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1

Catalase activity prevents exercise-induced up-regulation of vasoprotective proteins in venous tissue.  

PubMed

Physical activity induces favourable changes of arterial gene expression and protein activity, although little is known about its effect in venous tissue. Although our understanding of the initiating molecular signals is still incomplete, increased expression of endothelial nitric oxide synthase (eNOS) is considered a key event. This study sought to investigate the effects of two different training protocols on the expression of eNOS and extracellular superoxide dismutase (ecSOD) in venous and lung tissue and to evaluate the underlying molecular mechanisms. C57Bl/6 mice underwent voluntary exercise or forced physical activity. Changes of vascular mRNA and protein levels and activity of eNOS, ecSOD and catalase were determined in aorta, heart, lung and vena cava. Both training protocols similarly increased relative heart weight and resulted in up-regulation of aortic and myocardial eNOS. In striking contrast, eNOS expression in vena cava and lung remained unchanged. Likewise, exercise up-regulated ecSOD in the aorta and in left ventricular tissue but remained unchanged in lung tissue. Catalase expression in lung tissue and vena cava of exercised mice exceeded that in aorta by 6.9- and 10-fold, respectively, suggesting a lack of stimulatory effects of hydrogen peroxide. In accordance, treatment of mice with the catalase inhibitor aminotriazole for 6 weeks resulted in significant up-regulation of eNOS and ecSOD in vena cava. These data suggest that physiological venous catalase activity prevents exercise-induced up-regulation of eNOS and ecSOD. Furthermore, therapeutic inhibition of vascular catalase might improve pulmonary rehabilitation. PMID:21129156

Dao, Vu Thao-Vi; Floeren, Melanie; Kumpf, Stephanie; Both, Charlotte; Peter, Bärbel; Balz, Vera; Suvorava, Tatsiana; Kojda, Georg

2011-11-01

2

Icariin inhibits hydrogen peroxide-mediated cytotoxicity by up-regulating sirtuin type 1-dependent catalase and peroxiredoxin.  

PubMed

Previous studies suggest that flavonol icariin protects against neuron injury after oxygen and glucose deprivation by increasing SIRT1. This study demonstrates that icariin can inhibit H(2) O(2) -induced neurotoxicity. The neuroprotection of icariin enhances the antioxidant capacity through both a direct scavenging effect on over-produced free radicals and an indirect stimulating effect on the expression and activity of cellular antioxidant enzymes including catalase (CAT) and peroxiredoxin 1 (Prx1). The mechanism may be partially involved in the up-regulation of SIRT1. The SIRT1 antagonist can partly block this neuroprotection and the enhancement of CAT/Prx1 by icariin. These results indicate that the effect of icariin on H(2) O(2) -induced neurotoxicity is dependent on increasing SIRT1 and provides a potentially novel pharmacological strategy for stroke prevention and/or treatment. PMID:20533910

Zhang, Ling; Huang, Siyuan; Chen, Yanting; Wang, Zhongyuan; Li, Erguang; Xu, Yun

2010-11-01

3

CATALASE ACTIVITY IN LEPTOSPIRA  

PubMed Central

Rao, P. J. (University of Illinois, Urbana), A. D. Larson, and C. D. Cox. Catalase activity in Leptospira. J. Bacteriol. 88:1045–1048. 1964.—A number of serotypes of Leptospira were found to possess catalase activity, although considerable variation in activity existed among various serotypes. Catalase activity of L. pomona was reduced by inhibitors commonly employed for arresting catalase activity in other biological systems. Catalase activity was increased three to five times by growing cultures under conditions of oxygen availability; however, aeration had no beneficial effect on total viable cell crop. The relationship of oxygen to metabolism and future studies on virulence of the leptospirae is discussed. PMID:14219017

Rao, P. J.; Larson, A. D.; Cox, C. D.

1964-01-01

4

Cancer and Human Liver Catalase  

Microsoft Academic Search

SUMMARY Data presented in the present paper indicate that human liver catalase depression is related to weight loss. A statistical study was first made to determine the catalase activity in correlation of the iodotitrimetric and spectrophotometric methods for biopsy and autopsy samples from cancer and cancer-free patients. Cancer patients had a 2~ per cent lower liver catalase activity than cancer-free

EDWARD E. MASON; TING-FONG CHIN; YAO W. LI; SIDNEY E. ZIFFREN

1960-01-01

5

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

6

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

7

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

8

7 CFR 58.432 - Catalase.  

Code of Federal Regulations, 2011 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...

2011-01-01

9

7 CFR 58.432 - Catalase.  

Code of Federal Regulations, 2012 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...

2012-01-01

10

7 CFR 58.432 - Catalase.  

...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...

2014-01-01

11

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

12

Transcriptional regulation of the Drosophila catalase gene by the DRE/DREF system  

E-print Network

Reactive oxygen species (ROS) cause oxidative stress and aging. The catalase gene is a key component of the cellular antioxidant defense network. However, the molecular mechanisms that regulate catalase gene expression are poorly understood. In this study, we have identi®ed a DNA replication-related element (DRE; 5¢-TATCGATA) in the 5¢-¯anking region of the Drosophila catalase gene. Gel mobility shift assays revealed that a previously identi®ed factor called DREF (DREbinding factor) binds to the DRE sequence in the Drosophila catalase gene. We used site-directed mutagenesis and in vitro transient transfection assays to establish that expression of the catalase gene is regulated by DREF through the DRE site. To explore the role of DRE/DREF in vivo, we established transgenic ¯ies carrying a catalase±lacZ fusion gene with or without mutation in the DRE. The b-galactosidase expression patterns of these reporter transgenic lines demonstrated that the catalase gene is upregulated by DREF through the DRE sequence. In addition, we observed suppression of the ectopic DREF-induced rough eye phenotype by a catalase amorphic Catn1 allele, indicating that DREF activity is modulated by the intracellular redox state. These results indicate that the DRE/ DREF system is a key regulator of catalase gene expression and provide evidence of cross-talk between the DRE/DREF system and the antioxidant defense system.

So Young Park; Young-shin Kim; Dong-jin Yang; Mi-ae Yoo

2003-01-01

13

In vitro assembly of catalase.  

PubMed

Most aerobic organisms contain catalase, which functions to decompose hydrogen peroxide. Typical catalases are structurally complex homo-tetrameric enzymes with one heme prosthetic group buried in each subunit. It is not known how catalase in the cell is assembled from its constituents. The bacterium Enterococcus faecalis cannot synthesize heme but can acquire it from the environment to form a cytoplasmic catalase. We have in E. faecalis monitored production of the enzyme polypeptide (KatA) depending on the availability of heme and used our findings to devise a procedure for the purification of preparative amounts of in vivo-synthesized apocatalase. We show that fully active catalase can be obtained in vitro by incubating isolated apoprotein with hemin. We have characterized features of the assembly process and describe a temperature-trapped hemylated intermediate of the enzyme maturation process. Hemylation of apocatalase does not require auxiliary cell components, but rapid assembly of active enzyme seemingly is assisted in the cell. Our findings provide insight about catalase assembly and offer new experimental possibilities for detailed studies of this process. PMID:25148685

Baureder, Michael; Barane, Elisabeth; Hederstedt, Lars

2014-10-10

14

In Vitro Assembly of Catalase*  

PubMed Central

Most aerobic organisms contain catalase, which functions to decompose hydrogen peroxide. Typical catalases are structurally complex homo-tetrameric enzymes with one heme prosthetic group buried in each subunit. It is not known how catalase in the cell is assembled from its constituents. The bacterium Enterococcus faecalis cannot synthesize heme but can acquire it from the environment to form a cytoplasmic catalase. We have in E. faecalis monitored production of the enzyme polypeptide (KatA) depending on the availability of heme and used our findings to devise a procedure for the purification of preparative amounts of in vivo-synthesized apocatalase. We show that fully active catalase can be obtained in vitro by incubating isolated apoprotein with hemin. We have characterized features of the assembly process and describe a temperature-trapped hemylated intermediate of the enzyme maturation process. Hemylation of apocatalase does not require auxiliary cell components, but rapid assembly of active enzyme seemingly is assisted in the cell. Our findings provide insight about catalase assembly and offer new experimental possibilities for detailed studies of this process. PMID:25148685

Baureder, Michael; Barane, Elisabeth; Hederstedt, Lars

2014-01-01

15

High Dietary Fat Selectively Increases Catalase Expression within Cardiac Mitochondria*  

PubMed Central

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 H2O2 production, suggest that a localized catalase increase is needed to consume excessive mitochondrial H2O2 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 H2O2-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

2013-01-01

16

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

17

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

18

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

19

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

20

Classical catalase: ancient and modern.  

PubMed

This review describes the historical difficulties in devising a kinetically satisfactory mechanism for the classical catalase after its identification as a unique catalytic entity in 1902 and prior to the breakthrough 1947 analysis by Chance and co-workers which led to the identification of peroxide compounds I and II. The role of protons in the formation of these two ferryl complexes is discussed and current problems of inhibitory ligand and hydrogen donor binding at the active site are outlined, especially the multiple roles involving formate or formic acid. A previous mechanism of NADPH-dependent catalase protection against substrate inhibition is defended. A revised model linking the catalytic ('catalatic') action and the one-electron side reactions involving compound II is suggested. And it is concluded that, contrary to an idea proposed in 1963 that eukaryotic catalase might be a 'fossil enzyme', current thinking gives it a central role in the redox protective processes of long term importance for human and other eukaryotic and prokaryotic life. PMID:22326823

Nicholls, Peter

2012-09-15

21

Selective induction of catalase-mediated autophagy by dihydrocapsaicin in lung cell lines.  

PubMed

We reported that dihydrocapsaicin (DHC) induces autophagy in a catalase-regulated manner. In this study, we further examined the role of DHC-induced autophagy in lung cell lines. DHC-induced cytotoxicity was higher in WI38 and H1299 cells than in H460 and A549 cells, and was related to the loss of cell membrane integrity. However, apoptotic cells markedly increased in H460 and A549 cells. In WI38 and H1299 cells, DHC-induced catalase was correlated with a decrease of intracellular reactive oxygen species (ROS) and an increase in the level of LC3II, an autophagy marker, and LC3 conversion was attenuated by the catalase inhibitor 3-amino-1,2,4-triazole (3AT) or by knockdown of the catalase gene. In A549 cells, DHC downregulated catalase, led to ROS accumulation, and blocked LC3 conversion. In H460 cells expressing limited amount of catalase, DHC caused ROS accumulation and blocked LC3 conversion. However, H460 cells overexpressing catalase were able to induce autophagy. In contrast to Earle's balanced salt solution and rotenone, H(2)O(2) treatment caused ROS accumulation and did not promote upregulation of catalase and LC3II in lung cell lines. Cytoplasmic vacuolization in WI38 and H1299 cells was blocked by treatment of 3AT and which enhanced caspase-3 activity and LDH release. Suppression of autophagy by 3-methyladenine also enhanced DHC-induced cell death through apoptotic and necrotic cell death. In A549 and H460 cells, treatment of rapamycin attenuated DHC-induced cell death. Collectively, these results suggest that catalase regulates autophagy, which helps protect cells against apoptotic and necrotic cell death. PMID:20417273

Choi, Cheol-Hee; Jung, Yong-Keun; Oh, Seon-Hee

2010-07-15

22

Rapid upregulation of heart antioxidant enzymes during arousal from estivation in the Giant African snail (Achatina fulica)  

E-print Network

, a drastically suppressed metabolic rate and enhanced stress resistance. We tested the hypothesis that Achatina, or glutathione peroxidase, glutathione reductase or catalase activities were associated with estivation in any reductase activity was upregulated at 4 h post arousal in heart and foot tissues whereas catalase activity

Tattersall, Glenn

23

Catalase and glutathione peroxidase mimics  

PubMed Central

Overproduction of the reactive oxygen species (ROS) superoxide (O2?) and hydrogen peroxide (H2O2) are increasingly implicated in human disease and aging. ROS are also being explored as important modulating agents in a number of cell signaling pathways. Earlier work has focused on development of small catalytic scavengers of O2?, commonly referred to as superoxide dismutase (SOD) mimetics. Many of these compounds also have substantial abilities to catalytically scavenge H2O2 and peroxynitrite (ONOO?). Peroxides have been increasingly shown to disrupt cell signaling cascades associated with excessive inflammation associated with a wide variety of human diseases. Early studies with enzymatic scavengers like SOD frequently reported little or no beneficial effect in biologic models unless SOD was combined with catalase or a peroxidase. Increasing attention has been devoted to developing catalase or peroxidase mimetics as a way to treat overt inflammation associated with the pathophysiology of many human disorders. This review will focus on recent development of catalytic scavengers of peroxides and their potential use as therapeutic agents for pulmonary, cardiovascular, neurodegenerative and inflammatory disorders. PMID:18948086

Day, Brian J.

