residual activity detectable after preincubation of catalase (1.5 nmol/L) with various concentrations of acriflavine went from 50% to 20% of the control value as the acriflavine concentration increased from 30 to 90 micromol/L. Correlatively with the decrease in activity, alterations in the enzyme's conformation were observed as indicated by fluorescence spectroscopy, circular dichroism spectroscopy, and electronic absorption spectroscopy. The enzyme's intrinsic fluorescence obtained upon excitation at either 297 nm (tryptophan residues) or 280 nm (tyrosine and tryptophan residues) decreased as a function of acriflavine concentration. Circular dichroism studies showed alterations of the protein structure by acriflavine with up to 13% decrease in alpha helix, 16% increase in beta-sheet content, 17% increase in random coil, and 4% increase in beta turns. Spectrophotometric studies showed a blueshift and modifications in the chromicity of catalase at 405 nm, corresponding to an absorbance band due to the enzyme's prosthetic group. Thus, acriflavine induced in vitro a profound change in the structure of catalase so that the enzyme could no longer function. Our results showed that acriflavine, a compound producing apoptosis and necrosis, can have a direct effect on vital functions in cells by disabling key enzymes. PMID:19723068

Attar, Farnoosh; Khavari-Nejad, Sarah; Keyhani, Jacqueline; Keyhani, Ezzatollah

2009-08-01

272

Overexpression of Human Catalase Gene Decreases Oxidized Lipid-Induced Cytotoxicity in Vascular Smooth Muscle Cells  

Microsoft Academic Search

Reactive oxygen metabolites such as hydrogen peroxide (H 2O2) and oxidized fatty acids are proinflammatory and are involved in the pathophysiology of various diseases including atherosclerosis. The effects of these oxidants could be inhibited by the external addition of an antioxidant, suggesting the promotion or propagation of further oxidation. In this study, we describe the stable overexpression of human catalase

Nalini Santanam; Nathalie Auge; Mimi Zhou; Channa Keshava; Sampath Parthasarathy

2010-01-01

273

CLINICAL ASSESSMENT OF GLUTATHIONE PEROXIDASE AND CATALASE TO THE STATUS OF MALONDIALDEHYDE IN UROLITHIASIS  

Microsoft Academic Search

Objective: To assess the role of lipid peroxidation and antioxidant enzymes in serum of urolithiasis patients. Methodology: Glutathione peroxidase (GPx), catalase (CAT) and malondialadehyde (MDA) in serum of urolithiasis patients have been measured. Results: The study has revealed a significant increase in MDA and a significant decrease in GPx and CAT. There have been no significant correlations of serum MDA,

Roula Hamid Mahmoud; Mufeed J. Ewadh; Kadhum J. Al-Hamadani

2009-01-01

274

Effects of autogamy in Paramecium tetraurelia on catalase activity and on radiosensitivity to natural ionizing radiations  

Microsoft Academic Search

Catalase activity of Paramecium tetraurelia decreased during autogamy and recovered to normal 5 days later. Autogamy also caused changes in the ciliate's sensitivity sensitivity to natural ionizing radiations - the decrease in cell growth rate previously described in shielded cultures did not occur when autogamous cells were used. Maximum effect of shielding was observed in 11-day-old postautogamous cells. The role

F. Croute; D. Dupouy; J. P. Charley; J. P. Soleilhavoup; H. Planel

1980-01-01

275

Expression of heat shock proteins, glutathione peroxidase and catalase in childhood acute lymphoblastic leukemia and nephroblastoma  

Microsoft Academic Search

In this study we analyzed the mRNA expression of the heat shock proteins 27 and 70, and the expression of the radical scavenging enzymes catalase and glutathione peroxidase (GPX) in childhood acute lymphoblastic leukemia (ALL, n = 54) and in nephroblastoma (n = 34). We found a significant positive correlation between both heat shock proteins and also between glutathione peroxidase

G. Stammler; M. Volm

1996-01-01

276

Middle ear catalase distribution in an animal model of otitis media  

Microsoft Academic Search

Increasing evidence implicates free radicals in the pathogenesis of inflammatory disease, including otitis media. The anti-oxidant enzymes catalase, glutathione peroxidase and superoxide dismutase protect tissues from the destructive effects of free radicals. Our previous work has shown depressed levels of superoxide dismutase in the infected middle ears of a guinea pig model of otitis media in comparison with normal control

R. R. Parks; C. C. Huang; J. Haddad Jr

1996-01-01

277

Induction and inactivation of catalase and superoxide dismutase of Escherichia coli by ozone  

Microsoft Academic Search

Oxyradicals have been implicated in ozone (Oâ) toxicity and in other oxidant stress. In this study, we investigated the effects of Oâ on the biosynthesis of the antioxidant enzymes catalase and superoxide dismutase in Escherichia coli to determine their role in the defense against ozone toxicity. Inhibition of growth and loss of viability were observed in cultures exposed to ozone.

C. Whiteside; H. M. Hassan

1987-01-01

278

Regulation of the oxidative stress protective enzymes, catalase and superoxide dismutase in Xanthomonas — a review  

Microsoft Academic Search

Xanthomonas showed atypical regulation of catalase (Kat) and superoxide dismutase with respect to growth phase and response to various inducers. The highest levels of both enzymes were detected during early log phase of growth and declined as growth continued. This was in contrast to resistance levels to superoxides, H2O2 and organic peroxides, which reached maximum levels during stationary phase. Xanthomonas

Suvit Loprasert; Paiboon Vattanaviboon; Wipa Praituan; Sangpen Chamnongpol; Skorn Mongkolsuk

1996-01-01

279

Novel Delivery of Antioxidant Enzyme Catalase to Alveolar Macrophages by Fc Receptor-Mediated Endocytosis  

Microsoft Academic Search

Excessive production of reactive oxygen species by alveolar macrophages (AMs) in response to inhaled toxic substances is a major cause of oxidative lung injury. Therapeutic approaches designed to protect the lungs from oxidative injury by administering native antioxidant enzymes such as catalase and superoxide dismutase have been suggested. However, problems associated with poor penetration of these enzymes to the intracellular

Jeannine Harrison; Xianglin Shi; LiYing Wang; Joseph K. H. Ma; Yongyut Rojanasakul

1994-01-01

280

Catalase activity and expression in developing sunflower seeds as related to drying  

Microsoft Academic Search

Changes in catalase (CAT) activity and in CAT iso- form pattern and expression were investigated in developing sunflower (Helianthus annuus L.) seeds during desiccation on the mother plant and after arti- ficial drying on the flowerheads. Seeds regularly des- iccated during their development on the mother plant and reached mass maturity at c. 42 d after flowering (DAF). Freshly harvested

Christophe Bailly; Juliette Leymarie; Arnaud Lehner; Sandra Rousseau; Francoise Corbineau

2004-01-01

281

Effect of temperature preconditioning on catalase, peroxidase, and superoxide dismutase in chilled zucchini squash  

Microsoft Academic Search

The development of chilling injury symptoms in zucchini squash (Cucurbita pepo L., cv. ‘Elite’) stored at 5 °C was delayed by preconditioning the fruit at a temperature of 15 °C for two days. This temperature preconditioning treatment suppressed the increase in peroxidase activity and reduced the decline of catalase activity in squash during subsequent storage at 5 °C. The superoxide

Chien Yi Wang

1995-01-01

282

Occurrence and biosynthesis of catalase at different stages of seed maturation  

Microsoft Academic Search

It was to be shown whether during the biogenesis of microbodies some of their components were already present in the cell prior to the organelle's assembly. To this end, the occurrence and properties of catalase in soluble and particular fractions of ripening cucumber seeds were examined. Homogenates of seeds from ripening fruits were fractionated by isopycnic density gradient centrifugation, and

H. Kindl; S. Schiefer; H.-G. Löffler

1980-01-01

283

Associations between Breast Cancer Risk and the Catalase Genotype, Fruit and Vegetable Consumption, and Supplement Use  

Microsoft Academic Search

Observed weak or null associations between fruit and vegetable intake and breast cancer risk could be due to heterogeneity in endogenous antioxidant capabilities. The authors evaluated potential relations between a func- tional polymorphism in catalase, an antioxidant enzyme, and breast cancer risk, particularly in relation to fruit and vegetable intake and supplement use. Women (1,008 cases and 1,056 controls) in

Jiyoung Ahn; Marilie D. Gammon; Regina M. Santella; Mia M. Gaudet; Julie A. Britton; Susan L. Teitelbaum; Mary Beth Terry; Susan Nowell; Warren Davis; Cutberto Garza; Alfred I. Neugut; Christine B. Ambrosone

2005-01-01

284

Ectopic expression of catalase in Drosophila mitochondria increases stress resistance but not longevity  

Microsoft Academic Search

The goal of this study was to test the hypothesis that the rate of mitochondrial oxidant production governs the aging process of the fruit fly, Drosophila melanogaster. Catalase, an antioxidative enzyme expressed in the cytosol and peroxisomes of Drosophila, was targetted ectopically to the mitochondrial matrix by fusion of a leader peptide derived from ornithine aminotransferase with its N-terminus. The

Robin J Mockett; Anne-Cécile V Bayne; Linda K Kwong; William C Orr; Rajindar S Sohal

2003-01-01

285

Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes  

SciTech Connect

Genetic deficiencies of glucose-6-phosphate dehydrogenase (G6PD) and NADPH predispose affected erythrocytes to destruction from peroxides. Conversely, genetic deficiencies of catalase do not predispose affected erythrocytes to peroxide-induced destruction. These observations have served to strengthen the assumption that the NADPH/glutathione/glutathione peroxidase pathway is the principal means for disposal of H/sub 2/O/sub 2/ in human erythrocytes. Recently, however, mammalian catalase was found to have tightly bound NADPH and to require NADPH for the prevention and reversal of inactivation by its toxic substrate (H/sub 2/O/sub 2/). Since both catalase and the glutathione pathway are dependent on NADPH for function, this finding raises the possibility that both mechanisms destroy H/sub 2/O/sub 2/ in human erythrocytes. A comparison of normal and acatalasemic erythrocytes in the present study indicated that catalase accounts for more than half of the destruction of H/sub 2/O/sub 2/ when H/sub 2/O/sub 2/ is generated at a rate comparable to that which leads to hemolysis in G6PD- deficient erythrocytes.

Gaetani, G.F.; Galiano, S.; Canepa, L.; Ferraris, A.M.; Kirkman, H.N.

1989-01-01

286

Induction and inactivation of catalase and superoxide dismutase of Escherichia coli by ozone  

SciTech Connect

Oxyradicals have been implicated in ozone (O/sub 3/) toxicity and in other oxidant stress. In this study, we investigated the effects of O/sub 3/ on the biosynthesis of the antioxidant enzymes catalase and superoxide dismutase in Escherichia coli to determine their role in the defense against ozone toxicity. Inhibition of growth and loss of viability were observed in cultures exposed to ozone. Results also showed an increase in the activities of catalase and superoxide dismutase in cultures exposed to ozone, which was shown to be due to true induction rather than activation of preexisting apoproteins. Cessation of O/sub 3/ exposure resulted in 30 min of continual high rate of catalase biosynthesis followed by a gradual decrease in the level of the enzyme approaching that of control cultures. This decrease was attributed to a concomitant cessation of de novo enzyme synthesis and dilution of preexisting enzyme by cellular growth. Ozonation of cell-free extracts showed that superoxide dismutase and catalase are subject to oxidative inactivation by ozone. In vivo induction of these enzymes may represent an adaptive response evolved to protect cells against ozone toxicity.

Whiteside, C.; Hassan, H.M.

1987-09-01

287

Do Superoxide Dismutase (SOD) and Catalase (CAT) protect Cells from DNA Damage Induced by Active Arsenicals?  

EPA Science Inventory

Superoxide dismutase (SOD) catalyzes the conversion of superoxide to hydrogen peroxide, which can be converted to water and oxygen through the action of catalase. Heterozygous mice of strain B6: 129S7-SodltmlLeb/J were obtained from Jackson Laboratories and bred to produce offspr...

288

Preparation and Characterization of Catalase-Loaded Solid Lipid Nanoparticles Protecting Enzyme against Proteolysis  

PubMed Central

Catalase-loaded solid lipid nanoparticles (SLNs) were prepared by the double emulsion method (w/o/w) and solvent evaporation techniques, using acetone/methylene chloride (1:1) as an organic solvent, lecithin and triglyceride as oil phase and Poloxmer 188 as a surfactant. The optimized SLN was prepared by lecithin: triglyceride ratio (5%), 20-second + 30-second sonication, and 2% Poloxmer 188. The mean particle size of SLN was 296.0 ± 7.0 nm, polydispersity index range and zeta potential were 0.322–0.354 and ?36.4 ± 0.6, respectively, and the encapsulation efficiency reached its maximum of 77.9 ± 1.56. Catalase distributed between the solid lipid and inner aqueous phase and gradually released from Poloxmer coated SLNs up to 20% within 20 h. Catalase-loaded SLN remained at 30% of H2O2-degrading activity after being incubated with Proteinase K for 24 h, while free catalase lost activity within 1 h.

Qi, Ce; Chen, Yan; Jing, Qing-Zhe; Wang, Xing-Guo

2011-01-01

289

An increase of acidic isoform of catalase in red blood cells from HIV(+) population  

Microsoft Academic Search

A systemic oxidative stress of HIV (+) individuals has been recognized from a low glutathione level and a high level of inflammatory cytokines such as TNFa. Previously, we demonstrated that the catalase enzyme activity in HIV (+) population is significantly altered depending on the cell types; the level was significantly high in red blood cells while the enzymes in white

Sumio Yano; Maria Colon; Noriko Yano

1996-01-01

290

Impedance spectroscopy and conductometric biosensing for probing catalase reaction with cyanide as ligand and inhibitor.  

PubMed

In this work, a new biosensor was prepared through immobilization of bovine liver catalase in a photoreticulated poly (vinyl alcohol) membrane at the surface of a conductometric transducer. This biosensor was used to study the kinetics of catalase-H(2)0(2) reaction and its inhibition by cyanide. Immobilized catalase exhibited a Michaelis-Menten behaviour at low H(2)0(2) concentrations (<100mM) with apparent constant K(M)(app)=84±3mM and maximal initial velocity V(M)(app)=13.4?S min(-1). Inhibition by cyanide was found to be non-competitive and inhibition binding constant K(i) was 13.9±0.3?M. The decrease of the biosensor response by increasing cyanide concentration was linear up to 50?M, with a cyanide detection limit of 6?M. In parallel, electrochemical characteristics of the catalase/PVA biomembrane and its interaction with cyanide were studied by cyclic voltammetry and impedance spectroscopy. Addition of the biomembrane onto the gold electrodes induced a significant increase of the interfacial polarization resistance R(P). On the contrary, cyanide binding resulted in a decrease of Rp proportional to KCN concentration in the 4 to 50?M range. Inhibition coefficient I(50) calculated by this powerful label-free and substrate-free technique (24.3?M) was in good agreement with that determined from the substrate-dependent conductometric biosensor (24.9?M). PMID:20813591

Bouyahia, Naima; Hamlaoui, Mohamed Larbi; Hnaien, Mouna; Lagarde, Florence; Jaffrezic-Renault, Nicole

2010-08-14

291

Interleukin-10 is upregulated in LPS tolerance.  

PubMed

Lipopolysaccharide (LPS) stimulation of the human monocytic cell line Mono Mac 6 leads to rapid expression of both the pro-inflammatory cytokine tumor necrosis factor (TNF) and the anti-inflammatory cytokine interleukin-10 (IL-10). Preculture of these cells with a low dose of LPS for 2 days rendered the cells tolerant to subsequent stimulation, in that TNF gene expression is only minimal, both at the mRNA and at the protein level. IL-10 shows a reciprocal pattern, however, as expression of this gene is upregulated in precultured cells, and it will further increase upon subsequent stimulation. Although TNF has been shown to induce IL-10, and IL-10 was found to downregulate TNF, this reciprocal regulation does not explain the pattern observed in LPS tolerance in Mono Mac 6, since neutralizing antibodies against TNF and IL-10 could not prevent upregulation of IL-10 and downregulation of TNF, respectively. Treatment of Mono Mac 6 cells during LPS preculture with interferon-gamma (IFN-gamma) could, however, reverse tolerance: LPS/IFN-gamma precultured cells produced high levels of TNF transcripts upon subsequent stimulation, while the response of the IL-10 gene was attenuated. The data show that LPS tolerance does not involve a passive downregulation of all types of monocyte functions, but it is an orchestrated response with downregulation of pro- and upregulation of anti-inflammatory cytokines. PMID:7583353

Frankenberger, M; Pechumer, H; Ziegler-Heitbrock, H W

1995-01-01

292

Photosynthetic electron flow affects H2O2 signaling by inactivation of catalase in Chlamydomonas reinhardtii.  

PubMed

A specific signaling role for H(2)O(2) in Chlamydomonas reinhardtii was demonstrated by the definition of a promoter that specifically responded to this ROS. Expression of a nuclear-encoded reporter gene driven by this promoter was shown to depend not only on the level of exogenously added H(2)O(2) but also on light. In the dark, the induction of the reporter gene by H(2)O(2) was much lower than in the light. This lower induction was correlated with an accelerated disappearance of H(2)O(2) from the culture medium in the dark. Due to a light-induced reduction in catalase activity, H(2)O(2) levels in the light remained higher. Photosynthetic electron transport mediated the light-controlled down-regulation of the catalase activity since it was prevented by 3-(3'4'-dichlorophenyl)-1,1-dimethylurea (DCMU), an inhibitor of photosystem II. In the presence of light and DCMU, expression of the reporter gene was low while the addition of aminotriazole, a catalase inhibitor, led to a higher induction of the reporter gene by H(2)O(2) in the dark. The role of photosynthetic electron transport and thioredoxin in this regulation was investigated by using mutants deficient in photosynthetic electron flow and by studying the correlation between NADP-malate dehydrogenase and catalase activities. It is proposed that, contrary to expectations, a controlled down-regulation of catalase activity occurs upon a shift of cells from dark to light. This down-regulation apparently is necessary to maintain a certain level of H(2)O(2) required to activate H(2)O(2)-dependent signaling pathways. PMID:18781324

Shao, Ning; Beck, Christoph F; Lemaire, Stéphane D; Krieger-Liszkay, Anja

2008-09-10

293

Catalase and superoxide dismutase activities as biomarkers of oxidative stress in workers exposed to mercury vapors  

SciTech Connect

We investigated the role of three blood antioxidant enzyme activities and total antioxidant status (TAS) as biological markers of oxidative stress in workers exposed to mercury (Hg{degrees}) vapors. Twenty-two female workers took part in the study. Blood and urine sampling for biological analyses was performed. The workers were classified into three subgroups according to their creatinine-corrected Hg concentration in urine. Blood antioxidant enzyme activities and TAS were compared between groups with nonparametric distribution-free methods. A significant difference existed in catalase activity and a slight, but not significant, difference existed in Cu{sup 2+}/Zn{sup 2+} superoxide dismutase (Cu{sup 2+}/Zn{sup 2+} SOD) activity between the three groups. No differences were observed in either the glutathione peroxidase activity or the TAS between these groups. Catalase and Cu{sup 2+}/Zn{sup 2+} SOD activities were increased in the groups of workers with higher creatinine-corrected urinary Hg concentrations when compared with the group of lower creatinine-corrected urinary Hg concentrations. Catalase activity was positively correlated with the creatinine-corrected concentration of Hg in urine, and Cu{sup 2+}/Zn{sup 2+} SOD activity was slightly correlated with the creatinine-corrected concentration of Hg in urine. The role of erythrocyte catalase and Cu{sup 2}/Zn{sup 2+} SOD activities we have measured is in agreement with the hypothesis of the involvement of reactive oxygen species production as an important event in chronic exposure to Hg{degrees} vapors in humans. In spite of the small sample size, results indicate that erythrocyte catalase and Cu{sup 2+}/Zn{sup 2+} SOD activities could be considered as markers of biological effect in workers exposed to Hg{degrees} vapors. 24 refs., 3 figs., 2 tabs.

Perrin-Nadif, R.; Dusch, M.; Mur, J.M.; Koch, C. [INRS, Vandoeuvre-les-Nancy (France); Schmitt, P. [Association InterEntreprises de Medecine du Travail du Bas-Rhin, Strasbourg (France)

1996-06-07

294

Catalase and superoxide dismutase in alfalfa root nodules. [Medicago sativa L  

SciTech Connect

Catalase and superoxide dismutase (SOD), in scavenging H/sub 2/ O/sub 2/ and O/sub 2/, respectively, have been recently proposed to play a role in leghemoglobin protection. The occurrence of catalase and SOD activities in alfalfa (Medicago sativa L.) nodule cytosol is reported here. Enzymes were extracted at 0-4/sup 0/C from 0.5 g fresh nodules with 12 ml of a medium containing K-phosphate buffer 50 mM, pH 7.8 and Na/sub 2/EDTA 0.1 mM. The homogenate was filtered and centrifuged at 18,000 xg for 10 min, and the resulting supernatant was used for catalase assay. A further precipitation of leghemoglobin was required to avoid interferences with SOD determination. Catalase was determined by back-titration with KMnO/sub 4/. SOD was assayed by measuring the inhibition of nitro blue tetrazolium reduction. The sensitivity of SOD activity to CN/sup -/ was tested by including 1 mM KCN in the reaction mixture. Catalase activity of alfalfa nodule cytosol was 237 +/- 1 units/mg protein, decreasing very significantly (P < 0.01, Duncan's multiple range test) at 20 mM NO/sub 3//sup -/. Typical specific SOD activities were 94 +/- 5 and 65 +/- 4 units/mg protein, without CN/sup -/ and with CN/sup -/, respectively. Both activities increased very significantly at 20 mM NO/sub 3//sup -/. SOD activities with CN/sup -/ were 70-80% those without CN/sup -/ within the range of NO/sub 3//sup -/ investigated (0-20 mM).

Becana, M.; Aparicio-Tejo, P.M.; Sanchez-Diaz, M.

1986-04-01

295

Resonance Scattering Spectral Detection of Catalase Activity Using Au@Ag Nanoparticle as Probe and Coupling Catalase Catalytic Reaction with Fenton Reaction  

Microsoft Academic Search

The AucoreAgshell (Au@Ag) nanoparticles in size of 30 nm were prepared using 10 nm gold nanoparticles as seeds at 90°C, and were purified by\\u000a high-speed centrifugation to remove the excess trisodium citrate to obtain Au@Ag nanoprobe. In the medium of pH 4.0 acetate\\u000a buffer solution—7.2 ?mol\\/L H2O2–67 ?mol\\/L Fe(II), Au@Ag nanoparticles exhibited a resonance scattering (RS) peak at 538 nm. Upon addition of Catalase (Ct),\\u000a the

Aihui Liang; Yueyuan Liang; Zhiliang Jiang; Hesheng Jiang

2009-01-01

296

Understanding the role of the catalase/peroxide genes in H2O2 resistance of E. coli serotype O157:H7 biofilms  

Technology Transfer Automated Retrieval System (TEKTRAN)

Introduction: Escherichia coli serotype O157:H7 defenses against H2O2 include the peroxiredoxin AhpC and three catalases: KatG (catalase-peroxidase), KatE (catalase), and the plasmid-encoded KatP (catalase/peroxidase). AhpC, KatG, and KatP are induced by OxyR in exponential phase, while KatE is indu...

297

Differential activation of catalase expression and activity by PPAR agonists: Implications for astrocyte protection in anti-glioma therapy?  

PubMed Central

Glioma survival is dismal, in part, due to an imbalance in antioxidant expression and activity. Peroxisome proliferator-activated receptor (PPAR) agonists have antineoplastic properties which present new redox-dependent targets for glioma anticancer therapies. Herein, we demonstrate that treatment of primary cultures of normal rat astrocytes with PPAR agonists increased the expression of catalase mRNA protein, and enzymatic activity. In contrast, these same agonists had no effect on catalase expression and activity in malignant rat glioma cells. The increase in steady-state catalase mRNA observed in normal rat astrocytes was due, in part, to de novo mRNA synthesis as opposed to increased catalase mRNA stability. Moreover, pioglitazone-mediated induction of catalase activity in normal rat astrocytes was completely blocked by transfection with a PPAR?-dominant negative plasmid. These data suggest that defects in PPAR-mediated signaling and gene expression may represent a block to normal catalase expression and induction in malignant glioma. The ability of PPAR agonists to differentially increase catalase expression and activity in normal astrocytes but not glioma cells suggests that these compounds might represent novel adjuvant therapeutic agents for the treatment of gliomas.

Khoo, Nicholas K.H.; Hebbar, Sachin; Zhao, Weiling; Moore, Steven A.; Domann, Frederick E.; Robbins, Mike E.

2013-01-01

298

Differential activation of catalase expression and activity by PPAR agonists: Implications for astrocyte protection in anti-glioma therapy.  

PubMed

Glioma survival is dismal, in part, due to an imbalance in antioxidant expression and activity. Peroxisome proliferator-activated receptor (PPAR) agonists have antineoplastic properties which present new redox-dependent targets for glioma anticancer therapies. Herein, we demonstrate that treatment of primary cultures of normal rat astrocytes with PPAR agonists increased the expression of catalase mRNA protein, and enzymatic activity. In contrast, these same agonists had no effect on catalase expression and activity in malignant rat glioma cells. The increase in steady-state catalase mRNA observed in normal rat astrocytes was due, in part, to de novo mRNA synthesis as opposed to increased catalase mRNA stability. Moreover, pioglitazone-mediated induction of catalase activity in normal rat astrocytes was completely blocked by transfection with a PPAR?-dominant negative plasmid. These data suggest that defects in PPAR-mediated signaling and gene expression may represent a block to normal catalase expression and induction in malignant glioma. The ability of PPAR agonists to differentially increase catalase expression and activity in normal astrocytes but not glioma cells suggests that these compounds might represent novel adjuvant therapeutic agents for the treatment of gliomas. PMID:24024139

Khoo, Nicholas K H; Hebbar, Sachin; Zhao, Weiling; Moore, Steven A; Domann, Frederick E; Robbins, Mike E

2013-01-26

299

Synergistic Roles of Helicobacter pylori Methionine Sulfoxide Reductase and GroEL in Repairing Oxidant-damaged Catalase*  

PubMed Central

Hypochlorous acid (HOCl) produced via the enzyme myeloperoxidase is a major antibacterial oxidant produced by neutrophils, and Met residues are considered primary amino acid targets of HOCl damage via conversion to Met sulfoxide. Met sulfoxide can be repaired back to Met by methionine sulfoxide reductase (Msr). Catalase is an important antioxidant enzyme; we show it constitutes 4–5% of the total Helicobacter pylori protein levels. msr and katA strains were about 14- and 4-fold, respectively, more susceptible than the parent to killing by the neutrophil cell line HL-60 cells. Catalase activity of an msr strain was much more reduced by HOCl exposure than for the parental strain. Treatment of pure catalase with HOCl caused oxidation of specific MS-identified Met residues, as well as structural changes and activity loss depending on the oxidant dose. Treatment of catalase with HOCl at a level to limit structural perturbation (at a catalase/HOCl molar ratio of 1:60) resulted in oxidation of six identified Met residues. Msr repaired these residues in an in vitro reconstituted system, but no enzyme activity could be recovered. However, addition of GroEL to the Msr repair mixture significantly enhanced catalase activity recovery. Neutrophils produce large amounts of HOCl at inflammation sites, and bacterial catalase may be a prime target of the host inflammatory response; at high concentrations of HOCl (1:100), we observed loss of catalase secondary structure, oligomerization, and carbonylation. The same HOCl-sensitive Met residue oxidation targets in catalase were detected using chloramine-T as a milder oxidant.

Mahawar, Manish; Tran, ViLinh; Sharp, Joshua S.; Maier, Robert J.

2011-01-01

300

Immobilization of catalase via adsorption on poly(styrene- d-glycidylmethacrylate) grafted and tetraethyldiethylenetriamine ligand attached microbeads  

Microsoft Academic Search

Fibrous poly(styrene-d-glycidylmethacrylate) (P(S-GMA)) brushes were grafted on poly(styrene-divinylbenzene) (P(S-DVB)) beads using surface initiated-atom transfer radical polymerization (SI-ATRP). Tetraethyldiethylenetriamine (TEDETA) ligand was incorporated on P(GMA) block. The multi-modal ligand attached beads were used for reversible immobilization of catalase. The influences of pH, ionic strength and initial catalase concentration on the immobilization capacities of the P(S-DVB)-g-P(S-GMA)-TEDETA beads have been investigated. Catalase adsorption

Gulay Bayramoglu; Bunyamin Karagoz; Meltem Yilmaz; Niyazi Bicak; M. Yakup Arica

2011-01-01

301

A Laboratory Experiment Investigating Different Aspects of Catalase Activity in an Inquiry - Based Approach  

NASA Astrophysics Data System (ADS)

The action of the enzyme catalase on aqueous hydrogen peroxide to generate oxygen gas is a well-established demonstration (1-3). Catalase is typically obtained by aqueous extraction of a potato, and the potato extract is mixed together with 3% hydrogen peroxide. The oxygen that is produced can be collected over water. Variations on the procedure can demonstrate the dependence of catalytic activity on temperature or the presence of inhibitors (1, 2). The University of Colorado at Denver has used a version of this procedure as a laboratory in its second-semester course for nonmajors. Recently, students have been allowed to expand upon the procedures prescribed in the laboratory handout in an open-ended project format. We explored some of these variations in detail, and the results provided here offer ideas, centered around this laboratory, for open-ended projects that can be used in an inquiry-based approach.

Kimbrough, Doris R.; Magoun, Mary Ann; Langfur, Meg

1997-02-01

302

Diminishing of aggregation for bovine liver catalase through acidic residues modification.  

PubMed

The tendency of proteins to aggregate is an important problem in biotechnology and the pharmaceutical industry. Because proteins in the aggregated state generally do not have the same biological activity as proteins in the native state. In order to prevent aggregation, it is essential to know the effective parameters in anti-aggregation mechanism. Using a chemical protein modification approach, UV-vis and fluorescence spectroscopies and circular dichroism spectropolarimetry, this study investigates the parameters involved in anti-aggregation mechanism of bovine liver catalase. Our findings clearly indicate that the modified bovine liver catalase provides better protection than the native enzyme against thermal aggregation. It seems that a decrease in hydrophobicity resulting in chemical modification plays an important role in preventing aggregation. PMID:16828155

Hashemnia, S; Moosavi-Movahedi, A A; Ghourchian, H; Ahmad, F; Hakimelahi, G H; Saboury, A A

2006-06-06

303

Binding of chrysoidine to catalase: Spectroscopy, isothermal titration calorimetry and molecular docking studies.  

PubMed

Chrysoidine is an industrial azo dye and the presence of chrysoidine in water and food has become an environmental concern due to its negative effects on human beings. In this work, the interactions between chrysoidine and bovine liver catalase (BLC) were explored. Obvious loss in catalytic activity was observed after incubation of BLC with chrysoidine, and the inhibition effect of BLC was found to be of the non-competitive type. No profound conformational change of BLC occurs in the presence of chrysoidine as revealed by UV-vis absorption, circular dichroism and fluorescence spectroscopy studies. Isothermal titration calorimetry results indicate that catalase has two sets of binding sites for chrysoidine. Further, molecular docking simulations show that chrysoidine is located within the bottleneck in the main channel of the substrate to the active site of BLC, which explain the activity inhibition of BLC by chrysoidine. PMID:24001681

Yang, Bingjun; Hao, Fang; Li, Jiarong; Chen, Dongliang; Liu, Rutao

2013-08-15

304

Decrease in catalase activity of Folsomia candida fed a Bt rice diet.  

PubMed

Here we report the effects of three Bt-rice varieties and their non-Bt conventional isolines on biological traits including survival, reproduction, and the activities of three antioxidant enzymes superoxide dismutase, catalase and peroxidase, in the Collembolan, Folsomia candida. The reproduction was significantly lower when fed Kemingdao and Huahui1 than those feeding on their non-GM near-isogenic varieties Xiushui and Minghui63 respectively, this can be explained by the differences of plant compositions depended on variety of rice. The catalase activity of F. candida was significantly lower when fed the Bt-rice variety Kemingdao compared to the near-isogenic non-Bt-rice variety Xiushui. This suggests that some Bt-rice varieties may impose environmental stress to collembolans. We emphasize that changes in activity of antioxidant enzymes of non-target organisms are important in understanding the ecological consequences for organisms inhabiting transgenic Bt-rice plantations. PMID:21835518

Yuan, Yiyang; Ke, Xin; Chen, Fajun; Krogh, Paul Henning; Ge, Feng

2011-08-11

305

Cytochrome bd oxidase from Escherichia coli displays high catalase activity: an additional defense against oxidative stress.  

PubMed

Cytochrome bd oxygen reductase from Escherichia coli has three hemes, b558, b595 and d. We found that the enzyme, as-prepared or in turnover with O2, rapidly decomposes H2O2 with formation of approximately half a mole of O2 per mole of H2O2. Such catalase activity vanishes upon cytochrome bd reduction, does not compete with the oxygen-reductase activity, is insensitive to NO, CO, antimycin-A and N-ethylmaleimide (NEM), but is inhibited by cyanide (Ki ~2.5?M) and azide. The activity, possibly associated with heme-b595, was also observed in catalase-deficient E. coli cells following cytochrome bd over-expression suggesting a protective role against oxidative stress in vivo. PMID:23727202

Borisov, Vitaliy B; Forte, Elena; Davletshin, Albert; Mastronicola, Daniela; Sarti, Paolo; Giuffrè, Alessandro

2013-05-30

306

Investigation of lipid peroxidation and catalase activity in magnetic fluid treated mice  

NASA Astrophysics Data System (ADS)

The increasing interest in magnetic fluids (MFs) for biomedical applications demands a deeper knowledge of their effects in biological systems. To evaluate the in vivo response of a MF sample based on magnetite nanoparticles stabilized by a precoating double layer of dodecanoic acid plus ethoxylated polyalcohol (MFDE), the inflammation-related oxidative stress and antioxidant tissue response were both addressed in this study. MFDE sample was intraperitoneally administrated to mice at three different doses. The lipid peroxidation and the antioxidant defense induced in the liver and spleen were evaluated, respectively, by thiobarbituric acid-reactive substances (TBARS) and catalase activity, 1, 14, and 28 days after MFDE treatment. The liver and spleen responded with a huge increase in TBARS after MFDE treatment. We observed that oxidative changes as well as the variations in the liver catalase activity were time and MFDE-dose dependent.

Freitas, M. L. L.; Silva, L. P.; Freitas, J. L.; Azevedo, R. B.; Lacava, Z. G. M.; Homem de Bittencourt, P. I.; Curi, R.; Buske, N.; Morais, P. C.

2003-05-01

307

Catalase is encoded by a multigene family in Arabidopsis thaliana (L.) Heynh.  

PubMed Central

The catalase multigene family in Arabidopsis includes three genes encoding individual subunits that associate to form at least six isozymes that are readily resolved by nondenaturing gel electrophoresis. CAT1 and CAT3 map to chromosome 1, and CAT2 maps to chromosome 4. The nucleotide sequences of the three coding regions are 70 to 72% identical. The amino acid sequences of the three catalase subunits are 75 to 84% identical and 87 to 94% similar, considering conservative substitutions. Both the individual isozymes and the individual subunit mRNAs show distinct patterns of spatial (organ-specific) expression. Six isozymes are detected in flowers and leaves and two are seen in roots. Similarly, mRNA abundance of the three genes varies among organs. All three mRNAs are highly expressed in bolts, and CAT2 and CAT3 are highly expressed in leaves.

Frugoli, J A; Zhong, H H; Nuccio, M L; McCourt, P; McPeek, M A; Thomas, T L; McClung, C R

1996-01-01

308

Cytotoxicity of lawsone and cytoprotective activity of antioxidants in catalase mutant Escherichia coli.  

PubMed

Lawsone is an active naphthoquinone derivative isolated from henna (Lawsonia inermis L.), a widely used hair dye. Previous study on the toxicity of lawsone remains unclear since the involvement of oxidative stress and the kind of ROS (reactive oxygen species) involved have not been fully resolved yet. This present study reports the cytotoxic effects of lawsone and henna. We carried out CAT assay (a zone of inhibition test of bacterial growth and colony-forming efficiency test of transformant Escherichia coli strains that express mammalian catalase gene derived from normal catalase mice (Cs(a)) and catalase-deficient mutant mice (Cs(b))), Ames mutagenicity assay and H(2)O(2) generation assay. Lawsone generated H(2)O(2) slightly in phosphate buffer system and was not mutagenic in Ames assay using TA 98, TA 100 and TA 102, both in the absence and presence of metabolic activation. Lawsone exposure inhibited the growth of both Cs(a) and Cs(b) strains in a dose-dependent manner. Mean zone diameter for Cs(a) was 9.75+/-0.96 mm and 12.75+/-1.5 mm for Cs(b). Natural henna leaves did not show toxic effects, whereas two out of four samples of marketed henna products were shown toxicity effects. Catalase abolished zone of inhibition (ZOI) of marketed henna products, eliminated ZOI of lawsone in a dose-dependent manner and low concentration of exogenous MnSOD and Cu/ZnSOD eliminated the toxicity. Histidine and DTPA, the metal chelator; BHA and low concentration of capsaicin, the inducer of NADH-quinone reductase, effectively protected Cs(a) and Cs(b) against lawsone in this study. We suggest that lawsone cytotoxicity is probably mediated, at least in part, by the release of O(2)(-), H(2)O(2) and OH(-). PMID:17442476

Sauriasari, Rani; Wang, Da-Hong; Takemura, Yoko; Tsutsui, Ken; Masuoka, Noriyoshi; Sano, Kuniaki; Horita, Masako; Wang, Bing-Ling; Ogino, Keiki

2007-03-24

309

Catalase-like and superoxide dismutase-like activities in human seminal plasma  

Microsoft Academic Search

Human spermatozoa are highly susceptible to oxidative injury but are naturally protected from such injury by the antioxidant properties of seminal plasma. We measured catalase-like and superoxide dismutase (SOD)-like activities in the seminal plasma of fertile and vasectomized men in order to gain insight into the potential source(s) and function(s) of these antioxidants in semen. Semen samples were obtained from

A. Zini; M. Fischer; V. Mak; D. Phang; K. Jarvi

2002-01-01

310

Compounds I of Catalase and Horse Radish Peroxidase: pi -cation Radicals  

Microsoft Academic Search

Two-electron oxidation of cobaltous octa-ethylporphyrin [Co(II)(Et)8P] yields a stable pi -cation radical [Co(III)(Et)8P]2+\\\\cdot, the optical spectrum of which exhibits spectral changes dependent upon the nature of the counterion. Comparison of these spectra with those of Compounds I of horseradish peroxidase and catalase leads us to propose that these Compounds I contain a pi -cation radical of the heme prosthetic group.

D. Dolphin; A. Forman; D. C. Borg; J. Fajer; R. H. Felton

1971-01-01

311

Hydrogen Peroxide Formation and Catalase Activity in the Lactic Acid Bacteria  

Microsoft Academic Search

SUMMARY Some lactic acid bacteria formed detectable H202 and some did not, regardless of their preference or requirement for aerobic or anaerobic conditions. Whether or not H202 was formed depended in some instances on the substrate used as energy source. Two H202-splitting activities were encountered though never in the same organism. One, named pseudo- catalase activity, was insensitive to 0.01

R. Whittenbury

1964-01-01

312

Kinetic study of hydrogen peroxide decomposition by catalase in a flow-mix microcalorimetric system  

Microsoft Academic Search

The kinetics of hydrogen peroxide decomposition by the enzyme catalase was studied at pH 7.4 in the temperature range 10–30°C. Experiments were performed by the LKB-2277 Thermal Activity Monitor equipped with a flow-mix cylinder. The calorimetric reaction unit was schematised as a tubular reactor operating under plug-flow conditions. A first-order kinetic expression, with respect to both the substrate and the

Marcello Fidaleo; Roberto Lavecchia

2003-01-01

313

Influence on Erythropoiesis and Blood Catalase Activity Low Intensity Electromagnetic Millimeter Radiation  

Microsoft Academic Search

\\u000a The present study was undertaken to investigate changes of the blood catalase activity and regeneration processes in the circulatory\\u000a system of rabbits under conditions of bone-marrow deficiency and long-term exposure to lowpower extremely high frequency electromagnetic\\u000a radiation (EHF EMR) at frequency of 50.3 GHz. As it is known, this frequency is resonant for the vibrations of water hexagonal\\u000a structures[1]. During

Ts. I. Adamyan; E. S. Gevorgyan; H. H. Hovhanisyan; S. M. Minasyan; V. P. Kalantaryan; A. A. Hakhoumian

314

Resonance Raman spectra of bovine liver catalase: enhancement of proximal tyrosinate vibrations.  

PubMed

Resonance Raman spectra of native bovine liver ferri-catalase have been obtained in the 200-1800 cm-1 region. Excitation at a series of wavelengths ranging from 406.7 to 514.5 nm has been used and gives rise to distinct sets of resonance Raman bands. Excitation within the Soret and Q-bands of the heme group produces the expected set of polarized and nonpolarized porphyrin modes, respectively. The frequencies of the porphyrin skeletal stretching bands in the 1450-1700 cm-1 region indicate that catalase contains only five-coordinate, high-spin heme groups. In addition to the porphyrin modes, bovine liver catalase exhibits bands near 1612 and 1520 cm-1 that are attributable to ring vibrations of the proximal tyrosinate that are enhanced via resonance with a proximal tyrosinate----Fe(III) change transfer transition centered near 490 nm. Similar bands have been observed in mutant hemoglobins that have tyrosinate axial ligands and in other Fe(III)-tyrosinate proteins. No resonance Raman bands have been observed that can be attributed to degraded hemes. The spectra are relatively insensitive to pH over the range of 5-10, and the same spectra are observed for catalase samples that do and do not contain tightly bound NADPH. Resonance Raman spectra of the fluoride complex exhibit porphyrin skeletal stretching modes that show it to be six coordinate, high spin, while the cyanide complex is six coordinate, low spin. Both the azide and thiocyanate complexes, however, are spin-state mixtures with the high-spin form predominant. PMID:3236004

Chuang, W J; Johnson, S; Van Wart, H E

1988-11-01

315

Catalase inhibition by amino triazole induces oxidative stress in goldfish brain  

Microsoft Academic Search

The effects of in vivo inhibition of catalase by 3-amino 1,2,4-triazole (AMT) on the levels of damage products resulting from reactive oxygen species attack on proteins and lipids as well as on the activities of five antioxidant and associated enzymes were studied in the brain of goldfish, Carassius auratus. Intraperitoneal injection of AMT at a concentration of 0.1 mg\\/g wet

Tetyana V. Bagnyukova; Olena Yu. Vasylkiv; Kenneth B. Storey; Volodymyr I. Lushchak

2005-01-01

316

Direct evidence for catalase and peroxidase activities of ferritin–platinum nanoparticles  

Microsoft Academic Search

Using apoferritin (apoFt) as a nucleation substrate, we have successfully synthesized 1–2 nm platinum nanoparticles (Pt–Ft) which are highly stable. By directly measuring the products of Pt–Ft-catalyzed reactions, we showed, with no doubt, Pt–Ft possesses both catalase and peroxidase activities. With hydrogen peroxide as substrate, we observed oxygen gas bubbles were generated from hydrogen peroxide decomposed by Pt–Ft; the generation of

Jia Fan; Jun-Jie Yin; Bo Ning; Xiaochun Wu; Ye Hu; Mauro Ferrari; Gregory J. Anderson; Jingyan Wei; Yuliang Zhao; Guangjun Nie

2011-01-01

317

Morphometric cytochemistry of catalase and myeloperoxidase-containing granules in the rabbit polymorphonuclear leukocyte  

Microsoft Academic Search

Summary  Recently developed morphometric and statistical techniques were applied to the study of heterogeneity of the granule population of rabbit polymorphonuclear leukocytes. The cytochemical activities of myeloperoxidase and catalase were differentiated by incubation at pH 7.6, and pH 9.7 to 10.5, respectively. Each activity was found in more than one granule. Statistical evaluation suggested that in addition to the primary granule,

D. M. Zellmer; W. A. Shannon

1983-01-01

318

NAFENOPIN-INDUCED HEPATIC MICROBODY (PEROXISOME) PROLIFERATION AND CATALASE SYNTHESIS IN RATS AND MICE  

Microsoft Academic Search

Nafenopin (2-methyl-2(p-(1,2,3,4-tetrahydro-l-naphthyl)phenoxy)-propionic acid ; Su- 13437), a potent hypolipidemic compound, was administered in varying concentrations in ground Purina Chow to male and female rats, wild type (Csa strain) mice and acatalasemic (Csb strain) mice to determine the hepatic microbody proliferative and catalase-inducing effects . In all groups of animals, administration of nafenopin at dietary levels of 0 .125% and 0.25%

JARNARDAN K. REDDY; DANIEL L. AZARNOFF; DONALD J. SVOBODA; JADA D. PRASAD

319

UV photolysis of catalase revisited: a spectral study of photolytic intermediates  

Microsoft Academic Search

The 365-nm irradiation of 4.6 ?M (?1.1 mg\\/ml) catalase solutions in pH 7.4 phosphate buffer induces spectral modifications. Difference spectra show maxima at 434, 555, 584 nm at the beginning of the irradiation, then a final spectrum with a maximum at 568 nm and a shoulder at 530 nm is observed. These results suggest the formation of compound III (oxyferrous

Michel Aubailly; Josiane Haigle; Anne Giordani; Patrice Morlière; René Santus

2000-01-01

320

Characterization of a catalase-peroxidase from the hyperthermophilic archaeon Archaeoglobus fulgidus  

Microsoft Academic Search

A putative perA gene from Archaeoglobus fulgidus was cloned and expressed in Escherichia coli BL21(DE3), and the recombinant catalase-peroxidase was purified to homogeneity. The enzyme is a homodimer with a subunit molecular mass of 85 kDa. UV-visible spectroscopic analysis indicated the presence of protoheme IX as a prosthetic group (ferric heme), in a stoichiometry of 0.25 heme per subunit. Electron

Servé W. Kengen; Floris J. Bikker; Wilfred R. Hagen; Willem M. Vos; John Oost

2001-01-01

321

Effect of ascorbic acid on longevity, catalase and lipid peroxidation in Callosobruchus maculatus F  

Microsoft Academic Search

The natural defense against peroxidative damages inflicted by oxygen derived free radicals is provided by antioxygenic enzymes.\\u000a Feeding of exogenous antioxidants increases the life span of insects by decreasing age-independent susceptibility to death.\\u000a The present study describes the effect of L-ascorbic acid on the life span, catalase activity, and lipid peroxidation in Callosobruchus maculatus, a non-feeding insect. Life span studies

S. K. Garg; S. Mahajan

1993-01-01

322

Glyoxylate cycle enzymes and catalase in digitonin-fractionated mitochondria in Turbatrix aceti  

Microsoft Academic Search

Summary The subcellular localization of the glyoxylate cycle enzymes, isocitrate lyase and malate synthase, and the peroxisomal marker, catalase, was examined in 14-day-old cultures of the nematodeTurbatrix aceti. Glyoxylate cycle enzymes co-sedimented with selected mitochondrial enzymes during rate sedimentation. Two separate enzyme peaks were resolved after isopycnic centrifugation on a sucrose gradient: glyoxylate cycle enzymes, isocitrate lyase and malate synthase,

M. P. McKinley; R. N. Trelease

1978-01-01

323

Three-dimensional structure of the enzyme dimanganese catalase from Thermus Thermophilus at 1 Å resolution  

Microsoft Academic Search

The crystal structures of two forms of the enzyme dimanganese catalase from Thermus Thermophilus (native and inhibited by chloride) were studied by X-ray diffraction analysis at 1.05 and 0.98 resolution, respectively.\\u000a The atomic models of the molecules were refined to the R factors 9.8 and 10%, respectively. The three-dimensional molecular structures are characterized in detail. The analysis of\\u000a electron-density distributions

S. V. Antonyuk; V. R. Melik-Adamyan; A. N. Popov; V. S. Lamzin; P. D. Hempstead; P. M. Harrison; P. J. Artymyuk; V. V. Barynin

2000-01-01

324

The effect of supplementing hypothermic crystalloid cardioplegia with catalase plus allopurinol in the isolated rabbit heart  