2009-01-01

24

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

25

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

26

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

27

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

28

Molecular cloning, characterization and gene expression of an antioxidant enzyme catalase (MrCat) from Macrobrachium rosenbergii.  

PubMed

In this study, we reported a full length of catalase gene (designated as MrCat), identified from the transcriptome database of freshwater prawn Macrobrachium rosenbergii. The complete gene sequence of the MrCat is 2504 base pairs in length, and encodes 516 amino acids. The MrCat protein contains three domains such as catalase 1 (catalase proximal heme-ligand signature) at 350-358, catalase 2 (catalase proximal active site signature) at 60-76 and catalase 3 (catalase family profile) at 20-499. The mRNA expressions of MrCat in healthy and the infectious hypodermal and hematopoietic necrosis virus (IHHNV) challenged M. rosenbergii were examined using quantitative real time polymerase chain reaction (qRT-PCR). The MrCat is highly expressed in digestive tract and all the other tissues (walking leg, gills, muscle, hemocyte, hepatopancreas, pleopods, brain and eye stalk) of M. rosenbergii taken for analysis. The expression is strongly up-regulated in digestive tract after IHHNV challenge. To understand its biological activity, the recombinant MrCat gene was constructed and expressed in Escherichia coli BL21 (DE3). The recombinant MrCat existed in high thermal stability and broad spectrum of pH, which showed over 95% enzyme activity between pH 5 and 10.5, and was stable from 40 °C to 70 °C, and exhibited 85-100% enzyme activity from 30 °C to 40 °C. PMID:22293093

Arockiaraj, Jesu; Easwvaran, Sarasvathi; Vanaraja, Puganeshwaran; Singh, Arun; Othman, Rofina Yasmin; Bhassu, Subha

2012-05-01

29

The role and regulation of catalase in respiratory tract opportunistic bacterial pathogens.  

PubMed

Respiratory tract bacterial pathogens are the etiologic agents of a variety of illnesses. The ability of these bacteria to cause disease is imparted through survival within the host and avoidance of pathogen clearance by the immune system. Respiratory tract pathogens are continually bombarded by reactive oxygen species (ROS), which may be produced by competing bacteria, normal metabolic function, or host immunological responses. In order to survive and proliferate, bacteria have adapted defense mechanisms to circumvent the effects of ROS. Bacteria employ the use of anti-oxidant enzymes, catalases and catalase-peroxidases, to relieve the effects of the oxidative stressors to which they are continually exposed. The decomposition of ROS has been shown to provide favorable conditions in which respiratory tract opportunistic bacterial pathogens such as Haemophilus influenzae, Mycobacterium tuberculosis, Legionella pneumophila, and Neisseria meningitidis are able to withstand exposure to highly reactive molecules and yet survive. Bacteria possessing mutations in the catalase gene have a decreased survival rate, yet may be able to compensate for the lack of catalatic activity if peroxidatic activity is present. An incomplete knowledge of the mechanisms by which catalase and catalase-peroxidases are regulated still persists, however, in some bacterial species, a regulatory factor known as OxyR has been shown to either up-regulate or down-regulate catalase gene expression. Yet, more research is still needed to increase the knowledge base in relation to this enzyme class. As with this review, we focus on major respiratory tract opportunistic bacterial pathogens in order to elucidate the function and regulation of catalases. The importance of the research could lead to the development of novel treatments against respiratory bacterial infections. PMID:25109939

Eason, Mia M; Fan, Xin

2014-09-01

30

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

31

Role of oxyradicals in the inactivation of catalase by ozone  

Microsoft Academic Search

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,

C. Whiteside; H. M. Hassan

1988-01-01

32

Protection of Bacillus pumilus spores by catalases.  

PubMed

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. PMID:22752169

Checinska, Aleksandra; Burbank, Malcolm; Paszczynski, Andrzej J

2012-09-01

33

Upregulation of Opioid Receptors  

Microsoft Academic Search

\\u000a It is well established that chronic exposure to opioid receptor antagonists can result in opioid receptor upregulation. The\\u000a phenomenon of antagonist-induced receptor upregulation is not unique to the opioid system but is common to many receptor systems\\u000a including adenergic, cholinergic, serotinergic, and dopaminergic receptors. Chronic administration of naloxone or naltrexone\\u000a reliably produces increases in binding to opioid receptors both in

Ellen M. Unterwald; Richard D. Howells

34

21 CFR 173.135 - Catalase derived from Micrococcus lysodeikticus.  

...DEPARTMENT OF HEALTH AND HUMAN SERVICES (CONTINUED) SECONDARY DIRECT FOOD ADDITIVES PERMITTED IN FOOD FOR HUMAN CONSUMPTION Enzyme Preparations and Microorganisms § 173.135 Catalase derived from Micrococcus lysodeikticus. Bacterial catalase...

2014-04-01

35

21 CFR 173.135 - Catalase derived from Micrococcus lysodeikticus.  

Code of Federal Regulations, 2011 CFR

...CONTINUED) FOOD FOR HUMAN CONSUMPTION (CONTINUED) SECONDARY DIRECT FOOD ADDITIVES PERMITTED IN FOOD FOR HUMAN CONSUMPTION Enzyme Preparations and Microorganisms § 173.135 Catalase derived from Micrococcus lysodeikticus. Bacterial catalase...

2011-04-01

36

21 CFR 173.135 - Catalase derived from Micrococcus lysodeikticus.  

Code of Federal Regulations, 2013 CFR

...CONTINUED) FOOD FOR HUMAN CONSUMPTION (CONTINUED) SECONDARY DIRECT FOOD ADDITIVES PERMITTED IN FOOD FOR HUMAN CONSUMPTION Enzyme Preparations and Microorganisms § 173.135 Catalase derived from Micrococcus lysodeikticus. Bacterial catalase...

2013-04-01

37

21 CFR 173.135 - Catalase derived from Micrococcus lysodeikticus.  

Code of Federal Regulations, 2012 CFR

...CONTINUED) FOOD FOR HUMAN CONSUMPTION (CONTINUED) SECONDARY DIRECT FOOD ADDITIVES PERMITTED IN FOOD FOR HUMAN CONSUMPTION Enzyme Preparations and Microorganisms § 173.135 Catalase derived from Micrococcus lysodeikticus. Bacterial catalase...

2012-04-01

38

21 CFR 173.135 - Catalase derived from Micrococcus lysodeikticus.  

Code of Federal Regulations, 2010 CFR

...CONTINUED) FOOD FOR HUMAN CONSUMPTION (CONTINUED) SECONDARY DIRECT FOOD ADDITIVES PERMITTED IN FOOD FOR HUMAN CONSUMPTION Enzyme Preparations and Microorganisms § 173.135 Catalase derived from Micrococcus lysodeikticus. Bacterial catalase...

2010-04-01

39

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

40

Original article Restoring catalase activity in Staphylococcus aureus subsp.  

E-print Network

Original article Restoring catalase activity in Staphylococcus aureus subsp. anaerobius leads; accepted 15 February 2010) Abstract � Staphylococcus aureus subsp. anaerobius, a microaerophilic / pathogenesis / catalase / abscess disease / sheep 1. INTRODUCTION Staphylococcus aureus subsp. anaerobius

Paris-Sud XI, Université de

41

Proton transfer drives protein radical formation in Helicobacter pylori catalase but not in Penicillium vitale catalase.  

PubMed

Heme catalases prevent cells from oxidative damage by decomposing hydrogen peroxide into water and molecular oxygen. Here we investigate the factors that give rise to an undesirable side reaction competing with normal catalase activity, the migration of a radical from the heme active site to the protein in the principal reaction intermediate compound I (Cpd I). Recently, it has been proposed that this electron transfer reaction takes place in Cpd I of Helicobacter pylori catalase (HPC), but not in Cpd I of Penicillium vitale catalase (PVC), where the oxidation equivalent remains located on the heme active site. Unraveling the factors determining the different radical locations could help engineer enzymes with enhanced catalase activity for detection or removal of hydrogen peroxide. Using quantum mechanics/molecular mechanics metadynamics simulations, we show that radical migration in HPC is facilitated by the large driving force (-0.65 eV) of the subsequent proton transfer from a histidine residue to the ferryl oxygen atom of reduced Cpd I. The corresponding free energy in PVC is significantly smaller (-0.19 eV) and, as we argue, not sufficiently high to support radical migration. Our results suggest that the energetics of oxoferryl protonation is a key factor regulating radical migration in catalases and possibly also in hydroperoxidases. PMID:21381757

Alfonso-Prieto, M; Oberhofer, H; Klein, M L; Rovira, C; Blumberger, J

2011-03-30

42

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

43

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

44

HYDROGEN PEROXIDE INDUCED OXIDATION OF PEROXISOMAL MALATE SYNTHASE AND CATALASE.  

E-print Network

Page 1 HYDROGEN PEROXIDE INDUCED OXIDATION OF PEROXISOMAL MALATE SYNTHASE AND CATALASE. Pria Anand1-6100 E-mail: robdon@gwu.edu Short title: Oxidation of Peroxisomal Malate Synthase and Catalase * Revised Manuscript (Unmarked) Click here to view linked References #12;Page 2 Abbreviations CAT , catalase; MS

Simha, Rahul

45

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

46

Breaking of seed dormancy by catalase inhibition.  

PubMed Central

Germination of some dormant seeds is promoted by solutions of thiourea, sodium nitrite, and hydroxylamine salts. The promotions are accompanied by irreversible inhibition of catalase (EC 1.11.1.6) in extracts from the seeds. The seeds are also promoted in germination by catechol and pyrogallol solutions. These effects are recorded for lettuce (Lactuca sativa L. cv. Grand Rapids) and pigweed (Amaranthus albus L.) seeds. The results indicae that metabolically derived hydrogen peroxide, spared from decomposition by catalase inhibition, oxidizes reduced NADPH required as the oxidant in the pentose pathway of glucose use. The metabolic system for such use of H2O2 involves the enzymes, peroxidase (EC 1.11.1.7) and pyridine nucleotide quinone oxidoreductase (EC 1.6.99.2), which are present in the dormant seed prior to imbibition of water. PMID:235126

Hendricks, S B; Taylorson, R B

1975-01-01

47

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

48

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

49

Preparation of highly efficient manganese catalase mimics.  

PubMed

The series of compounds [Mn(bpia)(mu-OAc)](2)(ClO(4))(2) (1), [Mn(2)(bpia)(2)(muO)(mu-OAc)](ClO(4))(3).CH(3)CN (2), [Mn(bpia)(mu-O)](2)(ClO(4))(2)(PF(6)).2CH(3)CN (3), [Mn(bpia)(Cl)(2)](ClO)(4) (4), and [(Mn(bpia)(Cl))(2)(mu-O)](ClO(4))(2).2CH(3)CN (5) (bpia = bis(picolyl)(N-methylimidazol-2-yl)amine) represents a structural, spectroscopic, and functional model system for manganese catalases. Compounds 3 and 5 have been synthesized from 2 via bulk electrolysis and ligand exchange, respectively. All complexes have been structurally characterized by X-ray crystallography and by UV-vis and EPR spectroscopies. The different bridging ligands including the rare mono-mu-oxo and mono-mu-oxo-mono-mu-carboxylato motifs lead to a variation of the Mn-Mn separation across the four binuclear compounds of 1.50 A (Mn(2)(II,II) = 4.128 A, Mn(2)(III,III) = 3.5326 and 3.2533 A, Mn(2)(III,IV) = 2.624 A). Complexes 1, 2, and 3 are mimics for the Mn(2)(II,II), the Mn(2)(III,III), and the Mn(2)(III,IV) oxidation states of the native enzyme. UV-vis spectra of these compounds show similarities to those of the corresponding oxidation states of manganese catalase from Thermus thermophilus and Lactobacillus plantarum. Compound 2 exhibits a rare example of a Jahn-Teller compression. While complexes 1 and 3 are efficient catalysts for the disproportionation of hydrogen peroxide and contain an N(4)O(2) donor set, 4 and 5 show no catalase activity. These complexes have an N(4)Cl(2) and N(4)OCl donor set, respectively, and serve as mimics for halide inhibited manganese catalases. Cyclovoltammetric data show that the substitution of oxygen donor atoms with chloride causes a shift of redox potentials to more positive values. To our knowledge, complex 1 is the most efficient binuclear functional manganese catalase mimic exhibiting saturation kinetics to date. PMID:12377052

Triller, Michael U; Hsieh, Wen-Yuan; Pecoraro, Vincent L; Rompel, Annette; Krebs, Bernt

2002-10-21

50

Methanol teratogenicity in mutant mice with deficient catalase activity and transgenic mice expressing human catalase.  