Microsoft Academic Search

The effect of adding allopurinol and catalse to hypothermic cardioplegia for ischemic-reperfusion injury was investigated in the isolated rabbit heart. Hearts were divided into two groups, namely: Group C (n=7), which received a hypothermic crystalloid cardioplegic solution alone (4°C), and group T (n=7), which received the hypothermic cardioplegic solution with allopurinol (148 µmol\\/L)13 and catalase (37 nmol\\/L).12 The cardioplegic solution

Kazuya Nishida

1993-01-01

325

Evaluation of beam damage in catalase crystals observed in vitrified sections  

Microsoft Academic Search

It was a major breakthrough that Gleaser [1] quantitatively determined beam damage by measuring the fading of electron diffraction\\u000a spots in organic crystal. The method was soon extended to catalase crystal, which became a kind of working horse for quantitative\\u000a evaluation of specimen preparation methods [2,3]. For such purpose, catalse crystals are well suited because they can be grown\\u000a slowly

Hong-Mei Han; Bryant Gibson; Jacques Dubochet

326

Relation between catalase activity and fungal survival in lemon fruit infected by Phytophthora citrophthora  

Microsoft Academic Search

In lemon fruit inoculated with Phytophthora citrophthora, a continuous increase in H2O2 during the incubation and rot development periods was found at the infection site; seven to ten days after inoculation of the fungus, the mycelium and fruit cells were dead. The suggestion is made that the increase in H2O2 may be related to the decrease in catalase activity and

Eliahou Cohen; Mina Schiffmann-Nadel

1976-01-01

327

Low-Density Particles (W-Particles) Containing Catalase in Zellweger Syndrome and Normal Fibroblasts  

Microsoft Academic Search

By both histological and biochemical criteria, peroxisomes in patients with Zellweger syndrome appear to be absent or severely deficient. By using 15-30% (wt\\/vol) Nycodenz\\/sucrose gradients to study the subcellular localization of extraperoxisomal catalase activity, a commonly used marker for mature peroxisomes, we detected a single peak of activity in Zellweger syndrome fibroblasts at an equilibrium density of 1.13 g\\/cm^3, lower

J. Aikawa; W. W. Chen; R. I. Kelley; K. Tada; H. W. Moser; G. L. Chen

1991-01-01

328

Complete Nucleotide Sequence of cDNA and Deduced Amino Acid Sequence of Rat Liver Catalase  

Microsoft Academic Search

We have isolated five cDNA clones for rat liver catalase (hydrogen peroxide: hydrogen peroxide oxidoreductase, EC 1.11.1.6). These clones overlapped with each other and covered the entire length of the mRNA, which had been estimated to be 2.4 kilobases long by blot hybridization analysis of electrophoretically fractionated RNA. Nucleotide sequencing was carried out on these five clones and the composite

Shuichi Furuta; Hiroaki Hayashi; Makoto Hijikata; Shoko Miyazawa; Takashi Osumi; Takashi Hashimoto

1986-01-01

329

Thermotolerant Campylobacter with no or weak catalase activity isolated from dogs  

Microsoft Academic Search

ThermotolerantCampylobacter strains isolated from dog feces were characterized by phenotypical tests, DNA base composition, and DNA-DNA-hybridization. Out of 98 strains, 63 were catalase negative or weakly reacting (CNW); they were found in diarrheic as well as in healthy dogs. The CNW strains were all nalidixic-acid sensitive, hippurate negative, and grew at 42°C but not at 25°C. Seven strains were further

Karin Sandstedt; Jan Ursing; Mats Walder

1983-01-01

330

Extension of Life-Span with Superoxide Dismutase\\/Catalase Mimetics  

Microsoft Academic Search

We tested the theory that reactive oxygen species cause aging. We augmented the natural antioxidant systems of Caenorhabditis elegans with small synthetic superoxide dismutase\\/catalase mimetics. Treatment of wild-type worms increased their mean life-span by a mean of 44 percent, and treatment of prematurely aging worms resulted in normalization of their life-span (a 67 percent increase). It appears that oxidative stress

Simon Melov; Joanne Ravenscroft; Sarwatt Malik; Matt S. Gill; David W. Walker; Peter E. Clayton; Douglas C. Wallace; Bernard Malfroy; Susan R. Doctrow; Gordon J. Lithgow

2000-01-01

331

Biphasic character of fungal catalases inhibition with hydroxylamine in presence of hydrogen peroxide  

Microsoft Academic Search

The kinetics of hydrogen peroxide decomposition with fungal catalases, i.e. Aspergillus niger (ANC), Penicillium vitale (PVC), Scytalidium thermophilum (STC), exhibits biphasic character in the presence of hydroxylamine (HA). HA is inactive in the initial phase of the hydrogen peroxide decomposition. In the second phase, at pH 7.2, 30°C and 1mM H2O2 the concentration of the inhibitor that results in 50%

Juozas Kulys; Kostas Kriauciunas; Regina Vidziunaite

2003-01-01

332

Catalase and superoxide dismutase mimics for the treatment of inflammatory diseases  

Microsoft Academic Search

Conjugation of a metal ion chelator to aromatic amino acids generates a series of novel metal-binding anti-oxidant enzyme mimics. Our catalytic peptoids are designed to suppress oxidative damage via a number of routes. These include: (i) binding redox-active metal ions that further generate\\/activate RONS, (ii) removal of hydrogen peroxide by catalase activity, (iii) removal of superoxide by superoxide dismutase activity,

Anna E. O. Fisher; Suzette C. Maxwell; Declan P. Naughton

2003-01-01

333

cDNA cloning and differential gene expression of three catalases in pumpkin  

Microsoft Academic Search

Three cDNA clones (cat1, cat2, cat3) for catalase (EC 1.11.1.6) were isolated from a cDNA library of pumpkin (Cucurbita sp.) cotyledons. In northern blotting using the cDNA-specific probe, the cat1 mRNA levels were high in seeds and early seedlings of pumpkin. The expression pattern of cat1 was similar to that of malate synthase, a characteristic enzyme of glyoxysomes. These data

Muneharu Esaka; Naoko Yamada; Masao Kitabayashi; Yuji Setoguchi; Ryuji Tsugeki; Maki Kondo; Mikio Nishimura

1997-01-01

334

Superoxide dismutase, catalase, glutathione peroxidase and NADPH oxidase in lead-induced hypertension  

Microsoft Academic Search

Superoxide dismutase, catalase, glutathione peroxidase and NADPH oxidase in lead-induced hypertension.BackgroundEarlier studies from this laboratory have revealed the presence of oxidative stress and its role in the pathogenesis of lead-induced hypertension (HTN). We have further shown evidence of increased hydroxyl radical (·OH) and superoxide production in lead-treated rats and cultured endothelial cells. This study was designed to determine whether oxidative

Nosratola D Vaziri; Ching-Yi Lin; Farbod Farmand; Ram K Sindhu

2003-01-01

335

Glutathione, Glutathione-Related Enzymes, and Catalase Activities in the Earthworm Eisenia fetida andrei  

Microsoft Academic Search

.   The aim of this work was to provide basic data on the antioxidant defences in the annelid Eisenia fetida andrei (E. f. a.). Methods for measurement of three antioxidant enzymes—catalase (CAT), glutathione peroxidase (GPX), and glutathione\\u000a reductase (GR)—and of glutathione-S-transferase (GST) were optimized. GPX activity differed according to the substrate used:\\u000a cumene hydroperoxide (CUOOH) or hydrogen peroxide (H2O2). The

M. Saint-Denis; F. Labrot; J. F. Narbonne; D. Ribera

1998-01-01

336

Purification, characterization, and primary structure of a monofunctional catalase from Methanosarcina barkeri  

Microsoft Academic Search

Methanosarcina barkeri is a strictly anaerobic, cytochrome-containing, methane-forming archaeon. We report here that the microorganism contains\\u000a a catalase, which was purified and characterized. The enzyme with an apparent molecular mass of 190 kDa was shown to be composed\\u000a of four identical subunits of apparent molecular mass of 54 kDa. The heme-containing enzyme did not exhibit peroxidase activity,\\u000a which indicates that

Seigo Shima; Alexander Netrusov; Melanie Sordel; Michaela Wicke; Gudrun C. Hartmann; Rudolf K. Thauer

1999-01-01

337

A structural and dynamic investigation of the inhibition of catalase by nitric oxide.  

PubMed

Determining the chemical and structural modifications occurring within a protein during fundamental processes such as ligand or substrate binding is essential to building up a complete picture of biological function. Currently, significant unanswered questions relate to the way in which protein structural dynamics fit within the structure-function relationship and to the functional role, if any, of bound water molecules in the active site. Addressing these questions requires a multidisciplinary approach and complementary experimental techniques that, in combination, enhance our understanding of the complexities of protein chemistry. We exemplify this philosophy by applying both physical and biological approaches to investigate the active site chemistry that contributes to the inhibition of the Corynebacterium glutamicum catalase enzyme by nitric oxide. Ultrafast two-dimensional infrared spectroscopy (2D-IR) experiments exploit the NO ligand as a local probe of the active site molecular environment and shows that catalase displays a dynamically-restricted, 'tight,' structure. X-ray crystallography studies of C. glutamicum catalase confirm the presence of a conserved chain of hydrogen-bonded bound water molecules that link the NO ligand and the protein scaffold. This combination of bound water and restricted dynamics stands in stark contrast to other haem proteins, such as myoglobin, that exhibit ligand transport functionality despite the presence of a similar distal architecture in close proximity to the ligand. We conclude not only that the bound water molecules in the catalase active site play an important role in molecular recognition of NO but also may be part of the mechanistic operation of this important enzyme. PMID:24121528

Candelaresi, Marco; Gumiero, Andrea; Adamczyk, Katrin; Robb, Kirsty; Bellota-Antón, César; Sangal, Vartul; Munnoch, John; Greetham, Gregory M; Towrie, Michael; Hoskisson, Paul A; Parker, Anthony W; Tucker, Nicholas P; Walsh, Martin A; Hunt, Neil T

2013-10-11

338

Role of catalase in the smooth muscle relaxant actions of sodium azide and cyanamide  

Microsoft Academic Search

The aim of this study was to determine the role of catalase in the smooth muscle relaxant actions of sodium azide and cyanamide. The effects of 3-amino-1,2,4-triazole suggested a role for this enzyme in the relaxant actions of sodium azide on rat aorta and bovine retractor penis muscle and cyanamide on rat aorta. Moreover, results obtained using a difference spectrophotometric

Mohammad Shahidullah; Andrew Duncan; Peter D Strac?an; Komel M Rafique; Sarah L Ball; Mark J. W McPate; Silvia Nelli; William Martin

2002-01-01

339

The Euryhaline Yeast Debaryomyces hansenii has Two Catalase Genes Encoding Enzymes with Differential Activity Profile  

Microsoft Academic Search

Debaryomyces hansenii is a spoilage yeast able to grow in a variety of ecological niches, from seawater to dairy products. Results presented in\\u000a this article show that (i) D. hansenii has an inherent resistance to H2O2 which could be attributed to the fact that this yeast has a basal catalase activity which is several-fold higher than that\\u000a observed in Saccharomyces

Claudia Segal-Kischinevzky; Beatriz Rodarte-Murguía; Victor Valdés-López; Guillermo Mendoza-Hernández; Alicia González; Luisa Alba-Lois

2011-01-01

340

Antioxidative Effect of Glucose Oxidase and Catalase in Mayonnaises of Different Oxidative Susceptibility. II. Mathematical Modelling  

Microsoft Academic Search

A theoretical assessment was made of whether the enzyme system glucose oxidase\\/catalase (GOX\\/CAT) has an antioxidative effect in a food model consisting of an O\\/W emulsion packed in an oxygen-permeable plastic bag. This model represents food products such as mayonnaises and other high-fat dressings. The various oxygen transport and consumption processes were analysed theoretically and their relative significance estimated. This

Anette Isaksen; Jens Adler-Nissen

1997-01-01

341

Antioxidative Effect of Glucose Oxidase and Catalase in Mayonnaises of Different Oxidative Susceptibility. I. Product Trials  

Microsoft Academic Search

The antioxidative effect of the enzyme system glucose oxidase\\/catalase (GOX\\/CAT) in mayonnaises containing different amounts of fish oil stored at 25 °C was investigated. A complete block experiment was carried out with enzyme concentrations of 0, 400 and 800 units\\/kg, fish oil fractions of 0, 0.25 and 0.50 of the oil phase, and packaging of the mayonnaises in oxygen-permeable and

Anette Isaksen; Jens Adler-Nissen

1997-01-01

342

THE EFFECT OF MICROWAVE RADIATION ON CATALASE EXTRACTED FROM TARAXACUM ROOTS  

Microsoft Academic Search

SUMMARY The effect of the microwave on the enzyme activity is an appealing research subject with many applications. The root of Taraxacum officianle is a rich source for catalase. The enzyme can be easily extracted by homogenization in phosphate buffer. The optimal pH for enzyme activity was 7, at an optimal concentration of H2O2 around 50 mM. The optimal temperature

Laura Popet; Ana-Maria Lacrama; Adriana Isvoran; Vasile Ostafe

2006-01-01

343

Superoxide Dismutase, Peroxidatic Activity and Catalase in Mycobacterium leprae Purified from Armadillo Liver  

Microsoft Academic Search

~~ Superoxide dismutase has been identified and peroxidatic activity demonstrated in Mycobacterium leprae. The superoxide dismutase, shown indirectly to be a manganese- containing enzyme, was present at low activity in the cell-free extract. Peroxidatic activity was detected in a haemoprotein on polyacrylamide gels, but quantitative assay was not possible. Catalase, although present in a cell-free extract, appeared to be a

P. R. WHEELER; D. GREGORY

1980-01-01

344

Automated evaluation of the effect of ionic liquids on catalase activity.  

PubMed

An automated assay for the evaluation of the influence of ionic liquids on the activity of catalase was developed. The activity and inhibition assays were implemented in a sequential injection analysis (SIA) system and intended to contribute for the estimation of the toxicity of the tested compounds. The fast developed methodology was based on the oxidation of the non-fluorescent probe amplex red, in the presence of H?O?, to produce resorufin, a strong fluorescent compound. Catalase activity was monitored by the decreased of the fluorescence intensity due to the consumption of H?O? by the enzyme. The activity assays were performed in strictly aqueous media and in the presence of increasing concentrations of seven commercially available ionic liquids and sodium azide, a strong inhibitor of catalase. IC?? values between 0.15 and 2.77 M were obtained for the tested compounds, revealing distinct inhibitory effects. This allowed us to perform some considerations about the toxicity of the tested cations and anions. The developed SIA methodology showed to be robust and exhibited good repeatability in all the assay conditions. On the other hand, it proved to be in good agreement with the actual concerns of "Green Chemistry" since it involved the consumption of less than 200 ?L of reagents and the production of only 1.7 mL of effluent (per cycle) and at the same time reduced the operator exposure resulting in increased environmental and human safety. PMID:21185058

Pinto, Paula C A G; Costa, Andreia D F; Lima, José L F C; Saraiva, M Lúcia M F S

2010-12-23

345

On the role of catalase in the oxidation of tissue fatty acids  

SciTech Connect

The role of catalase in lipid metabolism has been studied by means of a comparison of the turnover characteristics of the major lipid classes in the normal mouse with those of animals in which the catalase activity had been inhibited and blocked by aminotriazole and allylisopropylacetamide. Double isotope ratios were determined in the lipid fractions of several tissues following the injection of labeled glycerol, and a number of significant differences were identified between these treatments. Since catalase is recognized as an integral component of the peroxisomal pathway of fatty acid oxidation, these results may be taken as indicating that interruption of the process of peroxisomal beta-oxidation in this manner cause extensive perturbations of lipid metabolism in the living animal, and these perturbations extend well beyond those tissues where the predominant localization of these organelles occurs. The concept which derives from these data--that of a significant regulatory role of peroxisomes in relation to the overall balance of lipid metabolism in the animal body--is described and discussed.

Crane, D.; Masters, C.

1984-02-15

346

Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity  

SciTech Connect

Melanogenesis is regulated in large part by tyrosinase, and defective tyrosinase leads to albinism. The mechanisms for other pigmentation determinants (e.g., those operative in tyrosinase-positive albinism and in murine coat-color mutants) are not yet known. One murine pigmentation gene, the brown (b) locus, when mutated leads to a brown (b/b) or hypopigmentated (B{sup lt}/B{sup lt}) coat versus the wild-type black (B/B). The authors show that the b locus codes for a glycoprotein with the activity of a catalase (catalase B). Only the c locus protein is a tyrosinase. Because peroxides may be by-products of melanogenic activity and hydrogen peroxide in particular is known to destroy melanin precursors and melanin, they conclude that pigmentation is controlled not only by tyrosinase but also by a hydroperoxidase. The studies indicate that catalase B is identical with gp75, a known human melanosomal glycoprotein; that the b mutation is in a heme-associated domain; and that the B{sup lt} mutation renders the protein susceptible to rapid proteolytic degradation.

Halaban, R.; Moellmann, G. (Yale Univ. School of Medicine, New Haven, CT (USA))

1990-06-01

347

Superoxide dismutase and catalase conjugated to polyethylene glycol increases endothelial enzyme activity and oxidant resistance  

SciTech Connect

Covalent conjugation of superoxide dismutase and catalase with polyethylene glycol (PEG) increases the circulatory half-lives of these enzymes from <10 min to 40 h, reduced immunogenicity, and decreases sensitivity to proteolysis. Because PEG has surface active properties and can induce cell fusion, the authors hypothesized that PEG conjugation could enhance cell binding and association of normally membrane-impermeable enzymes. Incubation of cultured porcine aortic endothelial cells with /sup 125/I-PEG-catalase or /sup 125/I-PEG-superoxide dismutase produced a linear, concentration-dependent increase in cellular enzyme activity and radioactivity. Fluorescently labeled PEG-superoxide dismutase incubated with endothelial cells showed a vesicular localization. Mechanical injury to cell monolayers, which is known to stimulate endocytosis, further increased the uptake of fluorescent PEG-superoxide dismutase. Addition of PEG and PEG-conjugated enzymes perturbed the spin-label binding environment, indicative of producing an increase in plasma membrane fluidity. Thus, PEG conjugation to superoxide dismutase and catalase enhances cell association of these enzymes in a manner which increases cellular enzyme activities and provides prolonged protection from partially reduced oxygen species.

Beckman, J.S.; Minor, R.L. Jr.; White, C.W.; Repine, J.E.; Rosen, G.M.; Freeman, B.A.

1988-05-15

348

Cytoplasmic superoxide dismutase and catalase activity and resistance to radiation lethality in murine tumor cells  

SciTech Connect

Reduced species of molecular oxygen are produced by the interaction of ionizing radiation with aqueous solutions containing molecular oxygen. The enzymes catalase and superoxide dismutase (SOD) are thought to function in vivo as scavengers of metabolically produced peroxide and superoxide respectively. SOD has been shown to protect against the lethal effects of ionizing radiation in vitro and in vivo. The authors have investigated the relationship between the cytosolic SOD catalase content and the sensitivity to radiation lethality of a number of murine cell lines (402AX, EL-4, MB-2T3, MB-4, MEL, P-815, SAI, SP-2, and SV-3T3). K/sub i/(CN/sup -/) for murine Cu-Zn-SOD was determined to be 6.8 x 10/sup -6/ M. No cytosolic Mn-SOD activity was found in any of the cell lines studied. No correlation was found between the cytosolic Cu-Zn-SOD or cytosolic catalase activity and the resistance to radiation lethality or the murine cell lines studied.

Davy, C.A.; Tesfay, Z.; Jones, J.; Rosenberg, R.C.; McCarthy, C.; Rosenberg, S.O.

1986-05-01

349

Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity.  

PubMed Central

Melanogenesis is regulated in large part by tyrosinase (monophenol monooxygenase; monophenol, L-dopa:oxygen oxidoreductase, EC 1.14.18.1), and defective tyrosinase leads to albinism. The mechanisms for other pigmentation determinants (e.g., those operative in tyrosinase-positive albinism and in murine coat-color mutants) are not yet known. One murine pigmentation gene, the brown (b) locus, when mutated leads to a brown (b/b) or hypopigmented (Blt/Blt) coat versus the wild-type black (B/B). We show that the b locus codes for a glycoprotein with the activity of a catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase, EC 1.11.1.6) (catalase B). Only the c locus protein is a tyrosinase. Because peroxides may be by-products of melanogenic activity and hydrogen peroxide in particular is known to destroy melanin precursors and melanin, we conclude that pigmentation is controlled not only by tyrosinase but also by a hydroperoxidase. Our studies indicate that catalase B is identical with gp75, a known human melanosomal glycoprotein; that the b mutation is in a heme-associated domain; and that the Blt mutation renders the protein susceptible to rapid proteolytic degradation. Images

Halaban, R; Moellmann, G

1990-01-01

350

Fe(III) complexes of 1,4,8,11-tetraaza[14]annulenes as catalase mimics.  

PubMed

The development of enzyme mimics of catalase which decompose hydrogen peroxide to water and molecular oxygen according to the 2:1 stoichiometry of native catalase and in aqueous solution at pH 7 and at micromolar concentrations of the enzyme model and hydrogen peroxide is reported. For this purpose, iron(III) complexes of 1,4,8,11-tetraaza[14]annulenes are prepared by various procedures. Efficacious preparations utilize reaction of the [N4] macrocyles with FeII salts in the presence of triphenylamine, followed by gentle oxidation of the FeII complexes by molecular oxygen or by tris(4-bromophenyl)aminium hexachloroantimonate. The complexes are characterized by SQUID magnetometry and by Mössbauer, EPR, and UV/vis spectrometry. In the solid state, the iron(III) center of the catalytically active complexes exists in the intermediate (quartet, S = 3/2) spin state. Several of these complexes decompose hydrogen peroxide in aqueous buffer solution at pH 7.2 at room temperature with turnover numbers between 40 and 80. The apparent second-order rate constant for hydrogen peroxide decomposition is in the range of 1400-2400 M(-1) s(-1), about 3 orders of magnitude lower than the value for native catalase. Besides oxygen production, a non-oxygen releasing pathway of hydrogen peroxide decomposition is unveiled. PMID:18001111

Sustmann, Reiner; Korth, Hans-Gert; Kobus, Diana; Baute, Jörg; Seiffert, Karl-Heinz; Verheggen, Elisabeth; Bill, Eckhard; Kirsch, Michael; de Groot, Herbert

2007-11-15

351

Nucleotide diversity and gene expression of Catalase and Glutathione peroxidase in irradiated Scots pine (Pinus sylvestris L.) from the Chernobyl exclusion zone.  

PubMed

In the Chernobyl exclusion zone forest trees have to tolerate and to adapt to ionizing radiation, therefore the molecular basis of their adaptive responses is of the utmost interest. Based on SNP analysis and real time PCR nucleotide diversity and expression profiles of gene fragments of catalase (Cat) and glutathione peroxidase (GPx), which are known as radical scavenging genes, were analysed in the needles of irradiated pine trees of the Chernobyl exclusion zone. In acutely and chronically irradiated trees (50 years old) planted before the accident a higher nucleotide diversity of Cat and more somatic mutations were found compared to their control. Chronically irradiated trees (20 years old) planted after the accident showed a similar nucleotide diversity of Cat compared to their control and in both collectives one somatic mutation was found. The nucleotide diversity of GPx was higher in all analysed trees compared to Cat. No somatic mutation events were found in GPx. For both gene fragments, no association between the received dose in a tree and the nucleotide diversity and mutation events was detected. The expression profiles of Cat and GPx in acutely and chronically and in chronically irradiated trees were similar. Compared to their corresponding control collectives, Cat was up-regulated and GPx slightly down-regulated. PMID:22304996

Vornam, Barbara; Arkhipov, Andrey; Finkeldey, Reiner

2011-11-29

352

Dynamics of Erythrocyte Count, Hemoglobin, and Catalase Activity in Rat Blood in Hypokinesia, Muscular Activity and Restoration.  

National Technical Information Service (NTIS)

Tests were conducted to prove that muscular exertion (in this instance swimming) of different duration and intensity, as well as hypodynamia, result in an increase of hemoglobin and number of red blood cells in peripheral blood rats. Catalase activity inc...