PubMed

The role of catalase in methanol (MeOH) teratogenesis is unclear. In rodents it both detoxifies reactive oxygen species (ROS) and metabolizes MeOH and its formic acid (FA) metabolite. We treated pregnant mice expressing either high (hCat) or low catalase activity (aCat), or their wild-type (WT) controls, with either MeOH (4g/kg ip) or saline. hCat mice and WTs were similarly susceptible to MeOH-initiated ophthalmic abnormalities and cleft palates. aCat and WT mice appeared resistant, precluding assessment of the developmental impact of catalase deficiency. Catalase activity was respectively increased at least 1.5-fold, and decreased by at least 35%, in hCat and aCat embryos and maternal livers. MeOH and FA pharmacokinetic profiles were similar among hCat, aCat and WT strains. Although the hCat results imply no ROS involvement, embryo culture studies suggest this may be confounded by maternal factors and/or a requirement for higher catalase activity in the hCat mice. PMID:23207165

Siu, Michelle T; Wiley, Michael J; Wells, Peter G

2013-04-01

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. PMID:22521743

Dash, Bhagirathi; Phillips, Timothy D.

2012-01-01

52

Hydrogen peroxide production regulates the mitochondrial function in insulin resistant muscle cells: effect of catalase overexpression.  

PubMed

The mitochondrial redox state plays a central role in the link between mitochondrial overloading and insulin resistance. However, the mechanism by which the ROS induce insulin resistance in skeletal muscle cells is not completely understood. We examined the association between mitochondrial function and H2O2 production in insulin resistant cells. Our hypothesis is that the low mitochondrial oxygen consumption leads to elevated ROS production by a mechanism associated with reduced PGC1? transcription and low content of phosphorylated CREB. The cells were transfected with either the encoded sequence for catalase overexpression or the specific siRNA for catalase inhibition. After transfection, myotubes were incubated with palmitic acid (500?M) and the insulin response, as well as mitochondrial function and fatty acid metabolism, was determined. The low mitochondrial oxygen consumption led to elevated ROS production by a mechanism associated with ?-oxidation of fatty acids. Rotenone was observed to reduce the ratio of ROS production. The elevated H2O2 production markedly decreased the PGC1? transcription, an effect that was accompanied by a reduced phosphorylation of Akt and CREB. The catalase transfection prevented the reduction in the phosphorylated level of Akt and upregulated the levels of phosphorylated CREB. The mitochondrial function was elevated and H2O2 production reduced, thus increasing the insulin sensitivity. The catalase overexpression improved mitochondrial respiration protecting the cells from fatty acid-induced, insulin resistance. This effect indicates that control of hydrogen peroxide production regulates the mitochondrial respiration preventing the insulin resistance in skeletal muscle cells by a mechanism associated with CREB phosphorylation and ?-oxidation of fatty acids. PMID:23643711

Barbosa, Marina R; Sampaio, Igor H; Teodoro, Bruno G; Sousa, Thais A; Zoppi, Claudio C; Queiroz, André L; Passos, Madla A; Alberici, Luciane C; Teixeira, Felipe R; Manfiolli, Adriana O; Batista, Thiago M; Cappelli, Ana Paula Gameiro; Reis, Rosana I; Frasson, Danúbia; Kettelhut, Isis C; Parreiras-e-Silva, Lucas T; Costa-Neto, Claudio M; Carneiro, Everardo M; Curi, Rui; Silveira, Leonardo R

2013-10-01

53

Staphylococcal catalase regulates its virulence and induces arthritis in catalase deficient mice.  

PubMed

To figure out whether in vivo expression of Staphylococcal catalase could correlate with the virulence and pathogenicity of the bacteria in the catalase deficient Swiss albino mice. 3 Amino 1, 2, 4 triazole (ATZ) (2 mg/g body wt) treated catalase deficient mice were infected with virulent S. aureus and bacterial burden, antioxidant enzyme levels were estimated after 3, 5 and 10 days of infection. Arthritic scores and levels of serum uric acid in mice were also determined. ATZ treatment was found to have slowed down the clearance of bacteria from blood and their rapid elimination from spleen. Increased tissue catalase activities in the spleen and liver of ATZ pre-treated mice even after 5 days of infection suggested its bacterial origin. It was further verified by zymographic analysis. Increased swelling of joints was observed after 5 days of infection. Uric acid level was found lesser in ATZ treated mice. ATZ treatment slowed the bacterial passage from blood with a lower tissue anti-oxidant enzymes leading to induction of joint inflammation. PMID:20509322

Sen, Riti; Das, Debaditya; Bishayi, Biswadev

2009-01-01

54

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

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

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] [Health Sciences Univ. of Hokkaido (Japan); and others

1996-02-09

57

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

58

Transcriptional repression of catalase in mouse skin tumor progression  

E-print Network

Previous studies in our laboratory have shown that the elevation of reactive oxygen species levels and the repression of the antioxidant enzyme, catalase, played a critical role in the in vitro progression of benign papilloma cells to malignant carcinoma cells. Catalase message, protein levels, and activity levels were found to be downregulated in the malignantly progressed cells. The goal of this study is to further characterize the repression of catalase in malignant progression of mouse skin tumors. To validate the in vitro observations, we examined catalase expression in tumor samples generated by the multistep chemical carcinogenesis protocol. Higher levels of catalase mRNA and protein were observed in benign papillomas versus malignant carcinomas. Nuclear run-on analysis showed that catalase repression in the cultured malignant cells was transcription-dependent. Results from luciferase reporter assays indicated that malignant cells have lower catalase promoter activities than benign papilloma cells, in part through the Wilm’s tumor suppressor 1 (WT1) binding site within the proximal promoter region. The WT1 protein levels were found to be inversely correlated with the observed catalase promoter activities, with higher levels observed in the malignant cells versus the benign cells. These results led us to conclude that WT1 is acting as a transcription repressor in catalase gene regulation during tumor progression.

Kevin A. Kwei; Joanne S. Finch; Eric J. Thompson; G. Tim Bowden

2004-01-01

59

RESEARCH Open Access The Role of Catalase in Pulmonary Fibrosis  

E-print Network

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-b 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

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

60

Catalases are NAD(P)H-dependent tellurite reductases  

E-print Network

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 (TeO3 22) to the less toxic, insoluble metal, tellurium (Teu), in vitro. AnEscherichia 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

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

2006-01-01

61

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

2006-01-01

62

Catalases Are NAD(P)H-Dependent Tellurite Reductases  

PubMed Central

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 (TeO32?) to the less toxic, insoluble metal, tellurium (Te°), 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

Calderon, Ivan L.; Arenas, Felipe A.; Perez, Jose Manuel; Fuentes, Derie E.; Araya, Manuel A.; Saavedra, Claudia P.; Tantalean, Juan C.; Pichuantes, Sergio E.; Youderian, Philip A.; Vasquez, Claudio C.

2006-01-01

63

RESTORATION INDUCED BY CATALASE IN IRRADIATED MICROORGANISMS  

E-print Network

Working with the bacterial strain Escherichia coli K-12 which had been irradiated with heavy doses of ultraviolet light, Monod, Torriani, and Jolit (1949) have recently observed a new type of restoration phenomenon. Mter irradiation, the rate of survival, estimated by colony counts on agar plates, seemed to increase with the size of plating, that is with the number of cells plated, as though the dead bacteria contributed some restoring factor. This same factor was found in extracts from various organs of the rabbit. After preliminary investigation, these authors identified the restoring factor as catalase. Ferrous sulfate exerted a similar effect but to a lesser degree. In addition, the restoring action was heavily favored by the administration of some visible light, insufficient in itself for giving a notable restoration. This paper presents results on further development of this study. I

Latarjet; Luis Renato Caldas

64

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

65

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

66

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

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

Nanoceria exhibit redox state-dependent catalase mimetic activity†  

PubMed Central

In this study we have found that cerium oxide nanoparticles exhibit catalase mimetic activity. Surprisingly, the catalase mimetic activity correlates with a reduced level of cerium in the +3 state, in contrast to the relationship between surface charge and superoxide scavenging properties. PMID:20369166

Pirmohamed, Talib; Dowding, Janet M.; Singh, Sanjay; Wasserman, Brian; Heckert, Eric; Karakoti, Ajay S.; King, Jessica E. S.; Seal, Sudipta; Self, William T.

2011-01-01

69

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

70

A Eukaryote without Catalase-Containing Microbodies: Neurospora crassa Exhibits a Unique Cellular Distribution of Its Four Catalases†  

E-print Network

Microbodies usually house catalase to decompose hydrogen peroxide generated within the organelle by the action of various oxidases. Here we have analyzed whether peroxisomes (i.e., catalase-containing microbodies) exist in Neurospora crassa. Three distinct catalase isoforms were identified by native catalase activity gels under various peroxisome-inducing conditions. Subcellular fractionation by density gradient centrifugation revealed that most of the spectrophotometrically measured activity was present in the light upper fractions, with an additional small peak coinciding with the peak fractions of HEX-1, the marker protein for Woronin bodies, a compartment related to the microbody family. However, neither in-gel assays nor monospecific antibodies generated against the three purified catalases detected the enzymes in any dense organellar fraction. Furthermore, staining of an N. crassa wild-type strain with 3,3?-diaminobenzidine and H 2O 2 did not lead to catalasedependent reaction products within microbodies. Nonetheless, N. crassa does possess a gene (cat-4) whose product is most similar to the peroxisomal type of monofunctional catalases. This novel protein indeed exhibited catalase activity, but was not localized to microbodies either. We conclude that N. crassa lacks catalase-containing peroxisomes, a characteristic that is probably restricted to a few filamentous fungi that produce little hydrogen peroxide within microbodies. Microbodies are nearly ubiquitous organelles of the eukaryotic

Wolfgang Schliebs; Christian Würtz; Wolf-hubert Kunau; Marten Veenhuis; Hanspeter Rottensteiner

2006-01-01

71

Effects of Inhibitors of Catalase on Photosynthesis and on Catalase Activity in Unwashed Preparations of Intact Chloroplasts  

PubMed Central

The catalase activity of unwashed preparations containing intact spinach (Spinacia oleracea L.) chloroplasts is inhibited both by cyanide and by azide at concentrations which also cause inhibition of photosynthetic CO2- dependent O2 evolution. Aminotriazole can also be used to inhibit this contaminant catalase, and in this case inhibition of catalase can be achieved at aminotriazole concentrations which have little effect on the rate of photosynthetic CO2 fixation. Aminotriazole may be used as a specific inhibitor of catalase in order to demonstrate inhibition of photosynthesis by added H2O2. It is therefore concluded that inhibition of photosynthesis by cyanide and azide does not necessarily result from inhibition of catalase in the chloroplast preparation, and that intact chloroplasts do not produce inhibitory concentrations of H2O2 under the best experimental conditions for CO2 fixation. PMID:16660434

Allen, John F.; Whatley, F. R.

1978-01-01

72

Stability of catalase and its role in lipid oxidation in beef muscle  

E-print Network

or frozen conditions. In frozen storage, even freeze-thawing would not affect endogenous catalase. Washing, however, markedly lowers catalase activity. This indicates that catalase probably contributes significantly to the antioxidant process in uncooked...

Pradhan, Abhijeet Amar

2012-06-07

73

Investigating Catalase Activity Through Hydrogen Peroxide Decomposition by Bacteria Biofilms in Real Time Using Scanning  

E-print Network

Investigating Catalase Activity Through Hydrogen Peroxide Decomposition by Bacteria Biofilms University, Las Cruces, New Mexico 88003, United States *S Supporting Information ABSTRACT: Catalase activity electrochemical microscopy (SECM). The catalase activity, in units of micromoles hydrogen peroxide decomposed per

Nishiguchi, Michele

74

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

75

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

76

Identification of Two Catalases in Azotobacter vinelandii: a KatG Homologue and a Novel Bacterial Cytochrome c Catalase, CCCAv? †  

PubMed Central

Azotobacter vinelandii produces two detectable catalases during growth on minimal medium. The heat-labile catalase expressed during exponential growth phase was identified as a KatG homologue by liquid chromatography-tandem mass spectrometry (LC-MS/MS) using a mixed protein sample. The second catalase was heat resistant and had substantial residual activity after treatment at 90°C. This enzyme was purified by anion-exchange and size exclusion chromatography and was found to exhibit strong absorption at 407 nm, which is often indicative of associated heme moieties. The purified protein was fragmented by proteinase K and identified by LC-MS/MS. Some identity was shared with the MauG/bacterial cytochrome c peroxidase (BCCP) protein family, but the enzyme exhibited a strong catalase activity never before observed in this family. Because two putative c-type heme sites (CXXCH) were predicted in the peptide sequence and were demonstrated experimentally, the enzyme was designated a cytochrome c catalase (CCCAv). However, the local organization of the CCCAv heme motifs differed significantly from that of the BCCPs as the sites were confined to the C-terminal half of the catalase. A possible Ca2+ binding motif, previously described in the BCCPs, is also present in the CCCAv peptide sequence. Some instability in the presence of EGTA was observed. Expression of the catalase was abolished in cccA mutants, resulting in a nearly 8,700-fold reduction in peroxide resistance in stationary phase. PMID:18055590

Sandercock, James R.; Page, William J.

2008-01-01

77

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

2011-12-01

78

The catalase activity of diiron adenine deaminase  

PubMed Central

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 Mn2+ 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 FeSO4. 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, [FeII/FeII]-ADE catalyzed the conversion of H2O2 to O2 and H2O. The values of kcat and kcat/Km for the catalase activity are 200 s?1 and 2.4 × 104 M?1 s?1, respectively. [FeII/FeII]-ADE underwent more than 100 turnovers with H2O2 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 gave = 4.3 EPR signal and no evidence of anti-ferromagnetic spin-coupling. A model is proposed for the disproportionation of H2O2 by [FeII/FeII]-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

2011-01-01

79

Contribution of catalase to hydrogen peroxide resistance in Enterococcus faecalis.  

PubMed

Enterococcus faecalis exhibits high resistance to oxidative stress. Several enzymes are responsible for this trait. The role of alkyl hydroperoxide reductase (Ahp), thiol peroxidase (Tpx), and NADH peroxidase (Npr) in oxidative stress defense was recently characterized. Enterococcus faecalis, in contrast to many other streptococci, contains a catalase (KatA), but this enzyme can only be formed when the bacterium is supplied with heme. We have used this heme dependency of catalase activity and mutants deficient in KatA and Npr to investigate the role of the catalase in resistance against exogenous and endogenous hydrogen peroxide stress. The results demonstrate that in the presence of environmental heme catalase contributes to the protection against toxic effects of hydrogen peroxide. PMID:22486165

Baureder, Michael; Reimann, Ronny; Hederstedt, Lars

2012-06-01

80

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

81

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

82

Comparative study of catalase-peroxidases (KatGs)  

Microsoft Academic Search

Catalase-peroxidases or KatGs from seven different organisms, including Archaeoglobus fulgidus,Bacillus stearothermophilus, Burkholderia pseudomallei, Escherichia coli, Mycobacterium tuberculosis, Rhodobacter capsulatus and Synechocystis PCC 6803, have been characterized to provide a comparative picture of their respective properties. Collectively, the enzymes exhibit similar turnover rates with the catalase and peroxidase reactions varying between 4900 and 15,900s?1 and 8–25s?1, respectively. The seven enzymes also

Rahul Singh; Ben Wiseman; Taweewat Deemagarn; Vikash Jha; Jacek Switala; Peter C. Loewen

2008-01-01

83

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

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

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

2013-08-01

86

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

87

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

88

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

89

Inhibition of Activity of Catalase from Potato Tubers by Salicylic and Succinic Acids  

Microsoft Academic Search

It was found that salicylic acid inhibits the activity of catalase from potato tubers in vitro. Succinic acid suppressed catalase activity at the same concentrations that salicylate; however, its effect was more long-term. Bovine catalase was less sensitive to salicylic and succinic acids than potato catalase. In the past years, the attention of researchers has been attracted to studying the

Ya. S. Panina; N. I. Vasyukova; O. L. Ozeretskovskaya

2004-01-01

90

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

2011-03-15

91

CENTRAL REINFORCING EFFECTS OF ETHANOL ARE BLOCKED BY CATALASE INHIBITION  

PubMed Central

Recent studies have systematically indicated that newborn rats are highly sensitive to ethanol’s positive reinforcing effects. Central administrations of ethanol (25–200 mg %) 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 (i.c.) administrations of 100 mg% ethanol. Half of the animals corresponding to each learning condition were pretreated with i.c. 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 employed 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 Edward; Molina, Juan Carlos; Spear, Norman

2007-01-01

92

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

93

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

94

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

95

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. PMID:24170119

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

2013-01-01

96

Research article PURIFICATION OF CATALASE ENZYME FROM PLEUROTUS OSTREATUS  

E-print Network

ABSTRACT: The oyster mushroom Pleurotus ostreatus is the most commonly cultivated mushroom, and are effective for antitumor, antibacterial, anti viral and hematological agents and in immune modulating treatments. Several compounds from oyster mushrooms, potentially beneficial for human health have been isolated and studied. The aim of this research is to purify an enzyme catalase from Pleurotus ostreatus through Sephadox G-75 column, its molecular weight was determined by polyacrylamide gel electrophoresis and the catalase enzyme stability were observed at various temperature and different pH condition. Under denaturing conditions, polyacrylamide gel electrophoresis revealed dissociation of a major component of molecular weight 62,000 kDa, which constituted 90 % of the total protein of the stained gel, suggesting that the native enzyme is tetrameric. The optimum temperature and pH for the purified enzyme catalase from Pleurotus ostreatus enzymatic reaction were 30°C and pH 7.5.

unknown authors

97

RESEARCH ARTICLE Catalase enzyme in mitochondria of Saccharomyces cerevisiae  

E-print Network

Catalase and superoxide dismutase activities have been explored in the yeast Saccharomyces cerevisiae during batchwise growth experiment. During the diauxic growth in YPD medium high Ys values were obtained (0.415- 0.423) and correlation between the total activities of both enzymes has been found. A mitochondrial fraction from three type strains of Saccharomyces cerevisiae has been isolated. The purity of this fraction was proved through different enzyme assays: hexokinase, glucose-6-phosphate dehydrogenase, D-amino acid oxidase, isocitric lyase, succinate dehydrogenase. Then the catalase, peroxidase, Mn and Cu/Zn superoxide dismutase activities were evaluated in the mitochondrial fraction. Polyacrylamide gel electrophoresis separations allowed to identify a

Ventsislava Yankova Petrova; Tanya Vassileva Rasheva; Anna V. Kujumdzieva

2002-01-01

98

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

99

21 CFR 184.1034 - Catalase (bovine liver).  

Code of Federal Regulations, 2012 CFR

...CAS Reg. No. 81457-95-6) is an enzyme preparation obtained from extracts of...purified liquid or powder. Its characterizing enzyme activity is catalase (EC 1.11.1...requirements and additional requirements for enzyme preparations in the Food...

2012-04-01

100

21 CFR 184.1034 - Catalase (bovine liver).  

Code of Federal Regulations, 2011 CFR

...CAS Reg. No. 81457-95-6) is an enzyme preparation obtained from extracts of...purified liquid or powder. Its characterizing enzyme activity is catalase (EC 1.11.1...requirements and additional requirements for enzyme preparations in the Food...

2011-04-01

101

21 CFR 184.1034 - Catalase (bovine liver).  

Code of Federal Regulations, 2013 CFR

...CAS Reg. No. 81457-95-6) is an enzyme preparation obtained from extracts of...purified liquid or powder. Its characterizing enzyme activity is catalase (EC 1.11.1...requirements and additional requirements for enzyme preparations in the Food...

2013-04-01

102

21 CFR 184.1034 - Catalase (bovine liver).  

Code of Federal Regulations, 2010 CFR

...CAS Reg. No. 81457-95-6) is an enzyme preparation obtained from extracts of...purified liquid or powder. Its characterizing enzyme activity is catalase (EC 1.11.1...requirements and additional requirements for enzyme preparations in the Food...

2010-04-01

103

21 CFR 184.1034 - Catalase (bovine liver).  

...CAS Reg. No. 81457-95-6) is an enzyme preparation obtained from extracts of...purified liquid or powder. Its characterizing enzyme activity is catalase (EC 1.11.1...requirements and additional requirements for enzyme preparations in the Food...

2014-04-01

104

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

105

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

106

Graft Union Formation in Tomato Plants: Peroxidase and Catalase Involvement  

PubMed Central

• Background and Aims The use of grafted plants in vegetable crop production is now being expanded greatly. However, few data are available on the formation of graft unions in vegetables. In this work, the structural development of the graft union formation in tomato plants is studied, together with the possible relationship with activities of peroxidases and catalases. • Methods Tomato (Lycopersicon esculentum Mill.) seedlings of cultivar Fanny were grafted on the rootstock of cultivar AR?9704 using the ‘tongue approach grafting’ method, and were grown in a crop chamber. A study of the structural development of the graft union and the involvement of peroxidases and catalases in the process of graft formation was carried out during the first stages of the graft union (4, 8 and 15 d after grafting). • Key Results Observation of the structure of the graft union showed formation of xylem and phloem vessels through the graft union 8 d after grafting. In addition, root hydraulic conductance, L0, indicate that the graft union is fully functional 8 d after grafting, which coincided with an increase of peroxidase and catalase activities. • Conclusions These results suggest that increased peroxidase and catalase activities might be implicated in graft development in tomato plants. PMID:14630693

FERNÁNDEZ?GARCÍA, NIEVES; CARVAJAL, MICAELA; OLMOS, ENRIQUE

2004-01-01

107

A gasometric method to determine erythrocyte catalase activity  

Microsoft Academic Search

We describe a new gasometric method to determine erythrocyte catalase activity by the measurement of the volume of oxygen pro- duced as a result of hydrogen peroxide decomposition in a system where enzyme and substrate are separated in a special reaction test tube connected to a manometer and the reagents are mixed with a motor-driven stirrer. The position of the

A. J. S. Siqueira; J. O. Remião; A. M. P. Azevedo; C. R. J. Azambuja

1999-01-01

108

Plasma catalase activity and malondialdehyde level in patients with cataract  

Microsoft Academic Search

Purpose Oxidative mechanisms play a major role in the aetiology and pathogenesis of cataract, especially in age-related cataract. Our study aims to investigate systemic oxidant and antioxidant markers in cataract patients.Methods The activity of erythrocyte catalase and the level of malondialdehyde in plasma were measured in 40 patients with cataract and 60 healthy control subjects. The malondialdehyde level, as an

N A Ate?; Ö Yildirim; L Tamer; A Ünlü; B Ercan; N Mu?lu; A Kanik; R Hatungil; U Atik

2004-01-01

109

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

110

Catalase expression in delayed and premature aging mouse models  

Microsoft Academic Search

The physiological decline that occurs with aging is thought to result, in part, from accumulation of oxidative damage produced by reactive oxygen species (ROS) generated during normal metabolism. Two genetic mouse models of aging, the Ames dwarf and growth hormone (GH) transgenic, suggest that hormone levels may play a role in antioxidative defense and aging. To explore this possibility, catalase

Sharlene G. Rakoczy

2000-01-01

111

The plant host Brassica napus induces in the pathogen Verticillium longisporum the expression of functional catalase peroxidase which is required for the late phase of disease.  