G. V. Taneyeva G. M. Potapovich N. A. Voloshko A. B. Uteshev

1980-01-01

353

Targeting of human catalase to peroxisomes is dependent upon a novel COOH-terminal peroxisomal targeting sequence  

PubMed Central

We have identified a novel peroxisomal targeting sequence (PTS) at the extreme COOH terminus of human catalase. The last four amino acids of this protein (-KANL) are necessary and sufficient to effect targeting to peroxisomes in both human fibroblasts and Saccharomyces cerevisiae, when appended to the COOH terminus of the reporter protein, chloramphenicol acetyl transferase. However, this PTS differs from the extensive family of COOH-terminal PTS tripeptides collectively termed PTS1 in two major aspects. First, the presence of the uncharged amino acid, asparagine, at the penultimate residue of the human catalase PTS is highly unusual, in that a basic residue at this position has been previously found to be a common and critical feature of PTS1 signals. Nonetheless, this asparagine residue appears to constitute an important component of the catalase PTS, in that replacement with aspartate abolished peroxisomal targeting (as did deletion of the COOH-terminal four residues). Second, the human catalase PTS comprises more than the COOH-terminal three amino acids, in that COOH-terminal-ANL cannot functionally replace the PTS1 signal-SKL in targeting a chloramphenicol acetyl transferase fusion protein to peroxisomes. The critical nature of the fourth residue from the COOH terminus of the catalase PTS (lysine) is emphasized by the fact that substitution of this residue with a variety of other amino acids abolished or reduced peroxisomal targeting. Targeting was not reduced when this lysine was replaced with arginine, suggesting that a basic amino acid at this position is required for maximal functional activity of this PTS. In spite of these unusual features, human catalase is sorted by the PTS1 pathway, both in yeast and human cells. Disruption of the PAS10 gene encoding the S. cerevisiae PTS1 receptor resulted in a cytosolic location of chloramphenicol acetyl transferase appended with the human catalase PTS, as did expression of this protein in cells from a neonatal adrenoleukodystrophy patient specifically defective in PTS1 import. Furthermore, through the use of the two-hybrid system, it was demonstrated that both the PAS10 gene product (Pas10p) and the human PTS1 receptor can interact with the COOH-terminal region of human catalase, but that this interaction is abolished by substitutions at the penultimate residue (asparagine-to- aspartate) and at the fourth residue from the COOH terminus (lysine-to-glycine) which abolish PTS functionality. We have found no evidence of additional targeting information elsewhere in the human catalase protein. An internal tripeptide (-SHL-, which conforms to the mammalian PTS1 consensus) located nine to eleven residues from the COOH terminus has been excluded as a functional PTS. Additionally, in contrast to the situation for S. cerevisiae catalase A, which contains an internal PTS in addition to a COOH-terminal PTS1, human catalase lacks such a redundant PTS, as evidenced by the exclusive cytosolic location of human catalase mutated in the COOH-terminal PTS. Consistent with this species difference, fusions between catalase A and human catalase which include the catalase A internal PTS are targeted, at least in part, to peroxisomes regardless of whether the COOH-terminal human catalase PTS is intact.

1996-01-01

354

Cloning and characterization of the rice CatA catalase gene, a homologue of the maize Cat3 gene  

Microsoft Academic Search

We isolated and sequenced a genomic clone (CatA) encoding CAT-A catalase, a homologue of the maize catalase isozyme 3 (CAT-3) from rice (Oryza sativa L.). The 5'-upstream non-coding region had very low similarity with the maize Cat3 gene and possible cis elements and sequence motifs in the maize Cat3 gene were not evident, except for TATA and CAAT motifs. Several

Kenichi Higo; Hiromi Higo

1996-01-01

355

Structure of Helicobacter pylori Catalase, with and without Formic Acid Bound, at 1.6 Å Resolution †  

Microsoft Academic Search

Helicobacter pylori produces one monofunctional catalase, encoded by katA (hp0875). The crystal structure of H. pylori catalase (HPC) has been determined and refined at 1.6 Å with crystallographic agreement factors R and Rfree of 17.4 and 21.9%, respectively. The crystal exhibits P21212 space group symmetry and contains two protein subunits in the asymmetric unit. The core structure of the HPC

Peter C. Loewen; Xavi Carpena; Carme Rovira; Anabella Ivancich; Rosa Perez-Luque; Rainer Haas; Stefan Odenbreit; Peter Nicholls; Ignacio Fita

2004-01-01

356

Direct electrochemistry and electrocatalytic activity of catalase incorporated onto multiwall carbon nanotubes-modified glassy carbon electrode  

Microsoft Academic Search

The direct voltammetry and electrocatalytic properties of catalase, which was adsorbed on the surface of multiwall carbon nanotubes (MWCNTs), was investigated. A pair of well-defined and nearly reversible cyclic voltammetry peaks for Fe(III)\\/Fe(II) redox couple of catalase adsorbed on the surface of MWCNTs at approximately ?0.05V versus reference electrode in pH 6.5 buffer solution, indicating the direct electron transfer between

Abdollah Salimi; Abdollah Noorbakhsh; Mahmoud Ghadermarz

2005-01-01

357

Intracellular distinction between peroxidase and catalase in exocrine cells of rat lacrimal gland: A biochemical and cytochemical study  

Microsoft Academic Search

Summary  The lacrimal gland (Glandula orbitalis externa) of rat contains both peroxidase and catalase and was used as a model for biochemical\\u000a and cytochemical distinction between peroxidase and catalase. Both enzymes were isolated by ammonium sulfate precipitation\\u000a from tissue homogenates, and the effects of fixation with glutaraldehyde and various conditions of incubation were investigated\\u000a colorimetrically using DAB as hydrogen donor. The

V. Herzog; H. D. Fahimi

1976-01-01

358

Purication and Partial Characterization of Catalase from Chicken Erythrocytes and the Eect of Various Inhibitors on Enzyme Activity  

Microsoft Academic Search

Catalase plays a major role in the protection of tissues from the toxic eects of H2O2 and partially reduced oxygen species. A nearly 136-fold enzyme purication was obtained from chicken erythrocyte by acetone precipitation, ethanol-chloroform treatment, CM-cellulose and Sephadex G-200 chromatography. The specic activity of puried enzyme was 42,556 U\\/mg. The molecular weight of the native chicken erythrocyte catalase was

Tulin AYDEM; Kevser KURU

359

Screening of Bacterial Isolates from Polluted Soils Exhibiting Catalase and Peroxidase Activity and Diversity of their Responses to Oxidative Stress  

Microsoft Academic Search

For the survival of individual isolates of gram-negative bacteria Pseudomonas putida, Achromobacter xylosoxidans, and the gram-positive bacterium Bacillus megaterium, in an environment polluted with crude oil products, the production of catalases exhibiting both catalase and dianisidine-peroxidase\\u000a activity is important. Electrophoretic resolution of cell-free extracts of aerobically grown strains in Luria–Bertani medium\\u000a during exponential phase revealed distinctive expression of catalatic and

Mária Bu?ková; Jana Godo?íková; Marcel Zámocký; Bystrík Polek

2010-01-01

360

Role of catalase in ethanol-induced conditioned taste aversion: a study with 3-amino-1,2,4-triazole  

Microsoft Academic Search

Recent studies involved acetaldehyde, the first ethanol metabolite, in both the rewarding and aversive effects of ethanol consumption. Brain acetaldehyde is believed to originate mainly from local brain metabolism of ethanol by the enzyme catalase. Therefore, the inhibition of catalase by 3-amino-1,2,4-triazole (aminotriazole) may help to clarify the involvement of acetaldehyde in ethanol's hedonic effects. In the present study, multiple

Etienne Quertemont; M. Dolores Escarabajal; Philippe De Witte

2003-01-01

361

cDNA cloning, characterization and expression analysis of the antioxidant enzyme gene, catalase, of Chinese shrimp Fenneropenaeus chinensis  

Microsoft Academic Search

Catalase is an important antioxidant protein that protects organisms against various oxidative stresses by eliminating hydrogen peroxide. The full-length catalase cDNA of Chinese shrimp Fenneropenaeus chinensis was cloned from the hepatopancreas using degenerate primers by the method of 3? and 5? rapid amplification of cDNA ends PCR. The cDNA sequence consists of 1892bp with a 1560bp open reading frame, encoding

Qingli Zhang; Fuhua Li; Xiaojun Zhang; Bo Dong; Jiquan Zhang; Yusu Xie; Jianhai Xiang

2008-01-01

362

Catalase activity in macro- and microorganisms as an indicator of biotic stress in coastal waters of the eastern Mediterranean Sea  

Microsoft Academic Search

In this study we examined the activity of catalase in the water column (mainly attributed to planktonic microorganisms) and\\u000a the activity of catalase and superoxide dismutase (SOD), as well as lipid peroxidation in the midgut gland of the benthic\\u000a bivalve Donax trunculus as possible indicators of biotic stress. The measurements were performed at stations situated at known contaminated and clean

D. L. Angel; U. Fiedler; N. Eden; N. Kress; D. Adelung; B. Herut

1999-01-01

363

Characterization of transgenic tomato plants expressing an antisense catalase gene and cloning of a TOMCAT2 gene  

Microsoft Academic Search

Transgenic tomatoes (Lycopersicon esculentum Mill. ‘Ohio 8245’) expressing an antisense catalase gene (ASTOMCAT1) were used to test the hypothesis that modification of the reactive oxygen species scavenging mechanism in plants can lead to changes in oxidative strew tolerance. A two to eight-fold reduction in total catalase activity and a two-fold increase in levels of H2O2 were detected in the leaf

Kanogwan Kerdnaimongkol

1999-01-01

364

A novel biosensor for specific determination of hydrogen peroxide: catalase enzyme electrode based on dissolved oxygen probe  

Microsoft Academic Search

A biosensor for the specific determination of hydrogen peroxide was developed using catalase (EC 1.11.1.6) in combination with a dissolved oxygen probe. Catalase was immobilized with gelatin by means of glutaraldehyde and fixed on a pretreated teflon membrane served as enzyme electrode. The electrode response was maximum when 50 mM phosphate buffer was used at pH 7.0 and at 35°C.

Sinan Akgöl; Erhan Dinçkaya

1999-01-01

365

Catalase alleviates cardiomyocyte dysfunction in diabetes: role of Akt, Forkhead transcriptional factor and silent information regulator 2  

Microsoft Academic Search

Oxidative stress has been speculated to play an essential role in diabetic cardiomyopathy. This study was designed to examine the effect of the antioxidant catalase on diabetes-induced cardiomyocyte dysfunction and the cellular mechanisms involved. Adult wild-type (FVB) and transgenic mice with cardiac-specific overexpression of catalase were made diabetic by a single injection of streptozotocin (STZ, 220 mg\\/kg; i.p., maintained for two

Subat Turdi; Qun Li; Faye L. Lopez; Jun Ren

2007-01-01

366

Two temporally synthesized charge subunits interact to form the five isoforms of cottonseed (Gossypium hirsutum) catalase.  

PubMed Central

Five charge isoforms of tetrameric catalase were isolated from cotyledons of germinated cotton (Gossypium hirsutum L.) seedlings. Denaturing isoelectric focusing of the individual isoforms in polyacrylamide gels indicated that isoforms A (most anodic) and E (most cathodic) consisted of one subunit of different charge, whereas isoforms B, C and D each consisted of a mixture of these two subunits. Thus the five isoforms apparently were formed through combinations of two subunits in different ratios. Labelling cotyledons in vivo with [35S]methionine at three daily intervals in the dark, and translation in vivo of polyadenylated RNA isolated from cotyledons at the same ages, revealed synthesis of two different subunits. One of the subunits was synthesized in cotyledons at all ages studied (days 1-3), whereas the other subunit was detected only at days 2 and 3. This differential expression of two catalase subunits helped explain previous results from this laboratory showing that the two anodic forms (A and B) found in maturing seeds were supplemented with three cathodic forms (C-E) after the seeds germinated. These subunit data also helped clarify our new findings that proteins of isoforms A, B and C (most active isoforms) accumulated in cotyledons of plants kept in the dark for 3 days, then gradually disappeared during the next several days, whereas isoforms D and E (least active isoforms) remained in the cells. This shift in isoform pattern occurred whether seedlings were kept in the dark or exposed to continuous light after day 3, although exposure to light enhanced this process. These sequential molecular events were responsible for the characteristic developmental changes (rise and fall) in total catalase activity. We believe that the isoform changeover is physiologically related to the changeover in glyoxysome to leaf-type-peroxisome metabolism. Images Fig. 1. Fig. 2. Fig. 3. Fig. 4. Fig. 5.

Ni, W; Trelease, R N; Eising, R

1990-01-01

367

Effects of metal ions on simultaneous production of glucose oxidase and catalase by Aspergillus niger.  

PubMed

The effects of various metal ions on the simultaneous production of glucose oxidase and catalase by Aspergillus niger were investigated. Calcium carbonate induced synthesis of both enzymes. The induction of calcium carbonate was accompanied by a metabolic shift from the glycolytic pathway (EMP, Embden-Meyerhof-Parnas) to direct oxidation of glucose by glucose oxidase. The time course of the biosynthesis of both enzymes is reported. The logistic model was in good agreement with the experimental growth results. The production of both enzymes was growth-associated. Finally, a model of growth and product formation was also proposed. PMID:11169035

Liu, J Z; Huang, Y Y; Liu, J; Weng, L P; Ji, L N

2001-01-01

368

A catalase from the freshwater mussel Cristaria plicata with cloning, identification and protein characterization.  

PubMed

Catalase is an important antioxidant protein which can protect organisms against various oxidative stresses by eliminating hydrogen peroxide. The catalase cDNA of Cristaria plicata (cpCAT) was cloned from the haemocytes using degenerate primers by the method of 3' and 5' rapid amplification of cDNA ends PCR. The gene is 4863 bp long and has a total of two introns and three exons. The precise size and location of the introns and exons have been determined. In addition the full-length cDNA of cpCAT contained 2618 bp, The cDNA contained a 5' untranslated region (UTR) of 136 nucleotides, the 3' UTR of 979 bp with a canonical polyadenylation signal sequence AATAAA and a polyA tail, and an open reading frame (ORF) of 1503 bp, encoding 501 amino acid residues with 56.86 kDa predicted molecular weight. The theoretical isoelectric point was 6.77. BLAST analysis showed that the deduced amino acid sequence of cpCAT had significant homology to catalases from animals, plants and bacteria. The deduced amino acid sequence of cpCAT had characteristic features of catalase family such as catalytic site motif (61FNRERIPERVVHAKGAG77), heme-ligand signature motif (351RLYSYSDTH359), two glycosylation sites (N145, N436), NADPH binding site and the three catalytic amino acid residues (His72, Asn145 and Tyr355). It had no signal peptide. The phylogenetic tree indicated that cpCAT gene was very close to the gene of scallops, Chlamys farreri. The enzymatic activity of purified recombinant cpCAT was 11194.4 ± 40.4 U/mg, it might resist against H(2)O(2). The recombinant enzyme held higher thermal stability, the optimum temperature was 25 °C, it retained more than 82% activity between 25 and 60 °C. The stability of the recombinant enzyme were higher between pH 5 and 10, and the optimal pH value was 7.0. When cpCAT was treated with 2-4 moL/L urea and 1%-3% SDS, the activity was also stable, it kept more than 80% activity. PMID:21689759

Yang, Xilan; Li, Gang; Wen, Chungen; Hu, Baoqing; Deng, Lirong; Pei, Pengzu; Xie, Yanhai

2011-06-12

369

A sulfonamide based glucose-responsive hydrogel with covalently immobilized glucose oxidase and catalase  

Microsoft Academic Search

A new glucose-sensitive hydrogel, based on sulfonamide chemistry with covalently conjugated glucose oxidase and catalase, was synthesized and tested. The pH-induced full swelling transition of the gel occurred in the range of pH 6.5?7.5. In a glucose concentration range of 0–300 mg\\/dl in an isotonic phosphate buffered saline solution (pH 7.4), the pH inside the gel varied from pH 7.4

Seong Il Kang; You Han Bae

2003-01-01

370

Dynamics of the reaction glucose-catalase-glucose oxidase-hydrogen peroxide  

NASA Astrophysics Data System (ADS)

Glucose-catalase-glucose oxidase-hydrogen peroxide reaction is one of the few known enzymatic systems studied in vitro in the field of nonlinear chemical dynamics. This reaction belongs to the family of oscillatory enzymatic reactions, which form a natural basis of oscillations in biological systems. A parametric study of dependence on mixing, temperature and initial concentrations of components in a batch stirred reactor was carried out. A newly proposed mathematical model of the reaction conforms to the obtained experimental data. Results of our experiments and simulations hint at further directions of research of non-linear dynamics in this reaction.

?íp, M.; Schreiberová, L.; Schreiber, I.

2011-12-01

371

X-ray diffraction study of Penicillium Vitale catalase in the complex with aminotriazole  

SciTech Connect

The three-dimensional structure of the enzyme catalase from Penicillium vitale in a complex with the inhibitor aminotriazole was solved and refined by protein X-ray crystallography methods. An analysis of the three-dimensional structure of the complex showed that the inhibition of the enzyme occurs as a result of the covalent binding of aminotriazole to the amino-acid residue His64 in the active site of the enzyme. An investigation of the three-dimensional structure of the complex resulted in the amino-acid residues being more precisely identified. The binding sites of saccharide residues and calcium ions in the protein molecule were found.

Borovik, A. A.; Grebenko, A. I.; Melik-Adamyan, V. R., E-mail: mawr@ns.crys.ras.ru [Russian Academy of Sciences, Shubnikov Institute of Crystallography (Russian Federation)

2011-07-15

372

X-ray diffraction study of Penicillium Vitale catalase in the complex with aminotriazole  

NASA Astrophysics Data System (ADS)

The three-dimensional structure of the enzyme catalase from Penicillium vitale in a complex with the inhibitor aminotriazole was solved and refined by protein X-ray crystallography methods. An analysis of the three-dimensional structure of the complex showed that the inhibition of the enzyme occurs as a result of the covalent binding of aminotriazole to the amino-acid residue His64 in the active site of the enzyme. An investigation of the three-dimensional structure of the complex resulted in the amino-acid residues being more precisely identified. The binding sites of saccharide residues and calcium ions in the protein molecule were found.

Borovik, A. A.; Grebenko, A. I.; Melik-Adamyan, V. R.

2011-07-01

373

Upregulation of adenosine kinase in rasmussen encephalitis.  

PubMed

Rasmussen encephalitis (RE) is a rare neurologic disorder of childhood characterized by unihemispheric inflammation, progressive neurologic deficits, and intractable focal epilepsy. The pathogenesis of RE is still enigmatic. Adenosine is a key endogenous signaling molecule with anticonvulsive and anti-inflammatory effects, and our previous work demonstrated that dysfunction of the adenosine kinase (ADK)-adenosine system and astrogliosis are the hallmarks of epilepsy. We hypothesized that the epileptogenic mechanisms underlying RE are related to changes in ADK expression and that those changes might be associated with the development of epilepsy in RE patients. Immunohistochemistry was used to examine the expression of ADK and glial fibrillary acidic protein in surgically resected human epileptic cortical specimens from RE patients (n = 12) and compared with control cortical tissues (n = 6). Adenosine kinase expression using Western blot and enzymatic activity for ADK were assessed in RE versus control samples. Focal astrogliosis and marked expression of ADK were observed in the lesions of RE. Significantly greater ADK expression in RE versus controls was demonstrated by Western blot, and greater enzymatic activity for ADK was demonstrated using an enzyme-coupled bioluminescent assay. These results suggest that upregulation of ADK is a common pathologic hallmark of RE and that ADK might be a target in the treatment of epilepsy associated with RE. PMID:24128682

Luan, Guoming; Gao, Qing; Guan, Yuguang; Zhai, Feng; Zhou, Jian; Liu, Changqing; Chen, Yin; Yao, Kun; Qi, Xueling; Li, Tianfu

2013-11-01

374

Distribution of a Nocardia brasiliensis Catalase Gene Fragment in Members of the Genera Nocardia, Gordona, and Rhodococcus  

PubMed Central

An immunodominant protein from Nocardia brasiliensis, P61, was subjected to amino-terminal and internal sequence analysis. Three sequences of 22, 17, and 38 residues, respectively, were obtained and compared with the protein database from GenBank by using the BLAST system. The sequences showed homology to some eukaryotic catalases and to a bromoperoxidase-catalase from Streptomyces violaceus. Its identity as a catalase was confirmed by analysis of its enzymatic activity on H2O2 and by a double-staining method on a nondenaturing polyacrylamide gel with 3,3?-diaminobenzidine and ferricyanide; the result showed only catalase activity, but no peroxidase. By using one of the internal amino acid sequences and a consensus catalase motif (VGNNTP), we were able to design a PCR assay that generated a 500-bp PCR product. The amplicon was analyzed, and the nucleotide sequence was compared to the GenBank database with the observation of high homology to other bacterial and eukaryotic catalases. A PCR assay based on this target sequence was performed with primers NB10 and NB11 to confirm the presence of the NB10-NB11 gene fragment in several N. brasiliensis strains isolated from mycetoma. The same assay was used to determine whether there were homologous sequences in several type strains from the genera Nocardia, Rhodococcus, Gordona, and Streptomyces. All of the N. brasiliensis strains presented a positive result but only some of the actinomycetes species tested were positive in the PCR assay. In order to confirm these findings, genomic DNA was subjected to Southern blot analysis. A 1.7-kbp band was observed in the N. brasiliensis strains, and bands of different molecular weight were observed in cross-reacting actinomycetes. Sequence analysis of the amplicons of selected actinomycetes showed high homology in this catalase fragment, thus demonstrating that this protein is highly conserved in this group of bacteria.

Vera-Cabrera, Lucio; Johnson, Wendy M.; Welsh, Oliverio; Resendiz-Uresti, Francisco L.; Salinas-Carmona, Mario C.

1999-01-01

375

Uncaria tomentosa extracts protect human erythrocyte catalase against damage induced by 2,4-D-Na and its metabolites.  

PubMed

The effect of ethanolic and aqueous extracts from leaves and bark of Uncaria tomentosa was studied, with particular attention to catalase activity (CAT - EC. 1.11.1.6). We observed that all tested extracts, at a concentration of 250 ?g/mL were not toxic to erythrocyte catalase because they did not decreased its activity. Additionally, we investigated the protective effect of extracts on changes in CAT activity in the erythrocytes incubated with sodium salt of 2,4-dichlorophenoxyacetic acid (2,4-D-Na) and its metabolites i.e., 2,4-dichlorophenol (2,4-DCP) and catechol. Previous investigations showed that these chemicals decreased activity of erythrocyte catalase (Bukowska et al., 2000; Bukowska and Kowalska, 2004). The erythrocytes were divided into two portions. The first portion was incubated for 1 and 5h at 37°C with 2,4-D-Na, 2,4-DCP and catechol, and second portion was preincubated with extracts for 10 min and then incubated with xenobiotics for 1 and 5h. CAT activity was measured in the first and second portion of the erythrocytes. We found a protective effect of the extracts from U. tomentosa on the activity of catalase incubated with xenobiotics studied. Probably, phenolic compounds contained in U. tomentosa scavenged free radicals, and therefore protected active center (containing -SH groups) of catalase. PMID:22426356

Bukowska, Bo?ena; Bors, Milena; Gulewicz, Krzysztof; Koter-Michalak, Maria

2012-03-09

376

Evidence for separate substrate binding sites for hydrogen peroxide and cumene hydroperoxide (CHP) in the oxidation of ethanol by catalase  

SciTech Connect

The oxidation of ethanol by purified bovine liver catalase (Sigma, C-40) can be supported by H/sub 2/O/sub 2/ or by CHP. The time course of the H/sub 2/O/sub 2/ supported reaction (using glucose/glucose oxidase as the H/sub 2/O/sub 2/ source) was linear for at least one hr, whereas the rate of acetaldehyde formation in the CHP (4.2 mM) supported reaction decreased with time. When catalase was exposed o CHP for 5 min before the addition of ethanol, the rate of CHP supported ethanol oxidation was reduced by more than 90% compared to incubations where the addition of ethanol preceded that of CHP. In the CHP inhibited state, the peroxidative activity of catalase was not restored by further addition of CHP or ethanol; however, addition of fresh catalase yielded its expected activity. Significantly, the CHP inhibited enzyme was equally effective as the untreated enzyme in catalyzing (a) the oxidation of ethanol in the presence H/sub 2/O/sub 2/ supported peroxidative activity as well as catalytic activity by CHP inhibited catalase points to separate binding sites for H/sub 2/O/sub 2/ and CHP in this reaction. Alternatively, CHP may bind adjacent to a common peroxide active site, thereby sterically impeding the binding of CHP - but not of H/sub 2/O/sub 2/ - to this active site.

DeMaster, E.G.; Nagasawa,ss H.T.

1986-03-01

377

Down-regulation of catalase activity allows transient accumulation of a hydrogen peroxide signal in Chlamydomonas reinhardtii.  

PubMed

In photosynthetic organisms, excess light is a stress that induces production of reactive oxygen species inside the chloroplasts. As a response, the capacity of antioxidative defence mechanisms increases. However, when cells of Chlamydomonas reinhardtii were shifted from dark to high light, a reversible partial inactivation of catalase activity was observed, which correlated with a transient increase in the level of H2 O2 in the 10??m range. This concentration range seems to be necessary to activate H2 O2 -dependent signalling pathways stimulating the expression of H2 O2 responsive genes, such as the heat shock protein HSP22C. Catalase knock-down mutants had lost the transient accumulation of H2 O2 , suggesting that a decrease in catalase activity was the key element for establishing a transient H2 O2 burst. Catalase was inactivated by a one-electron event consistent with the reduction of a single cysteine. We propose that under high light intensity, the redox state of the photosynthetic electron transport chain is sensed and transmitted to the cytosol to regulate the catalase activity. This allows a transient accumulation of H2 O2 , inducing a signalling event that is transmitted to the nucleus to modulate the expression of chloroplast-directed protection enzymes. PMID:23237476

Michelet, Laure; Roach, Thomas; Fischer, Beat B; Bedhomme, Mariette; Lemaire, Stéphane D; Krieger-Liszkay, Anja

2013-01-13

378

Flow injection catalase activity measurement based on gold nanoparticles/carbon nanotubes modified glassy carbon electrode.  

PubMed

Amperometric flow injection method of hydrogen peroxide analysis was developed based on catalase enzyme (CAT) immobilization on a glassy carbon electrode (GC) modified with electrochemically deposited gold nanoparticles on a multiwalled carbon nanotubes/chitosan film. The resulting biosensor was applied to detect hydrogen peroxide with a linear response range 1.0×10(-7)-2.5×10(-3)M with a correlation coefficient 0.998 and response time less than 10s. The optimum conditions of film deposition such as potential applied, deposition time and pH were tested and the flow injection conditions were optimized to be: flow rate of 3ml/min, sample volume 75?l and saline phosphate buffer of pH 6.89. Catalase enzyme activity was successfully determined in liver homogenate samples of rats, raised under controlled dietary plan, using a flow injection analysis system involving the developed biosensor simultaneously with spectrophotometric detection, which is the common method of enzymatic assay. PMID:22817944

El Nashar, Rasha Mohamed

2011-12-09

379

Superoxide dismutase, catalase, and. alpha. -tocopherol content of stored potato tubers. [Solanum tuberosum L  

SciTech Connect

Activated oxygen or oxygen free radical mediated damage to plants has been established or implicated in many plant stress situations. The extent of activated oxygen damage to potato (Solanum tuberosum L.) tubers during low temperature storage and long-term storage is not known. Quantitation of oxygen free radical mediated damage in plant tissues is difficult. However, it is comparatively easy to quantitate endogenous antioxidants, which detoxify potentially damaging forms of activated oxygen. Three tuber antioxidants, superoxide dismutase, catalase, and {alpha}-tocopherol were assayed from four potato cultivars stored at 3{degree}C and 9{degree}C for 40 weeks. Tubers stored at 3{degree}C demonstrated increased superoxide dismutase activities (up to 72%) compared to tubers stored at 9{degree}C. Time dependent increases in the levels of superoxide dismutase, catalase, and {alpha}-tocopherol occurred during the course of the 40 week storage. The possible relationship between these increases in antioxidants and the rate of activated oxygen production in the tubers is discussed.

Spychalla, J.P.; Desborough, S.L. (Univ. of Minnesota, St. Paul (USA))

1990-11-01

380

Cell-mediated Transfer of Catalase Nanoparticles from Macrophages to Brain Endothelial and Neural Cells  

PubMed Central

Background Our laboratories forged the concept of macrophage delivery of protein antioxidants to attenuate neuroinflammation and nigrostriatal degeneration in Parkinson’s disease (PD). Notably, the delivery of the redox enzyme, catalase, incorporated into a polyion complex micelle (“nanozyme”) by bone marrow-derived macrophages protected the nigrostriatal against 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) intoxication. Nonetheless, how macrophage delivery of nanozyme increases the efficacy of catalase remains unknown. Methods Herein, we examined the transfer of nanozyme from macrophages to brain microvessel endothelial cells, neurons and astrocytes. Results Facilitated transport of the nanozyme from macrophages to endothelial and neural target cells occurred through endocytosis-independent mechanisms that involved fusion of cellular membranes; macrophage bridging conduits; and nanozyme lipid coatings. Nanozyme transfer was operative across an artificial blood brain barrier and showed efficient reactive oxygen species decomposition. Conclusion This is the first demonstration that drug-loaded macrophages discharge particles to contiguous target cells for potential therapeutic brain enzyme delivery. The pathways for drug delivery shown may be used for the treatment of degenerative disorders of the nervous system.

Haney, Matthew J.; Zhao, Yuling; Li, Shu; Higginbotham, Sheila M.; Booth, Stephanie L.; Han, Huai-Yun; Vetro, Joseph A.; Mosley, R. Lee; Kabanov, Alexander V.; Gendelman, Howard E.; Batrakova, Elena V.

2011-01-01

381

Catalase Activity as a Biomarker for Mild-Stress-Induced Robustness in Bacillus weihenstephanensis  

PubMed Central

Microorganisms are able to survive and grow in changing environments by activating stress adaptation mechanisms which may enhance bacterial robustness. Stress-induced enhanced robustness complicates the predictability of microbial inactivation. Using psychrotolerant Bacillus weihenstephanensis strain KBAB4 as a model, we investigated the impact of the culturing temperature on mild-oxidative-stress-induced (cross-)protection toward multiple stresses, including severe oxidative, heat, and acid stresses. Culturing at a refrigeration temperature (7°C) compared to the optimal growth temperature (30°C) affected both the robustness level of B. weihenstephanensis and the oxidative stress adaptive response. Scavengers of reactive oxygen species have a crucial role in adaptation to oxidative stresses, and this points to a possible predictive role in mild-oxidative-stress-induced robustness. Therefore, the catalase activity was determined upon mild oxidative stress treatment and was demonstrated to be significantly correlated with the robustness level of mild-stress-treated cells toward severe oxidative and heat stresses but not toward severe acid stress for cells grown at both refrigeration and optimal temperatures. The quantified correlations supported the predictive quality of catalase activity as a biomarker and also underlined that the predictive quality is stress specific. Biomarkers that are able to predict stress-induced enhanced robustness can be used to better understand stress adaptation mechanisms and might allow the design of effective combinations of hurdles to control microbial behavior.

Effraimidou, Styliani; Abee, Tjakko

2013-01-01

382

Evaluation of the catalase promoter for expressing the alkaline xylanase gene (alx) in Aspergillus niger.  

PubMed

Aspergillus niger represents a promising host for the expression of recombinant proteins, but only a few expression systems are available for this organism. In this study, the inducible catalase promoter (PcatR) from A. niger was characterized. For this, constructs were developed and checked for the expression of the alkaline xylanase gene transcriptionally fused under the cat R promoter. Two versions of the catalase (catR) promoter sequence from A. niger (P(cat300,) P(cat924)) were isolated and tested for their ability to drive expression of the alkaline xylanase (alx) gene. P(cat924) showed better efficiency (more than 10-fold increase in AlX activity compared to P(cat300)) under the optimized culture conditions. Induction of the catR promoter with 0.20% H(2)O(2) and 1.5% CaCO(3) in the culture medium, further increased expression of AlX 2.61- and 2.20-fold, respectively, clarifying its inducible nature. Specific induction or repression of the catR promoter provides the possibility for utilization of this promoter in heterologous protein production. PMID:22092890

Sharma, Ruchika; Katoch, Meenu; Govindappa, Nagraj; Srivastava, P S; Sastry, Kedarnath N; Qazi, Ghulam Nabi

2011-12-12

383

Catalase activity as a biomarker for mild-stress-induced robustness in Bacillus weihenstephanensis.  

PubMed

Microorganisms are able to survive and grow in changing environments by activating stress adaptation mechanisms which may enhance bacterial robustness. Stress-induced enhanced robustness complicates the predictability of microbial inactivation. Using psychrotolerant Bacillus weihenstephanensis strain KBAB4 as a model, we investigated the impact of the culturing temperature on mild-oxidative-stress-induced (cross-)protection toward multiple stresses, including severe oxidative, heat, and acid stresses. Culturing at a refrigeration temperature (7°C) compared to the optimal growth temperature (30°C) affected both the robustness level of B. weihenstephanensis and the oxidative stress adaptive response. Scavengers of reactive oxygen species have a crucial role in adaptation to oxidative stresses, and this points to a possible predictive role in mild-oxidative-stress-induced robustness. Therefore, the catalase activity was determined upon mild oxidative stress treatment and was demonstrated to be significantly correlated with the robustness level of mild-stress-treated cells toward severe oxidative and heat stresses but not toward severe acid stress for cells grown at both refrigeration and optimal temperatures. The quantified correlations supported the predictive quality of catalase activity as a biomarker and also underlined that the predictive quality is stress specific. Biomarkers that are able to predict stress-induced enhanced robustness can be used to better understand stress adaptation mechanisms and might allow the design of effective combinations of hurdles to control microbial behavior. PMID:23064331

den Besten, Heidy M W; Effraimidou, Styliani; Abee, Tjakko

2012-10-12

384

Hydrogen peroxide decomposition by a non-heme iron(III) catalase mimic: a DFT study.  

PubMed

Non-heme iron(III) complexes of 14-membered tetraaza macrocycles have previously been found to catalytically decompose hydrogen peroxide to water and molecular oxygen, like the native enzyme catalase. Here the mechanism of this reaction is theoretically investigated by DFT calculations at the (U)B3LYP/6-31G* level, with focus on the reactivity of the possible spin states of the FeIII complexes. The computations suggest that H2O2 decomposition follows a homolytic route with intermediate formation of an iron(IV) oxo radical cation species (L.+FeIV==O) that resembles Compound I of natural iron porphyrin systems. Along the whole catalytic cycle, no significant energetic differences were found for the reaction proceeding on the doublet (S=1/2) or on the quartet (S=3/2) hypersurface, with the single exception of the rate-determining O--O bond cleavage of the first associated hydrogen peroxide molecule, for which reaction via the doublet state is preferred. The sextet (S=5/2) state of the FeIII complexes appears to be unreactive in catalase-like reactions. PMID:17323385

Sicking, Willi; Korth, Hans-Gert; Jansen, Georg; de Groot, Herbert; Sustmann, Reiner

2007-01-01

385

Catalase plays a key role in salt stress acclimation induced by hydrogen peroxide pretreatment in maize.  

PubMed

Pretreatment in plants is recognized as a valuable strategy to stimulate plant defenses, leading to better plant development. This study evaluated the effects of H?O? leaf spraying pretreatment on plant growth and investigated the antioxidative mechanisms involved in the response of maize plants to salt stress. It was found that salinity reduced maize seedling growth when compared to control conditions, and H?O? foliar spraying was effective in minimizing this effect. Analysis of the antioxidative enzymes catalase (EC 1.11.1.6), guaiacol peroxidase (EC 1.11.1.7), ascorbate peroxidase (EC 1.11.1.1) and superoxide dismutase (EC 1.15.1.1) revealed that H?O? spraying increased antioxidant enzyme activities. Catalase (CAT) was the most responsive of these enzymes to H?O?, with higher activity early (48 h) in the treatment, while guaiacol peroxidase (GPX) and ascorbate peroxidase (APX) were responsive only at later stages (240 h) of treatment. Increased CAT activity appears linked to gene expression regulation. Lower malondialdehyde levels were detected in plants with higher CAT activity, which may result from the protective function of this enzyme. Overall, we can conclude that pretreatment with H?O? leaf spraying was able to reduce the deleterious effects of salinity on seedling growth and lipid peroxidation. These responses could be attributed to the ability of H?O? to induce antioxidant defenses, especially CAT activity. PMID:22609456

Gondim, Franklin Aragão; Gomes-Filho, Enéas; Costa, José Hélio; Mendes Alencar, Nara Lídia; Prisco, José Tarquinio

2012-04-25

386

Fluorometric enzymatic autoindicating biosensor for H2O2 determination based on modified catalase.  

PubMed

Our general aim is to develop reversible optical biosensors which can be used for continuous monitoring. In this paper we propose a biosensor for H(2)O(2) determination. The bioreceptor is catalase (Cat) previously linked to a Ruthenium O(2)-sensitive fluorophore (Cat-Ru). It is based on the reversible H(2)O(2) disproportionation into O(2) and H(2)O. First, the fluorescent-enzymatic system was optimized for batch measurements (linear response ranges from 1×10(-4) to, at least, 1×10(-3) M H(2)O(2)). Because of its reversibility, the same enzyme aliquot can be used for performing the whole calibration step (and the subsequent determination). Secondly, the optical sensor was prepared by Cat-Ru immobilization in a polyacrylamide film. The sensor permits H(2)O(2) determination in a similar concentration range as in batch mode and can be used during at least 1 month. A mathematical model has also been developed which permits the effect of the experimental parameters to predict. The model also explains the sensor behavior if different fluorophores are used, and shows that the analytical signal only slightly depends on the initial concentration of the O(2) in the sample. Finally an alternative sensor is presented based on a commercially available O(2) fluorescence sensor linked to catalase. This system gives an analytical behavior similar to that shown for the Cat-Ru sensor. PMID:22959015

Ortega, Estefania; de Marcos, Susana; Galbán, Javier

2012-08-23

387

Upregulation of neurodevelopmental genes during scarless healing.  

PubMed

Scarless fetal skin wound healing is a paradigm for ideal skin repair and is dependent on peripheral nerve function.To further explore neurogenic mechanisms influence on the scarless skin repair, fetal rats were wounded on gestational days 16 (E16; n = 24) and 18 (E18; n = 8) and wounds were harvested at 1 and 3 days after injury. Unwounded skin at identical gestational age was used for control comparison. The scarless E16 and scarring E18 wounds underwent macroarray gene expression analysis (1172 genes).During the scarless healing period, 53 (4.5%) genes had a statistically significant upregulation post-injury with at least a 2- to 3-fold change 1 day after wounding and 14 (1.2%) genes 3 days after wounding (P < 0.05). Many neurodevelopmental genes were increased during scarless repair on post-injury days 1 and 3. Neuropeptide Y Receptor type I, cJun related Transcription Factor (junD), Synaptophysin, SNAP 25, Neuronal calcium sensor 1 (NCS1), neural visine-like calcium binding protein 1 (NVP1), nerve growth factor-induced gene A (NGFI-A/EGR1), VGF8A protein, p27kip1, and members of the GABA and serotonin family each had 2- to 3-fold expression increases (P < 0.05).We speculate that fetal skin cells express neurotrophins during skin development that regulate peripheral neuron formation. During injury these factors promote the survival and regeneration of peripheral neurons; this interaction of neuropeptides, neuropeptide receptors, and neurotrophins may modulate the fetal scarless repair mechanisms in response to injury. Identification of these neurodevelopmental candidate genes provides insight for new investigation into mechanisms regulating scarless healing. PMID:20098115

Antony, Anuja K; Kong, Wuyi; Lorenz, H Peter

2010-02-01

388

Upregulation of Leukotriene Receptors in Gastric Cancer  

PubMed Central

Background Leukotrienes (LT) mediate allergic and inflammatory processes. Previously, we identified significant changes in the expression pattern of LT receptors in the gastric mucosa after eradication of Helicobacter pylori infection. The aim of the present study was to evaluate the expression of 5-lipoxygenase (5-LOX) and LT receptors in gastric cancer (GC). Methods The expression of 5-LOX and receptors for LTB4 (BLT-1, BLT-2) and cysteinyl-LT (CysLT-1, CysLT-2) were analyzed by immunohistochemistry (IHC) in GC samples of 35 consecutive patients who underwent gastrectomy and in 29 tumor-free tissue specimens from gastric mucosa. Results Male-to-female ratio was 24:11. The median age was 70 years (range 34–91). Twenty-two patients had GC of intestinal, six of diffuse, six of mixed and one of undifferentiated type. The IHC analysis showed a nearly ubiquitous expression of studied proteins in GC (88–97%) and in tumor-free specimens as well (89–100%). An increase in the immunoreactive score of both BLT receptors and CysLT-1 was observed in GC compared to tumor-free gastric mucosa (p < 0.001 for BLT-1; p < 0.01 for BLT-2 and CysLT-1, Mann-Whitney U-test). No differences in the IHC expression of 5-LOX and CsyLT-2 were observed between GC and tumor-free mucosa. The expression of BLT-2, CysLT-1 and CysLT-2 was increased in GC of intestinal type when compared to the diffuse type (p < 0.05; Mann-Whitney U-test). Conclusions LTB4 receptors and CysLT-1 are up-regulated in GC tissue implying a role in gastric carcinogenesis.

Venerito, Marino; Kuester, Doerthe; Harms, Caroline; Schubert, Daniel; Wex, Thomas; Malfertheiner, Peter

2011-01-01

389

Purification and characterization of a catalase from the nonsulfur phototrophic bacterium Rhodobacter sphaeroides ATH 2.4.1 and its role in the oxidative stress response  

Microsoft Academic Search

When challenged with reactive oxidants, the nonsulfur phototrophic bacterium Rhodobacter sphaeroides ATH 2.4.1 exhibited an oxidative stress response during both phototrophic and chemotrophic growth. Upon preincubation with\\u000a 100 ?M H2O2, catalase activity increased fivefold. Catalase was also induced by other forms of oxidative stress, heat-shock, ethanol\\u000a treatment, and stationary-phase conditions. Only one band of catalase activity was detected after native

Detlef P. Terzenbach; Michael Blaut

1998-01-01

390

Catalase induces the expression of inducible nitric oxide synthase through activation of NF-?B and PI3K signaling pathway in Raw 264.7 cells  

Microsoft Academic Search

It has been reported that macrophages produce substantial amounts of nitrite and nitrate after addition of catalase, but the mechanism associated remains unclear. In present study, we investigated whether catalase modulates the expression of inducible nitric oxide synthase (iNOS), an enzyme that produces nitric oxide. Exposure of Raw 264.7 macrophages (Raw cells) to catalase induced high expression of iNOS mRNA

Byeong-Churl Jang; Ji-Hye Paik; Sang-Pyo Kim; Jae-Hoon Bae; Kyo-Chul Mun; Dae-Kyu Song; Chi-Heum Cho; Dong-Hoon Shin; Taeg Kyu Kwon; Jong-Wook Park; Jong-Gu Park; Won-Ki Baek; Min-Ho Suh; Soo Hwan Lee; Suk-Hwan Baek; In-Seon Lee; Seong-Il Suh

2004-01-01

391

Expression analysis and characterization of the mutant of a growth-phase- and starvation-regulated monofunctional catalase gene from Xanthomonas campestris pv. phaseoli  

Microsoft Academic Search

Analysis of the Xanthomonas campestris pv. phaseoli (Xp) catalase profile using an activity gel revealed at least two distinct monofunctional catalase isozymes denoted Kat1 and Kat2. Kat1 was expressed throughout growth, whereas Kat2 was expressed only during the stationary phase of growth. The nucleotide sequence of a previously isolated monofunctional catalase gene, Xp katE, was determined. The deduced amino acid

Paiboon Vattanaviboon; Skorn Mongkolsuk

2000-01-01

392

AN AMPEROMETRIC BIOSENSOR FOR HYDROGEN PEROXIDASE BASED ON THE CO-IMMOBILIZATION OF CATALASE AND METHYLENE BLUE IN AN AL2O3 SOL-GEL MODIFIED ELECTRODE  

Microsoft Academic Search

A novel biosensor for the amperometric detection of hydrogen peroxide was developed based on the co-immobilization of catalase and methylene blue on an Al2O3 sol-gel fabricated glassy carbon electrode. The membrane structure of the sol-gel-immobilized catalase and methylene blue was studied with scanning electron microscopy. Cyclic voltammetric and amperometric measurements demonstrated that methylene blue co-immobilized with catalase in this way

Dandan Chen; Baohong Liu; Zhengjiu Liu; Jilie Kong

2001-01-01

393

Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase  

SciTech Connect

The usual method of staining polyacrylamide gel electropherograms for superoxide dismutase activity utilizes a photochemical flux of O/sub 2//sup -/ to reduce nitroblue tetrazolium. Superoxide dismutases intercept O/sub 2//sup -/, preventing formazan production and thus causing achromatic bands. In the presence of H/sub 2/O/sub 2/, catalase also yield achromatic bands during this staining procedure. This is due to local elevation of pO/sub 2/ by the catalytic decomposition of H/sub 2/O/sub 2/. O/sub 2/, in turn, inhibits the reduction of the tetrazolium by O/sub 2//sup -/. This phenomenon provides a new activity stain for catalase. A previously described activity stain for catalase has also been reexamined and significantly improved.

Clare, D.A.; Duong, M.N.; Darr, D.; Archibald, F.; Fridovich, I.

1984-08-01

394

Improved membrane filtration method incorporating catalase and sodium pyruvate for detection of chlorine-stressed coliform bacteria.  

PubMed Central

In vitro pure culture studies were conducted on three different strains of Escherichia coli (K-12, EPA 00244, and SWEI) to determine the effect of chlorination on catalase activity. In each case, stationary-phase cells exhibited significant (P less than 0.001) reductions in enzyme activity following exposure to chlorine. Mean differences in activity between control and chlorine-stressed cells ranged from 8.8 to 20.3 U/mg of protein for E. coli SWEI and EPA 00244, respectively. Following initial enzyme studies, resuscitation experiments utilizing the membrane filtration technique were conducted on chlorinated sewage effluent. Five different amendments, including catalase (1,000 U per plate), heat-inactivated catalase (1,000-U per plate), sodium pyruvate (0.05%), a catalase-sodium pyruvate combination (1,500 U/0.01%), and acetic acid (0.05%), were tested for the ability to enhance detection of chlorine-stressed cells on M-fecal coliform (M-FC), mT7, M-Endo, and tryptone-glucose-yeast extract (TGY) media. Significant (P less than 0.001) increases in recovery of fecal coliforms on M-FC, total coliforms on mT7 and M-Endo, and total heterotrophs on TGY were obtained on plates containing catalase, pyruvate, or the combination of these compounds. Supplementation with heat-inactivated catalase and acetic acid did not improve recovery of chlorine-stressed cells compared with recovery on nonamended media. Subsequent analysis of colonies from plates containing compounds which enhanced recovery indicated coliform verification percentages of greater than 80% on M-FC, greater than 90% on mT7, and greater than 94% on M-Endo media. These data suggest that the addition of peroxide-degrading compounds to various standard recovery media may improve detection of both coliform and heterotrophic bacteria in chlorinated waters.

Calabrese, J P; Bissonnette, G K

1990-01-01

395

Assessment of DNA damage and plasma catalase activity in healthy term hyperbilirubinemic infants receiving phototherapy.  

PubMed

Phototherapy (PT) is the most widely used form of treatment for unconjugated hyperbilirubinemia. One possible harmful consequence of PT is of a genetic nature. High levels of bilirubin may lead to oxidative damage in newborns: photochemical reactions may produce toxic photoproducts, probably peroxides. In order to investigate this hypothesis further under in vivo conditions, DNA strand-break frequency was examined by means of the comet assay in peripheral lymphocytes of icteric newborns undergoing PT treatment, and the levels of catalase, an antioxidant enzyme, were determined. We analyzed 20 term non-hemolitic hyperbilirubinemic jaundiced neonates before PT ('before PT' group) and just prior to ending PT ('after PT' group) and compared comet scores of these patients with those of 20 healthy term neonates who all had bilirubin levels in the physiological range. Comet scores (tail length, tail moment and %DNA in tail) of the group 'before phototherapy' were 23.5 +/- 16.3, 7.41 (0.97-40.7), 33.0 +/- 12.1, respectively and scores of after phototherapy group were 3.2 +/- 1.8, 0.29 (0.3-3.2), 10.7 +/- 3.7, respectively. Comet scores of the control group were 3.0 +/- 2.9, 0.25 (0.03-3.22), 10.9 +/- 4.5, respectively. Comet scores and plasma catalase activities in hyperbilirubinemic newborns were significantly higher before phototherapy, compared with the values after phototherapy and in the control groups (p < 0.001). There was no statistical difference between the 'after phototherapy' group and the controls (p > 0.05). These results indicate that high serum bilirubin level has genotoxic effects as is evident from the high rate of DNA strand-breaks in jaundiced newborns. Also PT does not cause an increase in DNA oxidation or induce the genotoxic effects of bilirubin. The counteracting effect of higher catalase activities in hyperbilirubinemic newborns may be responsible for the inactivating toxic and DNA-damaging effects of PT. PMID:19712750

Karakukcu, Cigdem; Ustdal, Muzaffer; Ozturk, Adnan; Baskol, Gulden; Saraymen, Recep

2009-08-25

396

Catalase-like and peroxidase-like catalytic activities of silicon nanowire arrays.  