PubMed

The devastating soilborne fungal pathogen Verticillium longisporum is host specific to members of the family Brassicaceae, including oilseed rape (Brassica napus) as the economically most important crop. The fungus infects through the roots and causes stunting and early senescence of susceptible host plants and a marked decrease in crop yield. We show here that V. longisporum reacts to the presence of B. napus xylem sap with the production of six distinct upregulated and eight downregulated proteins visualized by two-dimensional gel electrophoresis. Identification of 10 proteins by mass spectrometry revealed that all upregulated proteins are involved in oxidative stress response. The V. longisporum catalase peroxidase (VlCPEA) was the most upregulated protein and is encoded by two isogenes, VlcpeA-1 and VlcpeA-2. Both genes are 98% identical, corroborating the diploid or "amphihaploid" status of the fungus. Knock downs of both VlcpeA genes reduced protein expression by 80% and resulted in sensitivity against reactive oxygen species. Whereas saprophytic growth and the initial phase of the plant infection were phenotypically unaffected, the mutants were not able to perform the late phases of disease. We propose that the catalase peroxidase plays a role in protecting the fungus from the oxidative stress generated by the host plant at an advanced phase of the disease. PMID:22112218

Singh, Seema; Braus-Stromeyer, Susanna A; Timpner, Christian; Valerius, Oliver; von Tiedemann, Andreas; Karlovsky, Petr; Druebert, Christine; Polle, Andrea; Braus, Gerhard H

2012-04-01

112

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

113

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

114

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

115

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

116

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

117

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

118

Running Title: Pseudomonas pyocyanin inhibits epithelial cell catalase Address Correspondence To:  

E-print Network

Pyocyanin, produced by Pseudomonas aeruginosa, has many deleterious effects on human cells that relate to its ability to generate reactive oxygen species (ROS), such as superoxide and hydrogen peroxide. Human cells possess several mechanisms to protect themselves from ROS, including manganese superoxide dismutase (MnSOD), copper zinc superoxide dismutase (CuZnSOD), and catalase. Given the link between pyocyaninmediated epithelial cell injury and oxidative stress, we assessed pyocyanin’s affect on MnSOD, CuZnSOD, and catalase levels in the A549 human alveolar epithelial cell line and in normal human bronchial epithelial (NHBE) cells. In both cell types, CuZnSOD and MnSOD was unaltered, but over 24 h pyocyanin significantly decreased cellular catalase activity and protein content. Pyocyanin also decreased catalase mRNA. Overexpression of MnSOD in A549 cells prevented pyocyanin-mediated loss of catalase protein, but catalase activity still declined. Furthermore, pyocyanin decreased catalase activity, but not protein, in A549 cells overexpressing human catalase. These data suggest a direct effect of pyocyanin on catalase activity. Addition of pyocyanin to catalase in a cell-free system also decreased catalase activity. Mammalian catalase binds four

Yunxia Q. O’malley; Krzysztof J. Reszka; George T. Rasmussen; Maher Y; Gerene M. Denning; Bradley E. Britigan; Bradley E. Britigan

119

BIOLOGY OF HONEYBEE SPERMATOZOA. 3. EFFECT OF AMINO ACIDS AND CATALASE  

E-print Network

BIOLOGY OF HONEYBEE SPERMATOZOA. 3. EFFECT OF AMINO ACIDS AND CATALASE ON RESPIRATION AS MEASURED Catalase increased the rate of oxygen consumption of honeybee spermatozoa significantly, supporting the earlier view that these amino acids and catalase has beneficial effect on motility and survival

Paris-Sud XI, Université de

120

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

121

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

122

Plant Physiol. (1978) 61, 957-960 Effects of Inhibitors of Catalase on Photosynthesis and on  

E-print Network

Plant Physiol. (1978) 61, 957-960 Effects of Inhibitors of Catalase on Photosynthesis and on Catalase Activity in Unwashed Preparations of Intact Chloroplasts Received for publication October 6, 1977] 3RA, United Kingdom ABSTRACT The catalase activity ofunwashed preparations containing intact spinach

Allen, John F.

123

Structure of the Heme d of Penicillium vitale and Escherichia coli Catalases*  

E-print Network

Structure of the Heme d of Penicillium vitale and Escherichia coli Catalases* (Received-hydroxychlorin -spirolactone has been found in the crystal structures of Penicillium vitale catalase and Escherichia coli catalase hydroperoxidase II (HPII). The absolute stereochemistry of the two heme d chiral car- bon atoms

124

Catalase deciency drastically affects gene expression induced by high light in Arabidopsis thaliana  

E-print Network

Catalase de®ciency drastically affects gene expression induced by high light in Arabidopsis imbalances are managed at the production and scavenging levels. Because catalases are the major H2O2 and photorespiratory H2O2-induced cell death in transgenic catalase-de®cient Arabidopsis thaliana. These plants were

Gent, Universiteit

125

research papers 1972 Murshudov et al. Catalase Acta Cryst. (2002). D58, 19721982  

E-print Network

research papers 1972 Murshudov et al. Catalase Acta Cryst. (2002). D58, 1972±1982 Acta catalase, its ferryl intermediate (compound II) and NADPH complex Garib N. Murshudov,a * Albina I. Grebenko structure of the bacterial catalase from Micro- coccus lysodeikticus has been re®ned using the gene

126

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

127

Dihydrocapsaicin (DHC), a saturated structural analog of capsaicin, induces autophagy in human cancer cells in a catalase-regulated manner.  

PubMed

Although capsaicin, a pungent component of red pepper, is known to induce apoptosis in several types of cancer cells, the mechanisms underlying capsaicin-induced cytotoxicity are unclear. Here, we showed that dihydrocapsaicin (DHC), an analog of capsaicin, is a potential inducer of autophagy. DHC was more cytotoxic than capsaicin in HCT116, MCF-7 and WI38 cell lines. Capsaicin and DHC did not affect the sub-G(1) apoptotic peak, but induced G(0)/G(1) arrest in HCT116 and MCF-7 cells. DHC caused the artificial autophagosome marker GFP-LC3 to redistribute and upregulated expression of autophagy-related proteins. Blocking of autophagy by 3-methyladenine (3MA) as well as siRNA Atg5 induced a high level of caspase-3 activation. Although pretreatment with zVAD completely inhibited caspase-3 activation by 3MA, it did not prevent cell death. DHC-induced autophagy was enhanced by zVAD pretreatment, as shown by increased accumulation of LC3-II protein. DHC attenuated basal ROS levels through catalase induction; this effect was enhanced by antioxidants, which increased both LC3-II expression and caspase-3 activation. The catalase inhibitor 3-amino-1,2,4-triazole (3AT) abrogated DHC-induced expression of LC3-II, overexpression of the catalase gene increased expression of LC3-II protein, and knockdown decreased it. Additionally, DHC-induced autophagy was independent of p53 status. Collectively, DHC activates autophagy in a p53-independent manner and that may contribute to cytotoxicity of DHC. PMID:18818525

Oh, Seon Hee; Kim, Young Soon; Lim, Sung Chul; Hou, Yi Feng; Chang, In Youb; You, Ho Jin

2008-11-01

128

Two distinct groups of fungal catalase/peroxidases  

PubMed Central

Catalase/peroxidases (KatGs) are bifunctional haem b-containing (Class I) peroxidases with overwhelming catalase activity and substantial peroxidase activity with various one-electron donors. These unique oxidoreductases evolved in ancestral bacteria revealing a complex gene-duplicated structure. Besides being found in numerous bacteria of all phyla, katG genes were also detected in genomes of lower eukaryotes, most prominently of sac and club fungi. Phylogenetic analysis demonstrates the occurrence of two distinct groups of fungal KatGs that differ in localization, structural and functional properties. Analysis of lateral gene transfer of bacterial katGs into fungal genomes reveals that the most probable progenitor was a katG from a bacteroidetes predecessor. The putative physiological role(s) of both fungal KatG groups is discussed with respect to known structure–function relationships in bacterial KatGs and is related with the acquisition of (phyto)pathogenicity in fungi. PMID:19614592

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

2011-01-01

129

Catalases negatively regulate methyl jasmonate signaling in guard cells.  

PubMed

Methyl jasmonate (MeJA)-induced stomatal closure is accompanied by the accumulation of hydrogen peroxide (H?O?) in guard cells. In this study, we investigated the roles of catalases (CATs) in MeJA-induced stomatal closure using cat mutants cat2, cat3-1 and cat1 cat3, and the CAT inhibitor, 3-aminotriazole (AT). When assessed with 2',7'-dichlorodihydrofluorescein, the reduction of catalase activity by means of mutations and the inhibitor accumulated higher basal levels of H?O? in guard cells whereas they did not affect stomatal aperture in the absence of MeJA. In contrast, the cat mutations and the treatment with AT potentiated MeJA-induced stomatal closure and MeJA-induced H?O? production. These results indicate that CATs negatively regulate H?O? accumulation in guard cells and suggest that inducible H?O? production rather than constitutive elevation modulates stomatal apertures in Arabidopsis. PMID:22525681

Jannat, Rayhanur; Uraji, Misugi; Hossain, Mohammad Anowar; Islam, Mohammad Muzahidul; Nakamura, Yoshimasa; Mori, Izumi C; Murata, Yoshiyuki

2012-07-01

130

Identification of the peroxisomal targeting signal for cottonseed catalase.  

PubMed

Catalase is a ubiquitous peroxisomal matrix enzyme, yet the molecular targeting signal(s) for sorting it in plant cells has not been defined. The most common peroxisome targeting signal (PTS) is a C-terminal tripeptide composed of a conserved SKL motif (type 1 PTS). The PTS for cottonseed catalase (Ccat) was elucidated in this study from immunofluorescence microscopic analyses of tobacco BY-2 suspension cells serving as an in vivo import system. To distinguish biolistically introduced Ccat from endogenous tobacco catalase, Ccat was hemagglutinin (HA)epitope-tagged at its N-terminus. Bombardment with HA-Ccat resulted in the import of Ccat into glyoxysomes, the specialized type of peroxisome in BY-2 cells. The C-terminal tripeptide of Ccat, PSI, is necessary for import. Evidence for this were mislocalizations to the cytosol of PSI-truncated Ccat and AGV-substituted (for PSI) Ccat. PSI-COOH, however, was not sufficient to re-route chloramphenicol acetyltransferase (CAT) from the cytosol to glyoxysomes, whereas the Ccat tetrapeptide RPSI-COOH was sufficient. Surprisingly, substitution of K (common at the fourth position in other plant catalases) for the R (CAT-KPSI) decreased import efficiency. However, substitution of K did not affect import, when additional upstream residues in Ccat were included (e.g. CAT-NVKPSI). Other evidence for the importance of upstream residues comprised abolishment of Ccat import due to substitutions with non-conserved residues (e.g. -AGVNVRPSI for -SRLNVRPSI). These data indicate that Ccat is sorted to plant peroxisomes by a degenerate type 1 PTS (PSI-COOH) whose residues are functionally dependent on a strict context of adjacent C-terminal amino acid residues. PMID:9301084

Mullen, R T; Lee, M S; Trelease, R N

1997-08-01

131

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

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

Catalase activity, hydrogen peroxide content and thermotolerance of pepper leaves  

Microsoft Academic Search

Activated forms of oxygen, including hydrogen peroxide (H2O2), have been implicated in plant responses to stress. Catalases (CAT) and peroxidases are the primary enzymatic detoxifiers of H2O2 in most plant tissues. Pepper (Capsicum annuum L.) leaf disks floated on 0–100mM H2O2 solutions in the dark were not affected or showed minimal effects depending on the assay. Changes in electrolyte leakage

Jeffrey A Anderson

2002-01-01

134

Studies of stabilization of native catalase using additives  

Microsoft Academic Search

Native catalase preparations isolated from Bacillus Sp were formulated with different additives for storage stabilization and better performance at high temperature and pH. The additives studied were: polyethylene glycol, glycerol, BSA, casein, glutaraldehyde, n-butylamine, ethylenediamine, 1.6-diaminohexane, BSA\\/glutaraldehyde and casein\\/glutaraldehyde. The glycerol and glutaraldehyde showed the best performance for long-term storage at 30°C and neutral pH. No stabilization additives were effective

Silgia A. Costa; Tzanko Tzanova; Ana Filipa Carneiro; Andreas Paar; Georg M. Gübitz; Artur Cavaco-Paulo

2002-01-01

135

Are Catalase -844A/G Polymorphism and Activity Associated with Childhood Obesity?  

PubMed Central

Abstract Catalase (CAT) is a peroxisomal antioxidant enzyme that is up-regulated upon oxidative stress. Previous studies have found associations between some single nucleotide polymorphisms (SNPs) located in the CAT promoter region in a variety of metabolic diseases. This is the first study that analyzes the association between erythrocyte CAT activity and candidate CAT SNPs with childhood obesity. The association study showed a significant positive association of the promoter variant ?844A/G with childhood obesity and biomarkers of obesity such as weight, body mass index (BMI), BMI Z-Score, and adipocyte fatty acid-binding protein, along with a tendency toward significance with insulin resistance biomarkers. In addition, CAT erythrocyte activity was found to be significantly lower in obese children, and it was significantly correlated with obesity and insulin resistance biomarkers. No association was found between erythrocyte CAT activity and the SNP ?844A/G. However, further in vitro and in vivo studies are needed to fully understand the role of CAT activity and SNPs in the development of insulin resistance in the setting of obesity. We hypothesize that CAT plays a role in early metabolic complications of obesity. Antioxid. Redox Signal. 19, 1970–1975. PMID:23641975

Ruperez, Azahara I.; Olza, Josune; Gil-Campos, Mercedes; Leis, Rosaura; Mesa, Maria D.; Tojo, Rafael; Canete, Ramon; Gil, Angel

2013-01-01

136

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

137

Progeric effects of catalase inactivation in human cells.  

PubMed

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. PMID:18634817

Koepke, Jay I; Wood, Christopher S; Terlecky, Laura J; Walton, Paul A; Terlecky, Stanley R

2008-10-01

138

ROLES OF TWO INTERHELICAL INSERTIONS IN CATALASE-PEROXIDASE CATALYSIS: TRACING THE IMPACT OF PERIPHERAL PROTEIN STRUCTURES ON HEME ENZYME FUNCTION.  