PubMed

Silicon nanowire arrays (SiNWAs) were found to have catalytic activities similar to those of biological enzymes catalase and peroxidase. Thus not only can these materials catalyze the decomposition reaction of H(2)O(2) into water and oxygen, but they can also catalyze the oxidation of o-phenylenediamine (OPD), a common substrate for peroxidases, by H(2)O(2). The presence of Si-H bonds and the morphology of the SiNWAs are found to be crucial to the occurrence of such catalytic activity. When the SiNWAs are reacted with H(2)O(2), the data from Raman spectroscopy suggests the formation of (Si-H)(2)···(O species) ((Si-H)(2)···Os), which is presumably responsible for the catalytic activity. These findings suggest the potential use of SiNWAs as enzyme mimics in medicine, biotechnology, and environmental chemistry. PMID:23245188

Wang, Hongwei; Jiang, Wenwen; Wang, Yanwei; Liu, Xiaoli; Yao, Jianlin; Yuan, Lin; Wu, Zhaoqiang; Li, Dan; Song, Bo; Chen, Hong

2012-12-19

397

Lack of effect of deferoxamine, dimethyl sulfoxide, and catalase on monocrotaline pyrrole pulmonary injury  

SciTech Connect

Monocrotaline pyrrole (MCTP) is a reactive metabolite of the pyrrolizidine alkaloid monocrotaline. MCTP given intravenously to rats causes pulmonary hypertension and right ventricular hypertrophy. Lesions in lungs after MCTP treatment contain macrophages and neutrophils, which may contribute to the damage by generation of reactive oxygen metabolites. Rats were treated with MCTP and agents known to protect against oxygen radical-mediated damage in acute models of neutrophil-dependent lung injury. Rats received MCTP and deferoxamine mesylate (DF), dimethyl sulfoxide (DMSO), or polyethylene glycol-coupled catalase (PEG-CAT). MCTP/vehicle-treated controls developed lung injury manifested as increased lung weight, release of lactate dehydrogenase into the airway, and sequestration of SVI-labeled bovine serum albumin in the lungs. Cotreatment of rats with DF, DMSO, or PEG-CAT did not protect against the injury due to MCTP. These results suggest that toxic oxygen metabolites do not play an important role in the pathogenesis of MCTP-induced pulmonary injury.

Bruner, L.H.; Johnson, K.; Carpenter, L.J.; Roth, R.A.

1987-01-01

398

Differential characteristics of catalase-positive campylobacters correlated with DNA homology groups.  

PubMed

Eighty-four strains of catalase-positive campylobacters could be placed into seven distinct DNA homology groups (species), corresponding to Campylobacter fetus, "C. hyointestinalis," C. jejuni, C. coli, "C. laridis," "C. fecalis," and aerotolerant campylobacters. The biochemical and physiological characteristics of the strains were examined for their correlation with the homology groups. The characterization tests that provided the most reliable differentiation at the species and subspecies level were growth at 25 and 42 degrees C, sensitivity to cephalothin and nalidixic acid, growth in semisolid media containing 1% glycine and 3.5% NaCl, growth on plates containing 1.5% NaCl, growth in a semisolid minimal medium, anaerobic growth in the presence of 0.1% trimethylamine-N-oxide, hydrogen sulfide production in SIM medium and triple-sugar iron agar, hippurate hydrolysis, nitrite reduction, and growth on plates under an air atmosphere. PMID:6478314

Roop, R M; Smibert, R M; Johnson, J L; Krieg, N R

1984-07-01

399

Catalase HPI influences membrane permeability in Escherichia coli following near-UV stress  

SciTech Connect

The katG gene in Escherichia coli encodes catalase HPI, which is involved in membrane transport and protects the cell during oxidative stress. Hydrogen peroxide (H2O2) induces synthesis of HPI. We examined the role of HPI in membrane permeability (proline uptake) following exposure to near-ultraviolet radiation (NUV). We found that NUV resulted in the same type of induction as H2O2. KatG::Tn10 cells experienced a large drop in uptake after NUV exposure, and levels remained low following incubation. A strain carrying a katG+ plasmid, however, showed considerably less decrease in uptake after NUV, and uptake quickly resumed upon incubation. Further, in an srd mutant which lacks 4-thiouracil, NUV resulted in only a small drop in proline uptake, which was immediately resumed.

Leven, S.; Heimberger, A.; Eisenstark, A. (Univ. of Missouri, Columbia (USA))

1990-09-28

400

Catalase and superoxide dismutase activities after heat injury of listeria monocytogenes  

SciTech Connect

Four strains of Listeria monocytogenes were examined for catalase (CA) and superoxide dismutase (SOD) activities. The two strains having the highest CA activities (LCDC and Scott A) also possessed the highest SOD activities. The CA activity of heated cell extracts of all four strains examined decreased sharply between 55 and 60/sup 0/C. SOD was more heat labile than CA. Two L. monocytogenes strains demonstrated a decline in SOD activity after heat treatment at 45/sup 0/C, whereas the other two strains demonstrated a decline at 50/sup 0/C. Sublethal heating of the cells at 55/sup 0/C resulted in increased sensitivity to 5.5% NaCl. Exogenous hydrogen peroxide was added to suspensions of L. monocytogenes; strains producing the highest CA levels showed the greatest H/sub 2/O/sub 2/ resistance.

Dallmier, A.W.; Martin, S.E.

1988-02-01

401

Partial characterization and expression of leaf catalase in the CAM-inducible halophyte Mesembryanthemum crystallinum L.  

PubMed

Catalase (CAT; EC 1.11.1.6) isolated from leaves of the halophytic plant Mesembryanthemum crystallinum is characterized by a high apparent molecular mass of about 320kDa, and high resistance to denaturing agents (10% ME). SDS-treatment breaks active oligomeric CAT into the less active and putatively dimeric form of 160kDa apparent molecular mass. Three subunits are resolved after denaturing PAGE: 79, 74 and 62kDa. Higher molecular masses of subunits coincide with increased activity of CAT. M. crystallinum leaf CAT reveals a diel variation in the resistance to denaturing factors and the stability of CAT is increased in a light-dependent manner both in C(3)- and in CAM-induced plants. Unchanged level of leaf CAT transcripts is documented in the diurnal cycle of C(3) plants and after salinity-induced crassulacean acid metabolism (CAM). PMID:18203610

Niewiadomska, Ewa; Miszalski, Zbigniew

2007-10-06

402

A sulfonamide based glucose-responsive hydrogel with covalently immobilized glucose oxidase and catalase.  

PubMed

A new glucose-sensitive hydrogel, based on sulfonamide chemistry with covalently conjugated glucose oxidase and catalase, was synthesized and tested. The pH-induced full swelling transition of the gel occurred in the range of pH 6.5 approximately 7.5. In a glucose concentration range of 0-300 mg/dl in an isotonic phosphate buffered saline solution (pH 7.4), the pH inside the gel varied from pH 7.4 to 7.2. At the same glucose concentration range, the gel showed reversible glucose dependent swelling without hysteresis from 12 to 8, expressed in water (g)/polymer (g). PMID:12490377

Kang, Seong Il; Bae, You Han

2003-01-01

403

Early Upregulation of Endothelial Adhesion Molecules in Obese Hypertensive Men  

Microsoft Academic Search

Abstract—Upregulation of endothelial adhesion molecules is the earliest step of atherogenesis. Whether obesity induces endothelial adhesin upregulation is unknown. To address this topic, circulating vascular cell adhesion molecule-1 (VCAM-1), intercellular adhesion molecule-1 (ICAM-1), E-selectin, and von Willebrand factor (vWF) concentrations were evaluated in 22 obese hypertensive (51.464.6 years [mean6SD age]), 19 obese normotensive (50.663.8 years), 18 nonobese hypertensive (52.363.9 years),

Claudio Ferri; Giovambattista Desideri; Marco Valenti; Cesare Bellini; Mehtap Pasin; Anna Santucci; Giancarlo De Mattia

2010-01-01

404

Gene Up-Regulation in Heart during Mammalian Hibernation  

Microsoft Academic Search

A cDNA library prepared from heart of hibernating golden-mantled ground squirrels, Spermophilus lateralis, was differentially screened to clone genes that were up-regulated during hibernation. Two differentially expressed clones were found after three rounds of screening and were confirmed as up-regulated by Northern blotting. Clone Ang6 encoded a polypeptide with 116 amino acids that was identified as the ventricular isoform of

Andreas Fahlman; Janet M Storey; Kenneth B Storey

2000-01-01

405

Catalase ameliorates polychlorinated biphenyl-induced cytotoxicity in nonmalignant human breast epithelial cells.  

PubMed

Polychlorinated biphenyls (PCBs) are environmental chemical contaminants believed to adversely affect cellular processes. We investigated the hypothesis that PCB-induced changes in the levels of cellular reactive oxygen species (ROS) induce DNA damage resulting in cytotoxicity. Exponentially growing cultures of human nonmalignant breast epithelial cells (MCF10A) were incubated with PCBs for 3 days and assayed for cell number, ROS levels, DNA damage, and cytotoxicity. Exposure to 2,2',4,4',5,5'-hexachlorobiphenyl (PCB153) or 2-(4-chlorophenyl)benzo-1,4-quinone (4-Cl-BQ), a metabolite of 4-chlorobiphenyl (PCB3), significantly decreased cell number and MTS reduction and increased the percentage of cells with sub-G1 DNA content. Results from electron paramagnetic resonance (EPR) spectroscopy showed a 4-fold increase in the steady-state levels of ROS, which was suppressed in cells pretreated with catalase. EPR measurements in cells treated with 4-Cl-BQ detected the presence of a semiquinone radical, suggesting that the increased levels of ROS could be due to the redox cycling of 4-Cl-BQ. A dose-dependent increase in micronuclei frequency was observed in PCB-treated cells, consistent with an increase in histone 2AX phosphorylation. Treatment of cells with catalase blunted the PCB-induced increase in micronuclei frequency and H2AX phosphorylation that was consistent with an increase in cell survival. Our results demonstrate a PCB-induced increase in cellular levels of ROS causing DNA damage, resulting in cell killing. PMID:18691649

Venkatesha, Venkatasubbaiah A; Venkataraman, Sujatha; Sarsour, Ehab H; Kalen, Amanda L; Buettner, Garry R; Robertson, Larry W; Lehmler, Hans-Joachim; Goswami, Prabhat C

2008-07-22

406

ATTEMPT IN CLASSIFICATION OF CATALASE-POSITIVE STAPHYLOCOCCI AND MICROCOCCI1  

PubMed Central

Mossel, D. A. A. (Central Institute for Nutrition and Food Research T.N.O., Utrecht, The Nethrlands). Attempt in classification of catalase-positive staphylococci and micrococci. J. Bacteriol. 84:1140–1147. 1962.—About 390 strains of Staphylococcus aureus, isolated from clinical material, and about 190 strains of coagulase-negative staphylococci and micrococci from strictly nonclinical habitats were studied by the following recently recommended biochemical tests: anaerobic dissimilation (“fermentation”) of mannitol, gelatin liquefaction, type of growth on tellurite-glycine agar, hydrolysis of urea, and KCN tolerance. The latter three tests appeared either not specific for, or not positive for, most S. aureus strains. Virtually all strains of S. aureus were gelatin-positive, but 71% of the other types of cocci also liquefied gelatin. Rapid anaerobic breakdown of mannitol, however, was shown by ca. 95% of the strains of S. aureus, and late fermentation by an additional 3%. Of 105 obligately aerobic coagulase tive cocci (micrococci), none fermented mannitol; of 40 facultatively anaerobic, coagulase-negative cocci (staphylococci), only 7 (18%) fermented mannitol. Oxidative metabolism of mannitol occurred in only three (<1%) strains of S. aureus but was detected in roughly half of the isolates of both groups of coagulase-negative cocci. Pigmentation was confirmed to be of little value, because roughly 50% of both coagulase-positive and -negative strains showed a pale-yellow color on Chapman's mannitol salt agar while 13% of the S. aureus strains tested were white. A key to the classification of catalase-positive cocci consistent with that currently used for Enterobacteriaceae has been based on these figures.

Mossel, D. A. A.

1962-01-01

407

Probing the function of Mycobacterium tuberculosis catalase-peroxidase by site-directed mutagenesis.  

PubMed

Catalase-peroxidase is a multi-functional heme-dependent enzyme which is well known for its ability to carry out both catalatic and peroxidatic reactions. Catalase-peroxidase from Mycobacterium tuberculosis(mtCP) is of particular interest because this enzyme activates the pro-antitubercular drug isoniazid. It is estimated that 2 billion people are infected with M. tuberculosis, the principal causative agent of tuberculosis, and that 2 million people die from the disease each year. The rise of drug-resistant strains continues to be of critical concern and it is well documented that mutations which reduce activity or inactivate mtCP lead to increased levels of isoniazid resistance in M. tuberculosis. The recent determination of the crystal structure for M. tuberculosis mtCP has aided the understanding of how the enzyme functions and provides a three-dimensional framework for testing hypotheses about the roles of various residues in the active site. Here we report site-directed mutagenesis studies of three conserved residues located near the heme of mtCP, His-108, Trp-107 and Trp-321 including the construction of the double mutant W107F-W321F. Resulting mutants have been purified and their catalatic and peroxidatic activities have been determined. Data are compared in the context of related studies aimed at dissecting the roles of these residues in the different activities of the enzyme. Analyses of single and double mutants studied here emphasise that the hydrogen bonding network surrounding the heme in the active site appears more important for maintenance of catalatic rather than peroxidatic activity in CP enzymes. PMID:16315359

Eady, Nigel A J; Jesmin, Nigel A J; Servos, Spiros; Cass, Anthony E G; Nagy, Judit M; Brown, Katherine A

2005-11-01

408

Mechanism of the inhibition of catalase by ascorbate. Roles of active oxygen species, copper and semidehydroascorbate.  

PubMed

Ascorbate reversibly inhibits catalase, and this inhibition is enhanced and rendered irreversible by the prior addition of copper(II)-bishistidine. In the absence of copper, the inhibition was prevented and reversed by ethanol, but not by superoxide dismutase, benzoate, mannitol, thiourea, desferrioxamine, or DETAPAC. In the presence of the copper complex mannitol, benzoate, and superoxide dismutase still had no effect, but thiourea, desferrioxamine, DETAPAC, or additional histidine decreased the extent of inactivation to that seen in the absence of copper. In the presence of copper, ethanol protected at [ascorbate] less than 1 mM, but was ineffective at [ascorbate] greater than 2 mM, even in the absence of oxygen. Although in the absence of copper, complete removal of oxygen provided full protection against inactivation by ascorbate, this protection was not seen if the catalase was briefly preincubated with H2O2 prior to flushing with nitrogen, or if copper was present. In fact, if copper was present, inactivation was enhanced by the removal of oxygen. Increasing the concentration of oxygen from ambient to 100% slowed the inactivation, whether or not copper was present. It is concluded that the initial reversible inactivation involves reaction with H2O2 to form compound I, followed by one electron reduction of compound I to compound II. In the presence of added copper, the initial (reversible) inactivation allows H2O2 to accumulate sufficiently to permit irreversible inactivation. Since in the presence of copper oxygen is not required, and neither the reversible nor the irreversible inactivation was prevented by conventional scavengers of active forms of oxygen, the inactivation is likely mediated by semidehydroascorbate, and/or it may involve site-specific generation of the damaging intermediates. PMID:3003060

Davison, A J; Kettle, A J; Fatur, D J

1986-01-25

409

Characterization of the W321F mutant of Mycobacterium tuberculosis catalase-peroxidase KatG  

PubMed Central

A single amino acid mutation (W321F) in Mycobacterium tuberculosis catalase–peroxidase (KatG) was constructed by site-directed mutagenesis. The purified mutant enzyme was characterized using optical and electron paramagnetic resonance spectroscopy, and optical stopped-flow spectrophotometry. Reaction of KatG(W321F) with 3-chloroperoxybenzoic acid, peroxyacetic acid, or t-butylhydroperoxide showed formation of an unstable intermediate assigned as Compound I (oxyferryl iron:porphyrin ?-cation radical) by similarity to wild-type KatG, although second-order rate constants were significantly lower in the mutant for each peroxide tested. No evidence for Compound II was detected during the spontaneous or substrate-accelerated decay of Compound I. The binding of isoniazid, a first-line anti-tuberculosis pro-drug activated by catalase–peroxidase, was noncooperative and threefold weaker in KatG(W321F) compared with wild-type enzyme. An EPR signal assigned to a protein-based radical tentatively assigned as tyrosyl radical in wild-type KatG, was also observed in the mutant upon reaction of the resting enzyme with alkyl peroxide. These results show that mutation of residue W321 in KatG does not lead to a major alteration in the identity of intermediates formed in the catalytic cycle of the enzyme in the time regimes examined here, and show that this residue is not the site of stabilization of a radical as might be expected based on homology to yeast cytochrome c peroxidase. Furthermore, W321 is indicated to be important in KatG for substrate binding and subunit interactions within the dimer, providing insights into the origin of isoniazid resistance in clinically isolated KatG mutants.

Yu, Shengwei; Chouchane, Salem; Magliozzo, Richard S.

2002-01-01

410

The effect of intracellular delivery of catalase and antisense oligonucleotides to NF-kappaB using albumin microcapsules in the endotoxic shock model.  

PubMed

Microencapsulated (MC) catalase has been shown to inhibit H(2)O(2) and tumor necrosis factor (TNF) in vitro after endotoxin stimulation. It is the purpose of this study to determine whether MC catalase improves pro-inflammatory cytokine inhibition and mortality in an endotoxic shock model in vivo. We also examined whether MC catalase and antisense oligonucleotides (ASO) to nuclear factor kappaB (NF-kappaB) together improved survival by inhibiting pro-inflammatory cytokines using different mechanisms. Methods: Albumin microcapsules containing catalase and ASO to NF-kappaB were prepared 2-7 microm in size by using a Büchi spray dryer. Progressively increasing doses of MC catalase, MC ASO to NF-kappaB, and the combination were given to rats before the administration of Escherichia coli endotoxin. Results demonstrated 60% survival in rats given 15 mg/kg MC catalase, 70% survival with 20 mg/kg MC ASO NF-kappaB, and 80% survival with the combination. TNF was inhibited by 53% in the MC catalase group 4 h after endotoxin administration, 43% in the ASO NF-kappaB group, and 78% in the combination group compared to controls. In conclusion, this study demonstrates the effectiveness of MC intracellular delivery of the naturally occurring antioxidant catalase in improving animal survival. The addition of ASO to NF-kappaB improved both cytokine inhibition and animal survival in endotoxic shock. PMID:19845486

Siwale, Rodney C; Oettinger, Carl W; Addo, Richard; Siddig, Aladin; D'Souza, Martin J

2009-11-01

411

The effect of vasoactive intestinal peptide (VIP) on superoxide dismutase and catalase activities in renal tissues of rats exposed to hemorrhagic ischemia-reperfusion  

Microsoft Academic Search

The effect of vasoactive intestinal peptide (VIP) on the activities of superoxide dismutase and catalase was investigated in renal tissues of rats exposed to 30% hemorrhage followed by reperfusion. In addition to enzyme activities, renal tissues were also histologically evaluated. Thirty percent hemorrhage had no significant effect on the activity of either enzyme. Reperfusion altered the activity of renal catalase

Ne?e Tunçel; Muzaffer Tunçel

1995-01-01

412

Effect of the Peroxisome Proliferator Ciprofibrate on Lipid Peroxidation and 8-Hydroxydeoxyguanosine Formation in Transgenic Mice with Elevated Hepatic Catalase Activity  

Microsoft Academic Search

Peroxisome proliferators are a group of non-genotoxic hepatic carcinogens which have been proposed to act by increasing oxidative damage in the liver. To test this hypothesis, we have produced a transgenic mouse line that has elevated catalase activity specifically in the liver. In this study, we have examined if catalase overexpression influences the induction of lipid peroxidation or oxidative DNA

Vani Nilakantan; Brett T Spear; Howard P Glauert

1998-01-01

413

Preliminary Study on Glucose Oxidase–Catalase Enzyme System to Control the Browning of Apple and Pear Purées  

Microsoft Academic Search

Oxygen is a key factor in fruit purées browning. The use of a commercial glucose oxidase–catalase enzyme system (GOX) for oxygen removal and browning control of Golden Delicious apple and Kaiser pear purées during storage has been investigated. The effect of ascorbic acid and peroxidase has also been tested and results compared with control (no treatment). Colour change was quantified

G. P. Parpinello; F. Chinnici; A. Versari; C. Riponi

2002-01-01

414

Inabenfide-Induced Alleviation of Salt Stress in Rice as Linked to Changes in Salicylic Acid Content and Catalase Activity  

Microsoft Academic Search

The effect of inabenfide was investigated in rice seedlings subjected to salt stress in relation to changes in chlorophyll fluorescence (? F\\/Fm'), lipid peroxidation, salicylic acid (SA) content, and catalase (CAT) activity. A reduction in shoot growth of rice seedlings by 120 mM NaCl treatment was significantly alleviated by pretreatment with 30 ? M inabenfide. Sodium ion content was not

Hiroko Sawada; Dea-Wook Kim; Katsuichiro Kobayashi

415

Effect of moderated pressure on the activity and termostability of three microbial enzymes: catalase, ?-galactosidase and alcohol dehydrogenase  

Microsoft Academic Search

The effect of moderate gas pressure on the activity and termostability of three microbial enzymes: catalase from Aspergillus niger, ?-galactosidase from Escherichia coli and alcohol dehydrogenase from Saccharomyces cerevisiae was study. Batch assays were carried out in a hyperbaric bioreactor at increased pressure up to 9 bar using the activity at atmospheric pressure as pattern. Interactions between the effects of

Helena Ribeiro; Manuel Mota; Isabel Belo

416

Age-related changes in antioxidant enzymes, superoxide dismutase, catalase, glutathione peroxidase and glutathione in different regions of mouse brain  

Microsoft Academic Search

It has been proposed that neurodegenerative processes of aging are associated with the generation of reactive oxygen species (ROS) during cellular metabolism. These reactive oxygen species are scavenged by antioxidant enzymes in biological systems. The present study was designed to determine the selective distribution of the antioxidant enzymes superoxide dismutase, catalase and glutathione peroxidase activity and reduced glutathione (GSH) levels

S. Hussain; W. Slikker; S. F. Ali

1995-01-01

417

Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase  

Microsoft Academic Search

The usual method of staining polyacrylamide gel electropherograms for superoxide dismutase activity utilizes a photochemical flux of Oâ⁻ to reduce nitroblue tetrazolium. Superoxide dismutases intercept Oâ⁻, preventing formazan production and thus causing achromatic bands. In the presence of HâOâ, catalase also yield achromatic bands during this staining procedure. This is due to local elevation of pOâ by the catalytic decomposition

D. A. Clare; M. N. Duong; D. Darr; F. Archibald; I. Fridovich

1984-01-01

418

Evidence for three differentially regulated catalase genes in Neurospora crassa: effects of oxidative stress, heat shock, and development.  

PubMed Central

Genetic and biochemical studies demonstrated that Neurospora crassa possesses three catalases encoded by three separate structural genes. The specific activities of the three enzymes varied in response to superoxide-mediated stress, heat shock, and development. The three loci, which we designated cat-1, cat-2, and cat-3, map to the right arms of chromosomes III, VII, and III, respectively. The cat-1-encoded enzyme (designated Cat-1; estimated molecular weight, 315,000; pI 5.2) was the predominant catalase in rapid-growth mycelium, and its activity was substantially increased in paraquat-treated and heat-shocked mycelium. Cat-2 (Mw, 165,000; pI 5.4) was absent from rapid-growth mycelium but present at low levels in conidia and stationary-phase mycelium. It was the predominant catalase in extracts derived from mycelium that had been heat shocked for 2 h. Cat-3 (Mw, 340,000; pI 5.5) was the predominant catalase in extracts from mature conidia. Images

Chary, P; Natvig, D O

1989-01-01

419

Prospective Study of Catalase-positive Coryneform Organisms in Clinical Specimens: Identification, Clinical Relevance, and Antibiotic Susceptibility  

Microsoft Academic Search

During a 6-month period, all clinical isolates of catalase-positive coryneform organisms, which were isolated during the routine processing of clinical specimens, were characterized in the laboratory of the 1800-bed University Hospital of Leuven. The distribution of the species in the corynebacteria was: Corynebacterium amycolatum 70 (53%), Corynebacterium jeikeium 16 (12%), Corynebacterium striatum 11 (8%), Corynebacterium afermentans 10 (7%), Corynebacterium minutissimum

K Lagrou; J Verhaegen; M Janssens; G Wauters; L Verbist

1998-01-01

420

Superoxide dismutase, catalase and acetylcholinesterase: biomarkers for the joint effects of cadmium, zinc and methyl parathion contamination in water  

Microsoft Academic Search

Heavy metals are known to reduce the activities of antioxidant enzymes (e.g. superoxide dismutase, catalase), while organophosphorous insecticides are known to inhibit the activity of the enzyme acetylcholinesterase. In this study, the activities of these three enzymes in zebrafish (Danio rerio) tissues were assessed to evaluate the consequences heavy metal and organophosphate contamination in aquatic systems. When the fish were

XuePing Ling; YiHeng Zhang; YingHua Lu; HeQing Huang

2011-01-01

421

Combining ability for superoxide dismutase, peroxidase and catalase enzymes in cabbage head ( Brassica oleracea var. capitata L.)  

Microsoft Academic Search

Antioxidant enzymes have been touted as beneficial for enhancing the fitness, preventing disorders, and mitigating the effects of aging and senescence. Our objective was to evaluate combining ability of superoxide dismutase, peroxidase, and catalase activity in cabbage head. Head samples were frozen immediately in liquid nitrogen and placed at ?80°C for assay. Less than unity values of ?2gca\\/?2sca ratio for

B. K. Singh; S. R. Sharma

2009-01-01

422

Effects of crop rotation and fertilization on catalase activity in a soil of the southeastern United States  

Microsoft Academic Search

Summary Catalase activity of a loamy sand under a 3-year crop rotation in the southeastern U.S.A. was monitored. Corn (Zea mays L.), cotton (Gossypium hirsutum L.), and soybean [Glycine max (L.) Merr.] were the summer crops in the rotation. Winter wheat (Triticum aestivum L.) was planted after corn, and soybean was followed by a winter fallow period. Cotton was followed

R. Rodríguez-Kábana; B. Truelove

1982-01-01

423

The induction of human superoxide dismutase and catalase in vivo: a fundamentally new approach to antioxidant therapy.  

PubMed

A composition consisting of extracts of five widely studied medicinal plants (Protandim) was administered to healthy human subjects ranging in age from 20 to 78 years. Individual ingredients were selected on the basis of published findings of induction of superoxide dismutase (SOD) and/or catalase in rodents in vivo, combined with evidence of decreasing lipid peroxidation. Each ingredient was present at a dosage sufficiently low to avoid any accompanying unwanted pharmacological effects. Blood was analyzed before supplementation and after 30 and 120 days of supplementation (675 mg/day). Erythrocytes were assayed for SOD and catalase, and plasma was assayed for lipid peroxidation products as thiobarbituric acid-reacting substances (TBARS), as well as uric acid, C-reactive protein, and cholesterol (total, LDL, and HDL). Before supplementation, TBARS showed a strong age-dependent increase. After 30 days of supplementation, TBARS declined by an average of 40% (p = 0.0001) and the age-dependent increase was eliminated. By 120 days, erythrocyte SOD increased by 30% (p < 0.01) and catalase by 54% (p < 0.002). We conclude that modest induction of the catalytic antioxidants SOD and catalase may be a much more effective approach than supplementation with antioxidants (such as vitamins C and E) that can, at best, stoichiometrically scavenge a very small fraction of total oxidant production. PMID:16413416

Nelson, Sally K; Bose, Swapan K; Grunwald, Gary K; Myhill, Paul; McCord, Joe M

2006-01-15

424

Age-related changes in catalase and peroxidase activities in the excised leaves of Eleusine coracana Gaertin. cv PR 202 during senescence.  

PubMed

Changes in the activities of the enzymes catalase and peroxidase were studied in the excised leaves of ragi (Eleusine coracana Gaertn. cv PR 202) plants belonging to different ages. Catalase exhibited a positive and peroxidase a negative correlation with the changes in chlorophyll. Catalase and peroxidase were negatively correlated with each other. Peroxidase exhibited an age-related drift in its activity. Kinetin could maintain the levels of chlorophyll and catalase, and also caused an increase in peroxidase activity. Both indoleacetic acid and gibberellic acid had no effect on the changes of chlorophyll but increased peroxidase activity. Catalase levels were maintained by indoleacetic acid but gibberellic acid had no effect on this enzyme. PMID:6321215

Kumar, K B; Khan, P A

1983-01-01

425

Catalase Abrogates ?-Lapachone-Induced PARP1 Hyperactivation-Directed Programmed Necrosis in NQO1-Positive Breast Cancers.  

PubMed

Improving patient outcome by personalized therapy involves a thorough understanding of an agent's mechanism of action. ?-Lapachone (clinical forms, Arq501/Arq761) has been developed to exploit dramatic cancer-specific elevations in the phase II detoxifying enzyme NAD(P)H:quinone oxidoreductase (NQO1). NQO1 is dramatically elevated in solid cancers, including primary and metastatic [e.g., triple-negative (ER-, PR-, Her2/Neu-)] breast cancers. To define cellular factors that influence the efficacy of ?-lapachone using knowledge of its mechanism of action, we confirmed that NQO1 was required for lethality and mediated a futile redox cycle where ?120 moles of superoxide were formed per mole of ?-lapachone in 2 minutes. ?-Lapachone induced reactive oxygen species (ROS), stimulated DNA single-strand break-dependent poly(ADP-ribose) polymerase-1 (PARP1) hyperactivation, caused dramatic loss of essential nucleotides (NAD(+)/ATP), and elicited programmed necrosis in breast cancer cells. Although PARP1 hyperactivation and NQO1 expression were major determinants of ?-lapachone-induced lethality, alterations in catalase expression, including treatment with exogenous enzyme, caused marked cytoprotection. Thus, catalase is an important resistance factor and highlights H2O2 as an obligate ROS for cell death from this agent. Exogenous superoxide dismutase enhanced catalase-induced cytoprotection. ?-Lapachone-induced cell death included apoptosis-inducing factor (AIF) translocation from mitochondria to nuclei, TUNEL+ staining, atypical PARP1 cleavage, and glyceraldehyde 3-phosphate dehydrogenase S-nitrosylation, which were abrogated by catalase. We predict that the ratio of NQO1:catalase activities in breast cancer versus associated normal tissue are likely to be the major determinants affecting the therapeutic window of ?-lapachone and other NQO1 bioactivatable drugs. Mol Cancer Ther; 12(10); 2110-20. ©2013 AACR. PMID:23883585

Bey, Erik A; Reinicke, Kathryn E; Srougi, Melissa C; Varnes, Marie; Anderson, Vernon E; Pink, John J; Li, Long Shan; Patel, Malina; Cao, Lifen; Moore, Zachary; Rommel, Amy; Boatman, Michael; Lewis, Cheryl; Euhus, David M; Bornmann, William G; Buchsbaum, Donald J; Spitz, Douglas R; Gao, Jinming; Boothman, David A

2013-07-24

426

Further studies on O sub 2 -resistant photosynthesis and photorespiration in a tobacco mutant with enhanced catalase activity  

SciTech Connect

The increase in net photosynthesis in M{sub 4} progeny of an O{sub 2}-resistant tobacco (Nicotiana tabacum) mutant relative to wild-type plants at 21 and 42% O{sub 2} has been confirmed and further investigated. Self-pollination of an M{sub 3} mutant produced M{sub 4} progeny segregating high catalase phenotypes (average 40% greater than wild type) at a frequency of about 60%. The high catalase phenotype cosegregated precisely with O{sub 2}-resistant photosynthesis. About 25% of the F{sub 1} progeny of reciprocal crosses between the same M{sub 3} mutant and wild type had high catalase activity, whether the mutant was used as the maternal or paternal parent, indicating nuclear inheritance. In high-catalase mutants the activity of NADH-hydroxypyruvate reductase, another peroxisomal enzyme, was the same as wild type. The mutants released 15% less photorespiratory CO{sub 2} as a percent of net photosynthesis in CO{sub 2}-free 21% O{sub 2} and 36% less in CO{sub 2}-free 42% O{sub 2} compared with wild type. The mutant leaf tissue also released less {sup 14}CO{sub 2} per (1-{sup 14}C)glycolate metabolized than wild type in normal air, consistent with less photorespiration in the mutant. The O{sub 2}-resistant photosynthesis appears to be caused by a decrease in photorespiration especially under conditions of high O{sub 2} where the stoichiometry of CO{sub 2} release per glycolate metabolized is expected to be enhanced. The higher catalase activity in the mutant may decrease the nonenzymatic peroxidation of keto-acids such as hydroxypyruvate and glyoxylate by photorespiratory H{sub 2}O{sub 2}.

Zelitch, I. (Connecticut Agricultural Experiment Station, New Haven (USA))

1990-02-01

427

Cardiac-specific overexpression of catalase attenuates paraquat-induced myocardial geometric and contractile alteration: role of ER stress.  

PubMed

Paraquat, a quaternary nitrogen herbicide, is a highly toxic pro-oxidant that causes multiorgan failure including that of the heart via generation of reactive oxygen species, although the underlying mechanism has not been well elucidated. This study examined the influence of cardiac-specific overexpression of catalase, an antioxidant detoxifying H(2)O(2), on paraquat-induced myocardial geometric and functional alterations, with a focus on ER stress. FVB and catalase transgenic mice were administered paraquat for 48h. Myocardial geometry, contractile function, apoptosis, and ER stress were evaluated using echocardiography, edge detection, caspase-3 activity, and immunoblotting. Our results revealed that paraquat treatment significantly enlarged left ventricular (LV) end diastolic and systolic diameters; increased LV mass and resting myocyte length; reduced fractional shortening, cardiomyocyte peak shortening, and maximal velocity of shortening/relengthening; and prolonged relengthening duration in the FVB group. Whereas the catalase transgene itself did not alter myocardial geometry and function, it mitigated or significantly attenuated paraquat-elicited myocardial geometric and functional changes. Paraquat promoted overt apoptosis and ER stress as evidenced by increased caspase-3 activity, apoptosis, and ER stress markers including Bax, Bcl-2, GADD153, calregulin, and phosphorylated JNK, IRE1?, and eIF2?; all were ablated by the catalase transgene. Paraquat-induced cardiomyocyte dysfunction was mitigated by the ER stress inhibitor tauroursodeoxycholic acid. Moreover, the JNK inhibitor SP600125 reversed paraquat-induced ER stress as evidenced by enhanced GADD153 and IRE1? phosphorylation. Taken together, these data revealed that catalase may rescue paraquat-induced myocardial geometric and functional alteration possibly by alleviating JNK-mediated ER stress. PMID:20937379

Ge, Wei; Ge, We; Zhang, Yingmei; Han, Xuefeng; Ren, Jun

2010-10-27

428

Gestational exposure to BDE-99 produces toxicity through upregulation of CYP isoforms and ROS production in the fetal rat liver.  

PubMed

On gestation day (GD) 6 to GD 19, pregnant Sprague Dawley rats were orally exposed to 0, 0.5, 1, and 2 mg/kg/day to one of the most prevalent polybrominated diphenyl ethers congeners found in humans, 2,2',4,4',5-pentaBDE (BDE-99). All dams were euthanized on GD 20, and live fetuses were evaluated for sex, body weight, and external, internal, and skeletal malformations and developmental variations. The liver from one fetus of each litter was excised for the evaluation of oxidative stress markers and the messenger RNA expression of multiple cytochrome P450 (CYP) isoforms. Exposure to BDE-99 during the gestational period produced delayed ossification, slight hypertrophy of the heart, and enlargement of the liver in fetuses. A transplacental effect of BDE-99, evidenced by the activation of nuclear hormones receptors that induce the upregulation of CYP1A1, CYP1A2, CYP2B1, and CYP3A2 isoforms, was also found in fetal liver. These isoforms are correlated with the activity level of the enzyme catalase and the levels of thiobarbituric acid reactive substances. However, teratogenic effects from BDE-99 exposure were not observed. Clear signs of embryo/fetal toxicity, due to a possible hormonal disruption, were evidenced by a large increase in the CYP system and the production of reactive oxygen species in fetal liver. PMID:22331496

Blanco, Jordi; Mulero, Miquel; Domingo, José L; Sánchez, Domènec J

2012-02-13

429

Antioxidant pathways are up-regulated during biological nitrogen fixation to prevent ROS-induced nitrogenase inhibition in Gluconacetobacter diazotrophicus  

PubMed Central

Gluconacetobacter diazotrophicus, an endophyte isolated from sugarcane, is a strict aerobe that fixates N2. This process is catalyzed by nitrogenase and requires copious amounts of ATP. Nitrogenase activity is extremely sensitive to inhibition by oxygen and reactive oxygen species (ROS). However, the elevated oxidative metabolic rates required to sustain biological nitrogen fixation (BNF) may favor an increased production of ROS. Here, we explored this paradox and observed that ROS levels are, in fact, decreased in nitrogen-fixing cells due to the up-regulation of transcript levels of six ROS-detoxifying genes. A cluster analyses based on common expression patterns revealed the existence of a stable cluster with 99.8% similarity made up of the genes encoding the ?-subunit of nitrogenase Mo–Fe protein (nifD), superoxide dismutase (sodA) and catalase type E (katE). Finally, nitrogenase activity was inhibited in a dose-dependent manner by paraquat, a redox cycler that increases cellular ROS levels. Our data revealed that ROS can strongly inhibit nitrogenase activity, and G. diazotrophicus alters its redox metabolism during BNF by increasing antioxidant transcript levels resulting in a lower ROS generation. We suggest that careful controlled ROS production during this critical phase is an adaptive mechanism to allow nitrogen fixation.

Oliveira, Jose Henrique M.; Nogueira, Eduardo M.; Guedes, Helma V.; Oliveira, Pedro L.; Camara, Fernando; Baldani, Jose I.; Martins, Orlando B.

2010-01-01

430

Glucose oxidation catalyzed by liposomal glucose oxidase in the presence of catalase-containing liposomes.  

PubMed

A catalase-containing liposome (CAL) was prepared and characterized in terms of stability during storage and catalysis of the decomposition of hydrogen peroxide (H2O2) that was initially added or produced in the oxidation of glucose catalyzed by the glucose oxidase-containing liposomes (GOL). The reactors used were a test tube and an external loop airlift bubble column as the static liquid and circulating liquid flow systems, respectively. The free catalase (CA) at low concentrations was unstable during storage at 4 degrees C as a result of dissociation of the tetrameric CA subunits. On the other hand, the deactivation of the CA activity in the CAL was depressed because of the high CA concentration in the CAL liposome. The CAL effectively catalyzed the repeated decompositions at 25 degrees C with 10 mM H2O2 added initially, whereas the free CA was significantly deactivated during the repeated reactions. The high stability of the CAL was attributed to the moderately depressed reactivity, which was essentially derived from the diffusion limitation of the CAL membrane to H2O2 in the liquid bulk. In the GOL-catalyzed prolonged oxidation of 10 mM glucose at 40 degrees C in the static liquid in a test tube, both the free CA and CAL could continuously catalyze the decomposition of H2O2 produced. This was because the glucose oxidation rate was small due to the limited reactivity of the GOL to glucose with its low permeability through the GOL membrane. In the glucose oxidation catalyzed by the GOL with the free CA or the CAL in the airlift, much larger oxidation rates were observed compared to those in the test tube because the permeability of the GOL membrane to glucose was increased in the gas-liquid two phase flow in the airlift. The GOL/CAL system in the airlift operated in an acidic condition, which was preferable to the GO activity, gave the largest oxidation rate with negligible accumulation of the H2O2 produced. On the other hand, the GOL/free CA system gave an oxidation rate smaller than that of the GOL/CAL system even under the acidic condition due to an unfavorable interaction of the free CA molecules with the GOL membranes leading to the decreased reactivity of the GOL. PMID:16739952

Yoshimoto, Makoto; Miyazaki, Yuya; Kudo, Yoshiyuki; Fukunaga, Kimitoshi; Nakao, Katsumi

431

Failure of catalase to protect against aflatoxin B{sub 1}-induced mouse lung tumorigenicity  

SciTech Connect

The carcinogenic mycotoxin aflatoxin B{sub 1} (AFB{sub 1}) induces 8-hydroxy-2'-deoxyguanosine (8-OHdG) formation in mouse lung, an effect that can be prevented by treatment with polyethylene glycol-conjugated catalase (PEG-CAT). G {yields} T transversion mutation in K-ras, an early event in AFB{sub 1}-induced mouse lung carcinogenesis, is thought to result from AFB{sub 1}-8,9-exo-epoxide binding to DNA to form AFB{sub 1}-N{sup 7}-guanine, but may also result from formation of 8-OHdG. Therefore, oxidative DNA damage may be important in AFB{sub 1} carcinogenicity. The objective of this study was to determine whether PEG-CAT would prevent AFB{sub 1} tumorigenicity. Mouse lung tumorigenesis was assessed following treatment of female A/J mice with 300 kU/kg PEG-CAT ip and/or 50 mg/kg AFB{sub 1}. Mice were killed 7 months post-treatment and tumors greater than 1 mm in diameter were excised. Unexpectedly, the mean number of tumors per mouse in the PEG-CAT + AFB{sub 1} group (8.81 {+-} 3.64, n = 47) was greater than that of the group treated with AFB{sub 1} alone (7.05 {+-} 3.45, n = 42) (P < 0.05). The tumors obtained from mice treated with PEG-CAT + AFB{sub 1} were larger than those from mice treated with AFB{sub 1} alone (P < 0.05). There was no difference in K-ras exon 1 mutation spectrum or in the histological diagnosis of tumors between AFB{sub 1} and PEG-CAT + AFB{sub 1} groups (P > 0.05). In vitro incubation with mouse liver catalase (CAT) resulted in conversion of [{sup 3}H]AFB{sub 1} into a DNA-binding species, a possible explanation for the results observed in vivo. These results demonstrate that PEG-CAT is not protective against AFB{sub 1} carcinogenicity in mouse lung despite preventing DNA oxidation.

Guindon, Katherine A. [Department of Pharmacology and Toxicology, Queen's University, Kingston, Ontario, K7L 3N6 (Canada); Foley, Julie F.; Maronpot, Robert R. [National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709 (United States); Massey, Thomas E. [Department of Pharmacology and Toxicology, Queen's University, Kingston, Ontario, K7L 3N6 (Canada)], E-mail: masseyt@queensu.ca

2008-03-01

432

Biogenesis, trafficking and up-regulation of nicotinic ACh receptors.  

PubMed

Chronic nicotine exposure gives rise to neural adaptations that change whole cell physiology and behaviour mainly by interacting with neuronal nicotinic acetylcholine receptors (nAChRs). The major nicotine-induced neuroadaptation is the up-regulation of brain nAChRs by means of cell-delimited post-translational mechanisms. We review what is known of the processes regulating nAChR assembly, degradation and trafficking, and how nicotine-induced modulation of these processes leads to nAChR up-regulation and changes in downstream neuronal plasticity at molecular, cellular and circuit level. PMID:23830821

Colombo, Sara Francesca; Mazzo, Francesca; Pistillo, Fancesco; Gotti, Cecilia

2013-07-03

433

PaCATB, a secreted catalase protecting Podospora anserina against exogenous oxidative stress.  

PubMed

A differential mass spectrometry analysis of secreted proteins from juvenile and senescent Podospora anserina cultures revealed age-related differences in protein profiles. Among other proteins with decreased abundance in the secretome of senescent cultures a catalase, termed PaCATB, was identified. Genetic modulation of the abundance of PaCATB identified differential effects on the phenotype of the corresponding strains. Deletion of PaCatB resulted in decreased resistance, over-expression in increased resistance against hydrogen peroxide. While the lifespan of the genetically modified strains was found to be unaffected under standard growth conditions, increased exogenous hydrogen peroxide stress in the growth medium markedly reduced the lifespan of the PaCatB deletion strain but extended the lifespan of PaCatB over-expressors. Overall our data identify a component of the secretome of P. anserina as a new effective factor to cope with environmental stress, stress that under natural conditions is constantly applied on organisms and influences aging processes. PMID:21865610

Zintel, Sandra; Bernhardt, Dominik; Rogowska-Wrzesinska, Adelina; Osiewacz, Heinz D

2011-08-01

434

Catalase Prevents Maternal Diabetes-Induced Perinatal Programming via the Nrf2-HO-1 Defense System  

PubMed Central

We investigated whether overexpression of catalase (CAT) in renal proximal tubular cells (RPTCs) could prevent the programming of hypertension and kidney disease in the offspring of dams with maternal diabetes. Male offspring of nondiabetic and diabetic dams from two transgenic (Tg) lines (Hoxb7-green fluorescent protein [GFP]-Tg [controls] and Hoxb7/CAT-GFP-Tg, which overexpress CAT in RPTCs) were studied from the prenatal period into adulthood. Nephrogenesis, systolic blood pressure, renal hyperfiltration, kidney injury, and reactive oxygen species (ROS) generation were assessed. Gene expression of transforming growth factor-?1 (TGF-?1), nuclear factor erythroid 2p45–related factor-2 (Nrf2), and heme oxygenase-1 (HO-1) was tested in both in vitro and in vivo studies. Renal dysmorphogenesis was observed in offspring of Hoxb7-GFP-Tg dams with severe maternal diabetes; the affected male offspring displayed higher renal ROS generation and developed hypertension and renal hyperfiltration as well as renal injury with heightened TGF-?1 expression in adulthood. These changes were ameliorated in male offspring of diabetic Hoxb7/CAT-GFP-Tg dams via the Nrf2–HO-1 defense system. CAT promoted Nrf2 nuclear translocation and HO-1 gene expression, seen in both in vitro and in vivo studies. In conclusion, CAT overexpression in the RPTCs ameliorated maternal diabetes–induced perinatal programming, mediated, at least in part, by triggering the Nrf2–HO-1 defense system.

Chang, Shiao-Ying; Chen, Yun-Wen; Zhao, Xin-Ping; Chenier, Isabelle; Tran, Stella; Sauve, Alexandre; Ingelfinger, Julie R.; Zhang, Shao-Ling

2012-01-01

435

An immunodominant 90-kilodalton Aspergillus fumigatus antigen is the subunit of a catalase.  

PubMed Central

We have identified, purified, and characterized structurally and functionally a 90-kDa immunodominant antigen associated with the water-soluble fraction of Aspergillus fumigatus. This antigen is recognized by 90.3% of serum samples from patients with aspergilloma and should be considered either by itself or better in combination with other purified antigens as a candidate for developing a standardized immunoassay for the detection of aspergilloma. p90 is a glycoprotein containing at least two two N-linked sugar chains of 2 and 5 kDa, respectively, which are not necessary for its reactivity with aspergilloma serum samples. Using specific anti-p90 rabbit serum, we have demonstrated that under native conditions, p90 exists in oligomeric form and has associated catalase activity. This activity is resistant to extreme temperatures (> 60 degrees C), reducing agents (40 mM dithiothreitol), high concentrations of denaturing agents such as 8 M urea and 8% sodium dodecyl sulfate, and treatments with ethanol-chloroform-water (5:3:10 [vol/vol]) mixtures.

Lopez-Medrano, R; Ovejero, M C; Calera, J A; Puente, P; Leal, F

1995-01-01

436

Lack of effect of deferoxamine, dimethyl sulfoxide, and catalase on monocrotaline pyrrole pulmonary injury.  