E-print Network

??Monofunctional peroxidases and bifunctional catalase-peroxidases share almost superimposable active sites, yet peroxidases lack appreciable catalase activity. Moreover, catalase-peroxidases catalyze both catalase and peroxidase reactions with… (more)

LI, YONGJIANG

2005-01-01

139

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

140

Cloning and Genetic Characterization ofHelicobacter pylori Catalase and Construction of a Catalase-Deficient Mutant Strain  

Microsoft Academic Search

The N-terminal sequence of a protein, originally described as an adhesin ofHelicobacter pylori, was used in an oligonucleotide-based screening procedure of anH. pyloriplasmid library inEscherichia coli. Five indepen- dent plasmid clones were isolated, all mapping to the same chromosomal region and encoding the H. pylori catalase. The gene, designatedkatA, comprises 1,518 nucleotides and encodes a putative protein of 505 amino

STEFAN ODENBREIT; BJORN WIELAND; ANDRAINER HAAS

1996-01-01

141

Dierential developmental expression and cell type specicity of Dictyostelium catalases and their response to oxidative stress and  

E-print Network

Di¡erential developmental expression and cell type speci¢city of Dictyostelium catalases the Dictyostelium catalase and Cu/Zn superoxide dismutase antioxidant enzymes. We show that there are two catalase oxidative damage. We found that exposure to H2O2 does not result in the induction of the catalase

Devreotes, Peter

142

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

143

Neuroprotective effect of adenoviral catalase gene transfer in cortical neuronal cultures  

PubMed Central

Reduced availability of reactive oxygen species is a key component of neuroprotection against various toxic stimuli. Recently we showed that the hydrogen peroxide scavenger catalase plays a central role in delayed preconditioning induced by the mitochondrial ATP-sensitive potassium channel opener BMS-191095. The purpose of the experiments discussed here was to investigate the neuroprotective effect of catalase in vitro using a recombinant adenoviral catalase gene transfer protocol. To induce catalase overexpression, cultured rat cortical neurons were infected with the adenoviral vector Ad5CMVcatalase and control cells were incubated with Ad5CMVntLacZ for 24h. Gene transfer effectively increased catalase protein levels and activity, but did not influence other antioxidants tested. Ad5CMVcatalase, with up to 10 plaque forming units (pfu) per neuron, did not affect cell viability under control conditions and did not protect against glutamate excitotoxicity or oxygen-glucose deprivation. In contrast, catalase overexpression conferred a dose-dependent protection against exposure to hydrogen peroxide (viability: control, 33.02±1.09%; LacZ 10 pfu/cell, 32.85±1.51%; catalase 1 pfu/cell, 62.09±4.17%*; catalase 2 pfu/cell, 98.71±3.35%*; catalase 10 pfu/cell, 99.68±1.99%*; *p<0.05 vs. control; mean±SEM). Finally, the protection could be antagonized using the catalase inhibitor 3-aminotriazole. Our results support the view that enhancing cellular antioxidant capacity may play a crucial role in neuroprotective strategies. PMID:19302986

Gaspar, Tamas; Domoki, Ferenc; Lenti, Laura; Institoris, Adam; Snipes, James A; Bari, Ferenc; Busija, David W

2009-01-01

144

Inhibition of adhesion and proliferation of peritoneally disseminated tumor cells by pegylated catalase.  

PubMed

Hydrogen peroxide may aggravate the peritoneal dissemination of tumor cells by activating the expression of a variety of genes. In this study, we used pegylated catalase (PEG-catalase) to examine whether prolonged retention of catalase activity within the peritoneal cavity is effective in inhibiting peritoneal dissemination in mouse models. Murine B16-BL6 cells or colon 26 cells labeled with firefly luciferase gene were inoculated intraperitoneally into syngeneic mice. Compared with unmodified catalase, PEG-catalase was retained in the peritoneal cavity for a long period after intraperitoneal injection. A single injection of PEG-catalase just before tumor inoculation significantly reduced the number of the tumor cells at 1 and 7 days. The changes in the expression of molecules involved in the metastasis were evaluated by real time quantitative PCR analysis. Inoculation of the tumor cells increased the expression of intercellular adhesion molecule (ICAM)-1 in the greater omentum, which was inhibited by PEG-catalase. An injection of PEG-catalase at 3 days after tumor inoculation also reduced the number of the tumor cells, suggesting that processes other than the adhesion of tumor cells to peritoneal organs are also inhibited. Daily doses of PEG-catalase significantly prolonged the survival time of tumor-bearing mice. These results indicate that intraperitoneal injection of PEG-catalase inhibits the multiple processes of peritoneal dissemination of tumor cells by scavenging hydrogen peroxide in the peritoneal cavity. PMID:17086358

Hyoudou, Kenji; Nishikawa, Makiya; Kobayashi, Yuki; Kuramoto, Yukari; Yamashita, Fumiyoshi; Hashida, Mitsuru

2006-01-01

145

Crystallization and crystal packing of Proteus mirabilis PR catalase.  

PubMed

The tetrameric catalase from Proteus mirabilis PR (EC 1.11.1.6), known to bind NADPH, has been crystallized by the hanging-drop method in a form apparently depleted in dinucleotide. The crystals belong to the hexagonal space group P6(2)22 with a = b = 111.7 A, c = 248.8 A. There is one subunit in the asymmetric unit. Data were collected to 2.9 A at the L.U.R.E. (Orsay) synchrotron radiation facility. The tetramers have been located in the crystal, centered on the site (1/2, 0, 0) with 222 symmetry. PMID:1942042

Jouve, H M; Gouet, P; Boudjada, N; Buisson, G; Kahn, R; Duee, E

1991-10-20

146

Plating isolation of various catalase-negative microorganisms from soil  

NASA Technical Reports Server (NTRS)

A unique plating procedure was developed that allows isolation, but not enumeration, of representatives of the catalase-negative soil microflora. The numbers recovered, however, are low as compared to the numbers recovered when the modified dilution-to-extinction isolation procedure is used. The latter procedure provides prolonged inoculation in sealed tubes containing a nutritionally rich broth medium over small submerged agar slants. In contrast, the plating procedure utilizes nutritionally minimal media and the shorter incubations mandated by the inherent problems associated with plating.

Labeda, D. P.; Hunt, C. M.; Casida, L. E., Jr.

1974-01-01

147

Decoration and shadowing of freeze-etched catalase crystals.  

PubMed

Aqueous suspensions of catalase crystals were freeze-cleaved, deep-etched and either shadowed with Ta/W at 45 degrees or decorated with 0.1-0.9 nm thick deposits of Au and Pt at normal incidence. The electron micrographs of the decorated specimens were processed by correlation averaging and compared with a relief reconstruction obtained from shadowed specimens. Pronounced decoration was observed on the catalase crystals at temperatures between 130 and 180 K. Disregarding the difficulties in interpretation, the averages of 0.1-0.2 nm thick Au and Pt films reveal more structural detail than the relief reconstruction. Perfect shadowing provides information on surface topography and is relatively easy to comprehend; decoration renders variations in physico-chemical affinity visible. Problems of the interference of decoration and shadowing effects in the intuitive interpretation of freeze-etch replicas and in relief reconstruction are discussed as well as the disturbing effects of a non-ideal carbon backing. The perspectives of using decoration intentionally as a positive staining technique for the investigation of frozen-hydrated surfaces are evaluated and quality criteria are defined. PMID:2413603

Bachmann, L; Becker, R; Leupold, G; Barth, M; Guckenberger, R; Baumeister, W

1985-01-01

148

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

PubMed

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 electrophoresis and FPLC. The molecular weight and Stokes' radius of the purified enzyme were 339 kDa and 127 +/- 2 A. The enzyme had 11 sulfhydryl groups and 15 tryptophan groups per mol of the enzyme. A broad pH optimum in the range 5.2 to 7.8 was obtained. Sulfhydryl group binding agents, thiol reagents and N-Bromosuccinimide inhibited the enzyme activity. The kinetic data show no cooperativity between the substrate binding sites. Tryptophan, indole acetic acid, cysteine, formaldehyde and sodium azide inhibited the enzyme non-competitively with Ki values of 1.5, 1.6, 6.7, 0.55 and 0.0017 mM, respectively. PMID:8302290

Chatterjee, U; Sanwal, G G

1993-09-22

149

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

150

Adaptive response of antioxidant enzymes to catalase inhibition by aminotriazole in goldfish liver and kidney  

Microsoft Academic Search

This study was undertaken to clarify the physiological role of catalase in the maintenance of pro\\/antioxidant balance in goldfish tissues by inhibiting the enzyme in vivo with 3-amino 1,2,4-triazole. Intraperitoneal injection of aminotriazole (0.5 mg\\/g wet mass) caused a decrease in liver catalase activity by 83% after 24 h that was sustained after 168 h post-injection. In kidney catalase activity

Tetyana V. Bagnyukova; Kenneth B. Storey; Volodymyr I. Lushchak

2005-01-01

151

Methods for Determining the Rates of Catalase Synthesis and Destruction in vivo  

Microsoft Academic Search

ALTERATIONS in the amount of enzyme in a tissue can result from changes in the rate of synthesis or of destruction. The demonstration that 3-amino-1,2,4-triazole irreversibly inactivates catalase in the liver1 without interfering with its resynthesis2, and allyl-isopropyl acetamide blocks synthesis of new catalase3 suggested that these compounds might be used as tools for studying the kinetics of catalase synthesis

V. E. Price; M. Rechcigl; R. W. Hartley

1961-01-01

152

Determination of the activity of catalase using a europium(III)–tetracycline-derived fluorescent substrate  

Microsoft Academic Search

A one-step method is described for the fluorometric determination of the activity of the enzyme catalase (EC 1.11.1.6.), based on the finding that H2O2 in the europium (III)–tetracycline–hydrogen peroxide system is consumed by catalase. This is accompanied by a large decrease in both fluorescence intensity and decay time. The limit of detection (LOD; at S\\/N=3) for catalase at 30°C for

Meng Wu; Zhihong Lin; Otto S. Wolfbeis

2003-01-01

153

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

154

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

155

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

156

Action of Rennet on Casein as Influenced by Hydrogen Peroxide–Catalase Treatment[1] and [2  

Microsoft Academic Search

The effect of hydrogen peroxide-catalase treatment upon the release o£ glycomacro- peptide by rennet from casein in skimnfilk and caseinate-ultrafiltrate systems and on clotting time of these materials was inves- tigated. The hydrogen peroxide-catalase treat- ment of skimmilk and caseinate-ultrafiltrate systems retarded the release o£ glycomacro- peptide from K-casein by rennin. The peroxide-catalase treatment also reduced the rate and the

R. H. Schmidt; H. A. Morris; C. V. Morr

1969-01-01

157

Catalase deficiency renders remnant kidneys more susceptible to oxidant tissue injury and renal fibrosis in mice  

Microsoft Academic Search

Catalase deficiency renders remnant kidneys more susceptible to oxidant tissue injury and renal fibrosis in mice.BackgroundCatalase is one of the important antioxidant enzymes regulating the levels of intracellular hydrogen peroxide and hydroxyl radical. The effect of catalase deficiency on progressive renal fibrosis has not been fully elucidated.MethodsHomozygous acatalasemic mutant mice (C3H\\/AnLCsbCsb) and control wild-type mice (C3H\\/AnLCsaCsa) were subjected to 5\\/6

MIZUHO KOBAYASHI; HITOSHI SUGIYAMA; DA-HONG WANG; NAOMI TODA; YOHEI MAESHIMA; YASUSHI YAMASAKI; NORIYOSHI MASUOKA; MASAO YAMADA; SHOHEI KIRA; HIROFUMI MAKINO

2005-01-01

158

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

159

Stabilization of quaternary structure and activity of bovine liver catalase through encapsulation in liposomes  

Microsoft Academic Search

Bovine liver catalase was encapsulated in an aqueous phase of the phospholipid vesicle (liposome) to improve the stability of its tetrameric structure and activity. The catalase-containing liposomes (CALs) prepared were 30, 50 and 100nm in mean diameters (CAL30, CAL50 and CAL100, respectively). The CAL100 included the types I, II and III based on the amounts of catalase encapsulated. The CAL30,

Makoto Yoshimoto; Hideyuki Sakamoto; Noriko Yoshimoto; Ryoichi Kuboi; Katsumi Nakao

2007-01-01

160

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

161

Supramolecular assembly of ?-cyclodextrin-modified gold nanoparticles and Cu, Zn-superoxide dismutase on catalase  

Microsoft Academic Search

A bienzymatic supramolecular nanoassembly containing catalase and Cu, Zn-superoxide dismutase is reported. Catalase was hydrophobically modified with 1-adamantanecarboxylic acid and then immobilized on ?-cyclodextrin-coated gold nanospheres via supramolecular associations. The bienzymatic nanocatalyst was further prepared by co-immobilization of ?-cyclodextrin-modified superoxide dismutase. Supramolecularly immobilized catalase and superoxide dismutase retained 73 and 35%, respectively, of their initial specific activity. The range of

Reynaldo Villalonga; Roberto Cao; Alex Fragoso; Angelo E. Damiao; Pedro D. Ortiz; Julio Caballero

2005-01-01

162

Turnover of Catalase Heme and Apoprotein Moieties in Cotyledons of Sunflower Seedlings 1  

PubMed Central

The turnover of catalase apoprotein and catalase heme was studied in cotyledons of sunflower (Helianthus annuus L.) seedlings by density labeling of apoprotein and radioactive labeling of heme moieties. The heavy isotope (50% 2H2O) and the radioactive isotope ([14C]5-aminolevulinic acid) were applied either during growth in the dark (day 0-2.5) or in the light (day 2.5 and 5). Following isopycnic centrifugation of catalase purified from cotyledons of 5-day-old seedlings, superimposition curve fitting was used to determine the amounts of radioactive heme moieties in native and density-labeled catalase. Data from these determinations indicated that turnover of catalase heme and apoprotein essentially was coordinate. Only small amounts of heme groups were recycled into newly synthesized apoprotein during growth in the light, and no evidence was found for an exchange of heme groups in apoprotein moieties. It followed from these observations that degradation of catalase apoprotein was slightly faster than that of catalase heme. A degradation constant for catalase apoprotein of 0.263 per day was determined from the data on heme recycling and the degradation constant of catalase heme determined previously to be 0.205 per day (R Eising, B Gerhardt [1987] Plant Physiol 84: 225-232). PMID:16668566

Eising, Rainer; Suselbeck, Benno

1991-01-01

163

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

2014-01-01

164

Soluble epoxide hydrolase contamination of specific catalase preparations inhibits epoxyeicosatrienoic acid vasodilation of rat renal arterioles.  

PubMed

Cytochrome P-450 metabolites of arachidonic acid, the epoxyeicosatrienoic acids (EETs) and hydrogen peroxide (H(2)O(2)), are important signaling molecules in the kidney. In renal arteries, EETs cause vasodilation whereas H(2)O(2) causes vasoconstriction. To determine the physiological contribution of H(2)O(2), catalase is used to inactivate H(2)O(2). However, the consequence of catalase action on EET vascular activity has not been determined. In rat renal afferent arterioles, 14,15-EET caused concentration-related dilations that were inhibited by Sigma bovine liver (SBL) catalase (1,000 U/ml) but not Calbiochem bovine liver (CBL) catalase (1,000 U/ml). SBL catalase inhibition was reversed by the soluble epoxide hydrolase (sEH) inhibitor tAUCB (1 ?M). In 14,15-EET incubations, SBL catalase caused a concentration-related increase in a polar metabolite. Using mass spectrometry, the metabolite was identified as 14,15-dihydroxyeicosatrienoic acid (14,15-DHET), the inactive sEH metabolite. 14,15-EET hydrolysis was not altered by the catalase inhibitor 3-amino-1,2,4-triazole (3-ATZ; 10-50 mM), but was abolished by the sEH inhibitor BIRD-0826 (1-10 ?M). SBL catalase EET hydrolysis showed a regioisomer preference with greatest hydrolysis of 14,15-EET followed by 11,12-, 8,9- and 5,6-EET (V(max) = 0.54 ± 0.07, 0.23 ± 0.06, 0.18 ± 0.01 and 0.08 ± 0.02 ng DHET·U catalase(-1)·min(-1), respectively). Of five different catalase preparations assayed, EET hydrolysis was observed with two Sigma liver catalases. These preparations had low specific catalase activity and positive sEH expression. Mass spectrometric analysis of the SBL catalase identified peptide fragments matching bovine sEH. Collectively, these data indicate that catalase does not affect EET-mediated dilation of renal arterioles. However, some commercial catalase preparations are contaminated with sEH, and these contaminated preparations diminish the biological activity of H(2)O(2) and EETs. PMID:21753077

Gauthier, Kathryn M; Olson, Lauren; Harder, Adam; Isbell, Marilyn; Imig, John D; Gutterman, David D; Falck, J R; Campbell, William B

2011-10-01

165

Soluble epoxide hydrolase contamination of specific catalase preparations inhibits epoxyeicosatrienoic acid vasodilation of rat renal arterioles  

PubMed Central

Cytochrome P-450 metabolites of arachidonic acid, the epoxyeicosatrienoic acids (EETs) and hydrogen peroxide (H2O2), are important signaling molecules in the kidney. In renal arteries, EETs cause vasodilation whereas H2O2 causes vasoconstriction. To determine the physiological contribution of H2O2, catalase is used to inactivate H2O2. However, the consequence of catalase action on EET vascular activity has not been determined. In rat renal afferent arterioles, 14,15-EET caused concentration-related dilations that were inhibited by Sigma bovine liver (SBL) catalase (1,000 U/ml) but not Calbiochem bovine liver (CBL) catalase (1,000 U/ml). SBL catalase inhibition was reversed by the soluble epoxide hydrolase (sEH) inhibitor tAUCB (1 ?M). In 14,15-EET incubations, SBL catalase caused a concentration-related increase in a polar metabolite. Using mass spectrometry, the metabolite was identified as 14,15-dihydroxyeicosatrienoic acid (14,15-DHET), the inactive sEH metabolite. 14,15-EET hydrolysis was not altered by the catalase inhibitor 3-amino-1,2,4-triazole (3-ATZ; 10–50 mM), but was abolished by the sEH inhibitor BIRD-0826 (1–10 ?M). SBL catalase EET hydrolysis showed a regioisomer preference with greatest hydrolysis of 14,15-EET followed by 11,12-, 8,9- and 5,6-EET (Vmax = 0.54 ± 0.07, 0.23 ± 0.06, 0.18 ± 0.01 and 0.08 ± 0.02 ng DHET·U catalase?1·min?1, respectively). Of five different catalase preparations assayed, EET hydrolysis was observed with two Sigma liver catalases. These preparations had low specific catalase activity and positive sEH expression. Mass spectrometric analysis of the SBL catalase identified peptide fragments matching bovine sEH. Collectively, these data indicate that catalase does not affect EET-mediated dilation of renal arterioles. However, some commercial catalase preparations are contaminated with sEH, and these contaminated preparations diminish the biological activity of H2O2 and EETs. PMID:21753077

Olson, Lauren; Harder, Adam; Isbell, Marilyn; Imig, John D.; Gutterman, David D.; Falck, J. R.; Campbell, William B.

2011-01-01

166

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

167

Study of catalase adsorption on two mixed-mode ligands and the mechanism involved therein.  

PubMed

Mixed-mode chromatography sorbents n-hexylamine HyperCel™ (HEA) and phenylpropylamine HyperCel™ (PPA) were evaluated for the study of adsorption of catalase from two different sources. Various parameters such as buffer composition, ionic strength and pH were investigated to study the mechanism of interaction of commercially available pre-purified catalase from Bovine liver, purified catalase from black gram (Vigna mungo) and crude extract of black gram containing catalase with these mixed-mode ligands. A simple and economical screening protocol for identifying optimal buffer conditions for adsorption and desorption of catalase was established with micro volumes of the sorbent in batch mode. With HEA HyperCel, it was observed that pre-purified catalase from both bovine liver and black gram was completely retained at pH 7.0, irrespective of the presence or absence of NaCl in the adsorption buffer, whereas the catalase from crude extract of black gram was completely retained only in the presence of 0.2 M salt in the adsorption buffer. The elution of catalase from both the sources was accomplished by lowering the pH to 4.5 in absence of salt. In case of PPA HyperCel, catalase from both the sources was very strongly adsorbed under different buffer conditions studied, and elution did not yield a significant catalase activity. From the screening experiments, it could be concluded that the interaction of catalase with HEA HyperCel could be dominated by hydrophobic forces with minor contributions from ionic interaction and with PPA HyperCel, it could be a combination of different non-covalent interactions acting on different loci on the surface of the protein. PMID:23108613

Shiva Ranjini, S; Vijayalakshmi, M A

2012-11-01

168

The catalase-hydrogen peroxide system. Role of sub-units in the thermal deactivation of bacterial catalase in the absence of substrate  

PubMed Central

1. Kinetic studies of the thermal deactivation of bacterial catalase in the absence of substrate suggest that the reaction involves a protonation-induced reversible dissociation of catalase into catalatically inactive sub-units, followed by an irreversible transformation of the sub-units into deactivated products. It is possible that the sub-units are mono-haem species. The rate of deactivation decreases with increasing pressure in accordance with the predictions of the proposed model. 2. The results also imply that the addition of hydrogen peroxide substrate induces the re-formation of active catalase. Under appropriate conditions the activity of catalase is found to increase with time in a manner that is quantitatively consistent with the results of deactivation studies. PMID:5673527

Jones, Peter; Suggett, A.

1968-01-01

169

Study of catalase electrode for organic peroxides assays.  

PubMed

The catalytic activity of immobilized catalase (EC 1.11.1.6) for two model peroxide compounds (dibenzoyl peroxide and 3-chloroperoxibenzoic acid) in a non-aqueous medium was used to prepare an organic-phase enzyme electrode (OPEE). The enzyme was immobilized within a polymeric film on spectrographic graphite. The amperometric signal of the enzyme electrode in substrate solutions was found to be due to the reduction of oxygen generated in the enzyme layer. The electrode response is proportional to peroxide concentrations up to about 40 microM within the potential range from -450 to -650 mV (vs. Ag/AgCl), and the response time is at most 90 s. The enzyme electrode retains about 35% of its initial activity after a 3-week storage at room temperature. PMID:12414324

Horozova, Elena; Dimcheva, Nina; Jordanova, Zinaida

2002-12-01

170

EPR polarization studies on Mn catalase from Lactobacillus plantarum.  

PubMed

The binuclear manganese active site of Mn catalase catalyzes redox disproportionation of hydrogen peroxide, forming dioxygen and water. We report here multifrequency EPR and microwave polarization studies of the catalytically active homovalent Mn2+ complex of Lactobacillus plantarum Mn catalase, resolving spectra from each of the thermally accessible multiplet states of the coupled complex by multivariate methods. The experimental spectra have been simulated using computational approaches for the binuclear cluster to predict both intensity and polarization for arbitrary values of the ground state parameters. These two spectroscopic properties define the nature of the ground state wavefunctions and so serve as a sensitive and quantitative measure of the inter-ion interactions in the reduced complex. Interpretation of the spectra in terms of a pair Hamiltonian that includes Heisenberg exchange, dipolar, single site zero field splitting, and Zeeman perturbations leads to the most complete ground state description of the active site metal centers. The results of this spectroscopic analysis support a picture of two high spin ions weakly coupled by exchange interactions (J = 40 cm-1) with relatively small dipole-dipole coupling and single site zero field splittings for the ligand-free reduced enzyme. The coupling between fluoride binding and protonation of the complex has been demonstrated by proton uptake studies. The binding of two fluoride ions in the active site dramatically changes the pair spectra, reflecting a substantially reduced J-coupling (J = 10.5 cm-1) that must be a consequence of perturbation of the bridging ligands. Anion binding to the binuclear Mn complex appears to result in poisoning of the active site by protons, possibly associated with insertion of fluoride into bridging positions of the dimanganese core. PMID:8555195

Meier, A E; Whittaker, M M; Whittaker, J W

1996-01-01

171

Upregulation of imprinted genes in mice  

PubMed Central

Imprinted genes are expressed monoallelically because one of the two copies is silenced epigentically in a parent-of-origin pattern. This pattern of expression is controlled by differential marking of parental alleles by DNA methylation and chromatin modifications, including both suppressive and permissive histone acetylation and methylation. Suppressive histone modifications mark silenced alleles of imprinted genes, while permissive histone modifications mark the active alleles, suggesting the possibility that imprinted genes would show upregulation in gene expression. However, it is currently unknown whether imprinted genes show such upregulation. To address this question in mice, we estimated the intensity of expression of 59 genes relative to the rest of the genome by analyzing microarray data. Expression levels of 24 genes were validated using quantitative real-time PCR (qPCR). Expression of imprinted genes was found to be upreguled in various adult and embryonic mouse tissues. Consistent with their functions in growth and development, imprinted genes were found to be highly expressed in extraembryonic tissues and progressively upregulated during early embryonic development. In conclusion, upregulation of imprinted genes found in this study is similar to the dosage compensation (twofold upregulation) recently reported for X-linked genes. It has been proposed that the twofold upregulation of X-linked genes has been coupled with low transcriptional variation (noise) which could lead to deleterious effects on the organism. Results of this study suggest a general need for imprinted genes in the mouse to be upregulated to certain levels in order to avoid deleterious effects of variation in gene expression. PMID:20168089

Zaitoun, Ismail; Downs, Karen M.; Rosa, Guilherme J.M.; Khatib, Hasan

2011-01-01

172

Ascorbate activates soluble guanylate cyclase via H2O2-metabolism by catalase.  