PubMed

Monocrotaline pyrrole (MCTP) is a reactive metabolite of the pyrrolizidine alkaloid monocrotaline. MCTP given intravenously to rats causes pulmonary hypertension and right ventricular hypertrophy. Lesions in lungs after MCTP treatment contain macrophages and neutrophils, which may contribute to the damage by generation of reactive oxygen metabolites. Rats were treated with MCTP and agents known to protect against oxygen radical-mediated damage in acute models of neutrophil-dependent lung injury. Rats received MCTP and deferoxamine mesylate (DF), dimethyl sulfoxide (DMSO), or polyethylene glycol-coupled catalase (PEG-CAT). MCTP/vehicle-treated controls developed lung injury manifested as increased lung weight, release of lactate dehydrogenase into the airway, and sequestration of 125I-labeled bovine serum albumin in the lungs. Cotreatment of rats with DF, DMSO, or PEG-CAT did not protect against the injury due to MCTP. These results suggest that toxic oxygen metabolites do not play an important role in the pathogenesis of MCTP-induced pulmonary injury. PMID:3573071

Bruner, L H; Johnson, K; Carpenter, L J; Roth, R A

1987-01-01

437

Association of polymorphic markers of the catalase and superoxide dismutase genes with type 2 diabetes mellitus.  

PubMed

Our study aims at determining whether genetic polymorphisms of catalase (CAT 1167C/T) and superoxide dismutase (SOD +35 A/C) could be associated with type 2 diabetes mellitus (T2DM). The study was conducted on 105 Egyptian patients with T2DM and 115 control subjects. Genotypes were done by polymerase chain reaction-restriction fragment length polymorphism methods. Homeostatic model assessment of insulin resistance (HOMA-IR), CAT and SOD activities, glycated hemoglobin, and insulin and lipid profiles were assessed. CAT and SOD activities were significantly decreased in T2DM compared with the control subjects. T allele of CAT and C allele of SOD1 were significant risk factors for T2DM. No effects of CAT or SOD1 gene polymorphisms on glycated haemoglobin or on HOMA-IR were found. With regard to the enzymes activities, only +35 A/C of SOD1 was related to SOD activity. Genetic variants C1167T of CAT gene and +35 A/C of SOD1 gene has no role in insulin resistance in T2DM. PMID:22970972

Ghattas, Maivel H; Abo-Elmatty, Dina M

2012-09-12

438

Biopharmacology of Enzyme Conjugates: Vasoprotective Activity of Supramolecular Superoxide Dismutase-Chondroitin Sulfate-Catalase Derivative  

PubMed Central

Bienzyme conjugate was obtained by the covalent connection of superoxide dismutase with catalase through endothelial glycocalyx glycosaminoglycan – chondroitin sulfate (SOD-CHS-CAT). This SOD-CHS-CAT conjugate has vasoprotective activity in respect to platelet interactions, tonus of the ring arterial fragment of a rat blood vessel, as well as normalization of hemodynamic parameters in rats and rabbits in conditions of oxidative stress caused by the administration of hydrogen peroxide. The SOD-CHS-CAT conjugate had antiplatelet potential due to its antiaggregation action manifested through the combination of enzyme activities and an acquired supramolecular structure. The influence on arterial fragment tonus was equivalent for SOD and CAT in native and conjugated form. Blood pressure and heart rate were significant and effectively normalized with SOD-CHS-CAT conjugate in rats and rabbits (after hydrogen peroxide administration as a perturbance stimulus). We have discovered the possibility of using the antioxidant bienzyme conjugate in chronic prophylaxis. It is important for a real development of the oral form of the SOD-CHS-CAT conjugate. These results indicate that the development of enzyme conjugates can be medically significant, as a promising approach for the creation of new drugs.

Maksimenko, A.V.; Vavaev, A.V.; Bouryachkovskaya, L.I.; Mokh, V.P.; Uchitel, I.A.; Lakomkin, V.L.; Kapelko, V.I.; Tischenko, E.G.

2010-01-01

439

Oxidation of phenolic compounds by the bifunctional catalase-phenol oxidase (CATPO) from Scytalidium thermophilum.  

PubMed

The thermophilic fungus Scytalidium thermophilum produces a novel bifunctional catalase with an additional phenol oxidase activity (CATPO); however, its phenol oxidation spectrum is not known. Here, 14 phenolic compounds were selected as substrates, among which (+)-catechin, catechol, caffeic acid, and chlorogenic acid yielded distinct oxidation products examined by reversed-phase HPLC chromatography method. Characterization of the products by LC-ESI/MS and UV-vis spectroscopy suggests the formation of dimers of dehydrocatechin type B (hydrophilic) and type A (hydrophobic), as well as oligomers, namely, a trimer and tetramer from (+)-catechin, the formation of a dimer and oligomer of catechol, a dimer from caffeic acid with a caffeicin-like structure, as well as trimeric and tetrameric derivatives, and a single major product from chlorogenic acid suggested to be a dimer. Based on the results, CATPO oxidizes phenolic compounds ranging from simple phenols to polyphenols but all having an ortho-diphenolic structure in common. The enzyme also appears to have stereoselectivity due to the oxidation of (+)-catechin, but not that of epicatechin. It is suggested that CATPO may contribute to the antioxidant mechanism of the fungus and may be of value for future food and biotechnology applications where such a bifunctional activity would be desirable. PMID:22370948

Koclar Avci, Gulden; Coruh, Nursen; Bolukbasi, Ufuk; Ogel, Zumrut B

2012-02-28

440

Effects of Greek legume plant extracts on xanthine oxidase, catalase and superoxide dismutase activities.  

PubMed

Legumes are considered to have beneficial health implications, which have been attributed to their phytochemical content. Polyphenols are considered the most important phytochemical compounds extensively studied for their antioxidant properties. The aim of the present study was to examine the effects of potent antioxidant legume plant extracts on xanthine oxidase (XO), catalase (CAT) and superoxide dismutase (SOD) activities. XO exerts a dual role, as it is the major contributor of free radicals during exercise while it generates uric acid, the most potent antioxidant molecule in plasma. CAT and SOD are two of the main enzymes of the antioxidant defence of tissues. We demonstrate that the majority of the extracts inhibited XO activity, but they had no effect on CAT inhibition and SOD induction when used at low concentrations. These results imply that the tested extracts may be considered as possible source of novel XO inhibitors. However, we have shown that allopurinol administration, a known XO inhibitor, before exercise reduces performance and induces oxidative stress in rats. Considering the fact that the extracts examined had an inhibitory effect on XO activity, possibly posing a restriction in their characterization as antioxidants, phytochemical antioxidant administration before exercise should probably be reconsidered. PMID:21983805

Spanou, Chrysoula I; Veskoukis, Aristidis S; Stagos, Dimitrios; Liadaki, Kalliopi; Aligiannis, Nectarios; Angelis, Apostolos; Skaltsounis, Alexios-Leandros; Anastasiadi, Maria; Haroutounian, Serkos A; Kouretas, Dimitrios

2011-10-08

441

[The effect of superoxide dismutase and catalase on the delayed toxicity of doxorubicin].  

PubMed

The production of oxygen-free radicals has been proposed as a determinant of the delayed toxicity of doxorubicin. The aim of the present investigation was to evaluate the potential cardioprotective effect of superoxide dismutase (SOD) and catalase (CAT) against the delayed cardiomyopathy induced by doxorubicin (DXR) in a rat model. Female Sprague Dawley rats received 3 mg/kg of DXR intravenously weekly for 4 weeks. SOD or CAT were administered intravenously at the dose of 10000 U/kg 2 min before and 30 min after each DXR administration. Cardiac toxicity was monitored by means of electrocardiography (QaT interval) and by light and electron microscopy evaluation of left ventricle fragments. DXR treated rats showed, in comparison with control animals, a decrease of body weight gain, a progressive and irreversible prolongation of QaT and significant morphologic lesions consisting in myocyte vacuolization and myofibrillar loss. SOD significantly prevented the impairment of body weight gain and QaT prolongation. Moreover, morphologic lesions were significantly reduced in rats receiving DXR + SOD. On the contrary, CAT seems to be completely devoid of protective effect. PMID:1296877

Villani, F; Galimberti, M; Poggi, P; Rozza, A; Lanza, E; Favalli, L; Scavini, C

1992-10-01

442

Effects of humic acid-metal complexes on hepatic carnitine palmitoyltransferase, carnitine acetyltransferase and catalase activities  

SciTech Connect

A significant increase in activities of hepatic carnitine palmitoyltransferase and carnitine acetyltransferase was observed in male Balb/c mice intraperitoneally injected for 40 d with 0.125 mg/0.1 ml/d humic acid-metal complexes. Among these complexes, the humic acid-As complex was relatively effective, whereas humic acid-25 metal complex was more effective, and humic acid-26 metal complex was most effective. However, humic acid or metal mixtures, or metal such as As alone, was not effective. Humic acid-metal complexes also significantly decreased hepatic catalase activity. A marked decrease of 60-kDa polypeptide in liver cytoplasm was also observed on SDS-polyacrylamide gel electrophoresis after the mice had been injected with the complexes. Morphological analysis of a histopathological biopsy of such treated mice revealed several changes in hepatocytes, including focal necrosis and cell infiltration, mild fatty changes, reactive nuclei, and hypertrophy. Humic acid-metal complexes affect activities of metabolic enzymes of fatty acids, and this results in accumulation of hydrogen peroxide and increase of the lipid peroxidation. The products of lipid peroxidation may be responsible for liver damage and possible carcinogenesis. Previous studies in this laboratory had shown that humic acid-metal complex altered the coagulation system and that humic acid, per se, caused vasculopathy. Therefore, humic acid-metal complexes may be main causal factors of not only so-called blackfoot disease, but also the liver cancer prevailing on the southwestern coast of Taiwan.

Fungjou Lu; Youngshin Chen (National Taiwan Univ., Taipei (Taiwan, Province of China). Dept. of Biochemistry); Tienshang Huang (National Taiwan Univ., Taipei (Taiwan, Province of China). Dept. of Medicine)

1994-03-01

443

Potential toxicity of sarafloxacin to catalase: Spectroscopic, ITC and molecular docking descriptions  

NASA Astrophysics Data System (ADS)

The interaction between sarafloxacin and catalase (CAT) was studied by fluorescence spectroscopy, UV-visible absorption spectroscopy, circular dichroism (CD) spectroscopy, isothermal titration microcalorimetry (ITC) and molecular docking method. After deducting the inner filter effect, the fluorescence of CAT was quenched regularly by different concentrations of sarafloxacin. The quenching mechanism was studied by lifetime measurement, and it was proved to be mostly due to static quenching. The formation of sarafloxacin-CAT complex alters the micro-environment of amide moieties and tryptophan (Trp) residues, reduces the ?-helix content of the enzyme, changes the peripheral substituents on the porphyrin ring of heme and leads to the inhibition of the enzyme activity. Molecular docking study reveals that sarafloxacin is located between two ?-helix of CAT near to Trp 182 and Trp 185 residues, which supports the experimental results and helps to have a more clear understanding about the interaction mechanism. The change in the relative position of His 74 to heme induced by the variation of secondary structure is considered to be the major reason for the reduction of CAT activity. Moreover, sarafloxacin binds into a hydrophobic area of CAT mainly through hydrophobic interactions, which is consistent with the ITC analysis.

Cao, Zhaozhen; Liu, Rutao; Yang, Bingjun

2013-11-01

444

PaCATB, a secreted catalase protecting Podospora anserina against exogenous oxidative stress  

PubMed Central

A differential mass spectrometry analysis of secreted proteins from juvenile and senescent Podospora anserina cultures revealed age-related differences in protein profiles. Among other proteins with decreased abundance in the secretome of senescent cultures a catalase, termed PaCATB, was identified. Genetic modulation of the abundance of PaCATB identified differential effects on the phenotype of the corresponding strains. Deletion of PaCatB resulted in decreased resistance, over-expression in increased resistance against hydrogen peroxide. While the lifespan of the genetically modified strains was found to be unaffected under standard growth conditions, increased exogenous hydrogen peroxide stress in the growth medium markedly reduced the lifespan of the PaCatB deletion strain but extended the lifespan of PaCatB over-expressors. Overall our data identify a component of the secretome of P. anserina as a new effective factor to cope with environmental stress, stress that under natural conditions is constantly applied on organisms and influences aging processes.

Zintel, Sandra; Bernhardt, Dominik; Rogowska-Wrzesinska, Adelina; Osiewacz, Heinz D.

2011-01-01

445

Analysis of heme structural heterogeneity in Mycobacterium tuberculosis catalase-peroxidase (KatG).  

PubMed

Mycobacterium tuberculosis catalase-peroxidase (KatG) is a heme enzyme considered important for virulence, which is also responsible for activation of the anti-tuberculosis pro-drug isoniazid. Here, we present an analysis of heterogeneity in KatG heme structure using optical, resonance Raman, and EPR spectroscopy. Examination of ferric KatG under a variety of conditions, including enzyme in the presence of fluoride, chloride, or isoniazid, and at different stages during purification in different buffers allowed for assignment of spectral features to both five- and six-coordinate heme. Five-coordinate heme is suggested to be representative of "native" enzyme, since this species was predominant in the enzyme examined immediately after one chromatographic protocol. Quantum mechanically mixed spin heme is the most abundant form in such partially purified enzyme. Reduction and reoxidation of six-coordinate KatG or the addition of glycerol or isoniazid restored five-coordinate heme iron, consistent with displacement of a weakly bound distal water molecule. The rate of formation of KatG Compound I is not retarded by the presence of six-coordinate heme either in wild-type KatG or in a mutant (KatG[Y155S]) associated with isoniazid resistance, which contains abundant six-coordinate heme. These results reveal a number of similarities and differences between KatG and other Class I peroxidases. PMID:12506108

Chouchane, Salem; Girotto, Stefania; Kapetanaki, Sofia; Schelvis, Johannes P M; Yu, Shengwei; Magliozzo, Richard S

2002-12-28

446

Identification and characterization of tyrosyl radical formation in Mycobacterium tuberculosis catalase-peroxidase (KatG).  

PubMed

The catalytic function of Mycobacterium tuberculosis catalase-peroxidase (KatG) and its role in activation of the anti-tuberculosis antibiotic isoniazid were investigated using rapid freeze-quench electron paramagnetic resonance (RFQ-EPR) experiments. The reaction of KatG with peroxyacetic acid was followed as a function of time using x-band EPR at 77 K. A doublet EPR signal appears within 6.4 ms after mixing and at time points through hundreds of milliseconds. Thereafter, a singlet signal develops and finally predominates after 1 s, with a total yield of radical approximately 0.5 spin/heme. Simulation of the spectra provided EPR parameters consistent with those for tyrosyl radicals. Changes in the hyperfine splitting and/or line width in spectra for l-3,3-[2H2]tyrosine-labeled, but not l-2,4,5,6,7-[2H5]tryptophan-labeled KatG confirmed this assignment. The initial rate of radical formation was unchanged using a 3-fold or 10-fold excess of peroxyacetic acid, consistent with a rate-determining step involving an intermediate. Although Compound I is likely to be the precursor of tyrosyl radical in KatG, neither its EPR signal nor its reduction to Compound II during formation of the radical(s) could be observed. The tyrosyl radical doublet signal was rapidly quenched by addition of isoniazid and benzoic hydrazide, but not by iproniazid, which binds poorly to KatG. PMID:12205099

Chouchane, Salem; Girotto, Stefania; Yu, Shengwei; Magliozzo, Richard S

2002-08-29

447

Crystallization and preliminary X-ray analysis of a bifunctional catalase-phenol oxidase from Scytalidium thermophilum.  

PubMed

Catalase-phenol oxidase from Scytalidium thermophilum is a bifunctional enzyme: its major activity is the catalase-mediated decomposition of hydrogen peroxide, but it also catalyzes phenol oxidation. To understand the structural basis of this dual functionality, the enzyme, which has been shown to be a tetramer in solution, has been purified by anion-exchange and gel-filtration chromatography and has been crystallized using the hanging-drop vapour-diffusion technique. Streak-seeding was used to obtain larger crystals suitable for X-ray analysis. Diffraction data were collected to 2.8 A resolution at the Daresbury Synchrotron Radiation Source. The crystals belonged to space group P2(1) and contained one tetramer per asymmetric unit. PMID:19407383

Sutay Kocabas, Didem; Pearson, Arwen R; Phillips, Simon E V; Bakir, Ufuk; Ogel, Zumrut B; McPherson, Michael J; Trinh, Chi H

2009-04-24

448

PDZK1 upregulation in estrogen-related hyperpigmentation in melasma.  

PubMed

The pathogenesis of melasma is unknown, although the potential role of estrogen has been considered. Microarray and real-time PCR analyses revealed that upregulation of PDZ domain protein kidney 1 (PDZK1) is clinically correlated with melasma. Although there has been no report that PDZK1 is involved in pigmentation and/or melanogenesis, PDZK1 expression can be induced by estrogen. In this study, the role of PDZK1 upregulation in melasma was examined, particularly in connection with estrogen, using biopsied skin specimens from 15 patients and monocultures and cocultures of melanocytes and keratinocytes with or without overexpression or knockdown of PDZK1. Estrogen upregulated PDZK1. Overexpression of PDZK1 increased tyrosinase expression and melanosome transfer to keratinocytes, whereas PDZK1 knockdown reduced estrogen-induced tyrosinase expression, through regulation of expression of estrogen receptors (ERs) ER-? and ER-?. The PDZK1-induced tyrosinase expression and melanosome transfer was regulated by ion transporters such as sodium-hydrogen exchanger (NHE), cystic fibrosis transmembrane conductance regulator (CFTR), and SLC26A3, which showed a specific association with each ER subtype. In the melanosome transfer, PDZK1 also increased phosphorylation of ezrin/radixin/moesin (ERM) and ras-related C3 botulinum toxin substrate 1, but not the expression of proteinase-activated receptor-2. Collectively, upregulation of PDZK1 could have an important role in the development of melasma in connection with estrogen through NHE, CFTR, and SLC26A3. PMID:22696060

Kim, Nan-Hyung; Cheong, Kyung Ah; Lee, Tae Ryong; Lee, Ai-Young

2012-06-14

449

Immune up-regulation and tumor apoptosis by androstene steroids  

Microsoft Academic Search

? Androstenes steroid up-regulates immunity to increase resistance against lethal infection and lethal radiation, and mediates a rapid recovery of hematopoietic precursor cells after radiation injury. ? Androstenetriol increases the levels of the TH1 cytokines, IL-2, IL-3, IFN? and counteracts hydrocortisone mediated immune suppression. In contrast, 17? androstenediol inhibits proliferation and mediates apoptosis in tumor cells of murine and human

Roger M Loria

2002-01-01

450

Coexpression of bile salt hydrolase gene and catalase gene remarkably improves oxidative stress and bile salt resistance in Lactobacillus casei  

Microsoft Academic Search

Lactic acid bacteria (LAB) encounter various types of stress during industrial processes and gastrointestinal transit. Catalase\\u000a (CAT) and bile salt hydrolase (BSH) can protect bacteria from oxidative stress or damage caused by bile salts by decomposing\\u000a hydrogen peroxide (H2O2) or deconjugating the bile salts, respectively. Lactobacillus\\u000a casei is a valuable probiotic strain and is often deficient in both CAT and

Guohong WangSheng; Sheng Yin; Haoran An; Shangwu Chen; Yanling Hao

451

Purification and characterization of a novel bromoperoxidase-catalase isolated from bacteria found in recycled pulp white water  

Microsoft Academic Search

A bacterial strain, Pseudomonad EF group 70B, containing a high catalase-like activity was found in process water (white water) from pulp using recycled fibers. The enzyme was purified and characterized, and found to be a hydroperoxidase. The active enzyme has an apparent molecular mass of about 153 kDa with two identical subunits and a pI value of 4.7. It has

Heino Kuusk; Mariana Björklund; Jan Rydström

2001-01-01

452

Anti-apoptotic proteins and catalase-dependent apoptosis resistance in nickel chloride-transformed human lung epithelial cells  

PubMed Central

Chronic exposure to nickel compounds is associated with increased incidence of certain types of human cancer, including lung and nasal cancers. Despite intensive investigation, the oncogenic processes remain poorly understood. Apoptosis resistance is a key feature for tumor cells to escape physiological surveillance and acquire growth advantage over normal cells. Although NiCl2 exposure induces transformation of human lung epithelial cells, little information is available with regard to its molecular mechanisms, it is also not clear if the transformed cells are apoptosis resistant and tumorigenic. We explored the apoptosis resistance properties of nickel chloride-transformed human lung epithelial cells and the underlying mechanisms. The results showed that transformed BEAS-2B human lung epithelial cells are resistant to NiCl2-induced apoptosis. They have increased Bcl-2, Bcl-xL and catalase protein levels over the passage matched non-transformed counterparts. The mechanisms of apoptosis resistance are mitochondria-mediated and caspase-dependent. Forced overexpression of Bcl-2, Bcl-xL and catalase proteins reduced NiCl2-induced cell death; siRNA-mediated knockdown of their expression sensitized the cells to nickel-induced apoptosis, suggesting that Bcl-2, Bcl-xl and catalase protein expression plays a critical role in apoptosis resistance. Akt also participates in this process, as its overexpression increases Bcl-xL protein expression levels and attenuates NiCl2-induced apoptosis. Furthermore, transformed cells are tumorigenic in a xenograft model. Together, these results demonstrate that nickel-transformed cells are apoptosis-resistant and tumorigenic. Increased expression of Bcl-2, Bcl-xL and catalase proteins are important mechanisms contributing to transformed cell oncogenic properties.

YANG, YU-XIU; LI, XIU-LING; WANG, LEI; HAN, SHUANG-YIN; ZHANG, YAN-RUI; PRATHEESHKUMAR, POYIL; WANG, XIN; LU, JIAN; YIN, YUAN-QIN; SUN, LI-JUAN; BUDHRAJA, AMIT; HITRON, ANDREW J.; DING, SONG-ZE

2013-01-01

453

Exogenous H 2O 2 and catalase treatments interfere with Tri genes expression in liquid cultures of Fusarium graminearum  

Microsoft Academic Search

Effect of exogenous H2O2 and catalase was tested in liquid cultures of the deoxynivalenol and 15-acetyldeoxynivalenol-producing fungus Fusarium graminearum. Accordingly to previous results, H2O2 supplementation of the culture medium leads to increased toxin production. This study indicates that this event seems to be linked to a general up regulation of genes involved in the deoxynivalenol and 15-acetyldeoxynivalenol biosynthesis pathway, commonly

Nadia Ponts; Laetitia Pinson-Gadais; Christian Barreau; Florence Richard-Forget; Thérèse Ouellet

2007-01-01

454

Cloning and expression of the catalase-peroxidase gene from the hyperthermophilic archaeon Archaeoglobus fulgidus and characterization of the enzyme  

Microsoft Academic Search

A putative perA gene from Archaeoglobus fulgidus was cloned and expressed in Escherichia coli BL21(DE3), and the recombinant catalase-peroxidase was purified to homogeneity. The enzyme is a homodimer with a subunit molecular mass of 85 kDa. UV-visible spectroscopic analysis indicated the presence of protoheme IX as a prosthetic group (ferric heme), in a stoichiometry of 0.25 heme per subunit. Electron

S. W. M. Kengen; F. Bikker; Vos de W. M; Oost van der J

2001-01-01

455

The regulation of alcohol consumption in rats: The role of alcohol-metabolizing enzymes—Catalase and aldehyde dehydrogenase  

Microsoft Academic Search

Aldehyde dehydrogenase (ALDH) and catalase enzymatic activities in brain were assayed and compared to measures of alcohol consumption in two groups of animals screened and maintained on free-choice alcohol access under different conditions. In the first group of Long-Evans rats screened and maintained in home cages, mean alcohol intake was 3.49 g\\/kg\\/day with a range of 1.69–5.33 g\\/kg\\/day. When alcohol

Kathryn Gill; Zalman Amit; Brian R. Smith

1996-01-01

456

Biochemical biomarkers in environmental studies—lessons learnt from enzymes catalase, glutathione S -transferase and cholinesterase in two crustacean species  

Microsoft Academic Search

Background, aim and scope  For reliable environmental risk assessment of pollutants, knowledge on the effects at different levels of biological organisation\\u000a is needed. During the early days of biomarker research in environmental studies approximately two decades ago, biochemical\\u000a biomarkers were considered as the most promising tool for such purposes. Among these, three enzymes have often been studied:\\u000a catalase