PubMed

Conditions necessary for the activation by ascorbic acid of soluble guanylate cyclase purified from bovine lung have been examined. Ascorbic acid (0.1-10 mM) did not directly activate the enzyme, nonetheless, pronounced activation by ascorbate (3-10 mM) was observed in incubation mixtures containing 1 microM bovine liver catalase. Superoxide dismutase (SOD) and mannitol did not affect the catalase-dependent activation of guanylate cyclase elicited by ascorbate, suggesting that superoxide anion and hydroxyl radical were not mediating the activation of the enzyme. However, SOD enhanced the relatively low level activation of the enzyme elicited by catalase in the absence of added ascorbate. Pronounced inhibition (both with and without added ascorbate) was observed of catalase-dependent activation of guanylate cyclase by either ethanol (100 mM) or a fungal catalase preparation. Neither ethanol nor fungal catalase inhibited activation of guanylate cyclase by S-nitrosyl-N-acetyl-penicillamine (SNAP), a source of the nitric oxide free radical. These observations indicate that autoxidation of ascorbic acid or thiols present with the guanylate cyclase preparation leads to generation of H2O2, and its metabolism by bovine liver catalase mediates the concomitant activation of guanylate cyclase. The mechanism of activation appears to be associated with the presence of Compound I of catalase and to be inhibited by superoxide anion. PMID:2575561

Cherry, P D; Wolin, M S

1989-01-01

173

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

174

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

175

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

176

CATALASE AND SUPEROXIDE DISMUTASE OF ROOT-COLONIZING SAPROPHYTIC FLUORESCENT PSEUDOMONADS  

EPA Science Inventory

Root-colonizing, saprophytic fluorescent pseudomonads of the Pseudomonas putida-P. fluorescens group express similar levels of catalase and superoxide dismutase activities during growth on a sucrose- and amino acid-rich medium. ncreased specific activities of catalase but not sup...

177

Calcium Effects on Superoxide Dismutase and Catalase of the Rabbit Urinary Bladder Muscle and Mucosa  

Microsoft Academic Search

Purpose: Superoxide dismutase (SOD) and catalase are two important antioxidant mechanisms that work together to reduce free radical damage. Intracellular free calcium in smooth muscle can change rapidly and many enzymes can be affected. The sensitivity of SOD and catalase activity to calcium was determined in both rabbit bladder smooth muscle and mucosa. Materials and Methods: Calcium sensitivity was analyzed

Brittany Fitzpatrick; Catherine Schuler; Robert E. Leggett; Robert M. Levin

2012-01-01

178

Measurement of superoxide dismutase, catalase and glutathione peroxidase in cultured cells and tissue  

Microsoft Academic Search

Cells contain a large number of antioxidants to prevent or repair the damage caused by reactive oxygen species, as well as to regulate redox-sensitive signaling pathways. General protocols are described to measure the antioxidant enzyme activity of superoxide dismutase (SOD), catalase and glutathione peroxidase. The SODs convert superoxide radical into hydrogen peroxide and molecular oxygen, whereas the catalase and peroxidases

Christine J Weydert; Joseph J Cullen

2009-01-01

179

Spectrophotometric determination of hydrogen peroxide: catalase activity and rates of hydrogen peroxide removal by erythrocytes  

Microsoft Academic Search

A new method of hydrogen peroxide determination for the measurement of catalase activity and rates of hydrogen peroxide removal by erythrocytes was described. Hydrogen peroxide was determined by converting it to the indamine dye with a water-soluble ironporphyrin and measuring the absorbance at 590 nm. This method was applied to the assay of catalase in hemolysates from human, rat and

Noriyoshi Masuoka; Masahiro Wakimoto; Toshihiko Ubuka; Taku Nakano

1996-01-01

180

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

181

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

182

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

183

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...

184

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

185

Forchlorfenuron detection based on its inhibitory effect towards catalase immobilized on boron nitride substrate.  

PubMed

An enzymatic procedure based on a catalase biosensor for the detection of forchlorfenuron (CPPU) has been reported in this work. Catalase was immobilized on boron nitride (BN) sheets dispersed in chitosan by adsorption. The immobilized catalase exhibited direct electron transfer character and excellent electrocatalytic activity towards H2O2 reduction. After introducing CPPU into the H2O2 containing phosphate buffer solution, the catalase-catalyzed H2O2 reduction current decreased. By measuring the current decrease, CPPU can be determined in the range of 0.5-10.0µM with the detection limit of 0.07?M. The non-competitive inhibition behavior of CPPU towards catalase was verified by the Lineweaver-Burk plots. Long stability character has been ascribed to this biosensor. Possible use of this biosensor in flow systems is illustrated. The proposed biosensor has been successfully applied to CPPU determination in fruits samples with satisfactory results. PMID:25108110

Xu, Qin; Cai, Lijuan; Zhao, Huijie; Tang, Jiaqian; Shen, Yuanyuan; Hu, Xiaoya; Zeng, Haibo

2015-01-15

186

Cloning and Sequencing of a Candida albicans Catalase Gene and Effects of Disruption of This Gene†  

PubMed Central

Catalase plays a key role as an antioxidant, protecting aerobic organisms from the toxic effects of hydrogen peroxide, and in some cases has been postulated to be a virulence factor. To help elucidate the function of catalase in Candida albicans, a single C. albicans-derived catalase gene, designated CAT1, was isolated and cloned. Degenerate PCR primers based on highly conserved areas of other fungal catalase genes were used to amplify a 411-bp product from genomic DNA of C. albicans ATCC 10261. By using this product as a probe, catalase clones were isolated from genomic libraries of C. albicans. Nucleotide sequence analysis revealed an open reading frame encoding a protein of 487 amino acid residues. Construction of a CAT1-deficient mutant was achieved by using the Ura-blaster technique for sequential disruption of multiple alleles by integrative transformation using URA3 as a selectable marker. Resulting mutants exhibited normal morphology and comparable growth rates of both yeast and mycelial forms. Enzymatic analysis revealed an abundance of catalase in the wild-type strain but decreasing catalase activity in heterozygous mutants and no detectable catalase in a homozygous null mutant. In vitro assays showed the mutant strains to be more sensitive to damage by both neutrophils and concentrations of exogenous peroxide that were sublethal for the parental strain. Compared to the parental strain, the homozygous null mutant strain was far less virulent for mice in an intravenous infection model of disseminated candidiasis. Definitive linkage of CAT1 with virulence would require restoration of activity by reintroduction of the gene into mutants. However, initial results in mice, taken together with the enhanced susceptibility of catalase-deficient hyphae to damage by human neutrophils, suggest that catalase may enhance the pathogenicity of C. albicans. PMID:9573075

Wysong, Deborah R.; Christin, Laurent; Sugar, Alan M.; Robbins, Phillips W.; Diamond, Richard D.

1998-01-01

187

Catalase depression in malignant liver from chickens with myeloblastosis and Marek's disease  

E-print Network

Summary In rapidly frozen livers from chickens affected with myeloblastosis and Marek's disease and from unaffected control birds there exists a strong correlation between catalase activity and catalase Electron Paramagnetic Resonance (EPR) signal intensities. The diseased chickens had activities and signals reduced to as little as 10 % of control values. There were no changes in the EPR parameters in diseased liver and the data support the hypothesis that the lowering in activity is due to lowered catalase levels rather than to catalase inhibition. The rate of transformation of catalase to catalase-formate in liver was studied by freezeclamping liver in anaesthetised chickens, then warming to 370 for 1 or 2 minutes anaerobiosis, and then refreezing. The only difference of significance in this transformation between diseased and normal livers was the greater percentage of total catalase present as catalase-formate (, + 15%) in aerobic diseased liver, which may indicate a lowered production of hydrogen peroxide, relative to formate, in these livers. The rate of transformation was far faster in chickens (t- catalase activity in the livers of animals bearing malignant tumours was significantly lower than normal (Blumenthal & Brahn, 1910), an observation which was one of the first demonstrations of a systematic biochemical alteration produced by malignancy. This result has been substantiated and extended in a very large number of studies, which have been reviewed (Busch, 1962; Greenstein, 1954; Kampschmidt, 1965). It has been proposed that the deficiency in catalase activity is due to the effects of products of neoplastic metabolism which either directly inhibit the enzyme (Hargreaves & Deutsch, 1952; Hargreaves et al., 1959) or which lower its level, perhaps by repressing its synthesis (Ceriotti et al.,

D. L. Williams-smith; L. N. Payne; S. J. Wyard

188

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

2013-10-01

189

Characterization of a leaf-type catalase and its enzymatic regulation in sweet potato (Ipomoea batatas (L.)).  

E-print Network

??A major sweet potato leaf-type catalase was detected and identified from fullyexpandedmature leaves using in-gel activity staining assay with native- andSDS-PAGEs. The putative catalase activity… (more)

AFIYANTI, MUFIDAH

2011-01-01

190

Mitochondrial targeted catalase suppresses invasive breast cancer in mice  

PubMed Central

Background Treatment of invasive breast cancer has an alarmingly high rate of failure because effective targets have not been identified. One potential target is mitochondrial generated reactive oxygen species (ROS) because ROS production has been associated with changes in substrate metabolism and lower concentration of anti-oxidant enzymes in tumor and stromal cells and increased metastatic potential. Methods Transgenic mice expressing a human catalase gene (mCAT) were crossed with MMTV-PyMT transgenic mice that develop metastatic breast cancer. All mice (33 mCAT positive and 23 mCAT negative) were terminated at 110 days of age, when tumors were well advanced. Tumors were histologically assessed for invasiveness, proliferation and metastatic foci in the lungs. ROS levels and activation status of p38 MAPK were determined. Results PyMT mice expressing mCAT had a 12.5 per cent incidence of high histological grade primary tumor invasiveness compared to a 62.5 per cent incidence in PyMT mice without mCAT. The histological grade correlated with incidence of metastasis with 56 per cent of PyMT mice positive for mCAT showing evidence of pulmonary metastasis compared to 85.4 per cent of PyMT mice negative for mCAT with pulmonary metastasis (p ? 0.05). PyMT tumor cells expressing mCAT had lower ROS levels and were more resistant to hydrogen peroxide-induced oxidative stress than wild type tumor cells, suggesting that mCAT has the potential of quenching intracellular ROS and subsequent invasive behavior. The metastatic tumor burden in PyMT mice expressing mCAT was 0.1 mm2/cm2 of lung tissue compared with 1.3 mm2/cm2 of lung tissue in PyMT mice expressing the wild type allele (p ? 0.01), indicating that mCAT could play a role in mitigating metastatic tumor progression at a distant organ site. Expression of mCAT in the lungs increased resistance to hydrogen peroxide-induced oxidative stress that was associated with decreased activation of p38MAPK suggesting ROS signaling is dependent on p38MAPK for at least some of its downstream effects. Conclusion Targeting catalase within mitochondria of tumor cells and tumor stromal cells suppresses ROS-driven tumor progression and metastasis. Therefore, increasing the antioxidant capacity of the mitochondrial compartment could be a rational therapeutic approach for invasive breast cancer. Please see related commentary article: http://www.biomedcentral.com/1741-7015/9/62 PMID:21605372

2011-01-01

191

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

192

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

193

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

194

Volume84, number 2 FEBS LETTERS December 1977 EFFECTS OF WASHING AND OSMOTIC SHOCK ON CATALASE ACTIVITY OF INTACT  

E-print Network

Volume84, number 2 FEBS LETTERS December 1977 EFFECTS OF WASHING AND OSMOTIC SHOCK ON CATALASE] ). Since catalase causes release of oxygen from hydrogen peroxide, an enhancement of net oxygen evolution on addition of catalase to illuminated chloroplasts indicates that photosynthetic reduction of oxygen has

Allen, John F.

195

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

196

Vector-mediated overexpression of catalase A in the yeast Saccharomyces cerevisiae induces inclusion body formation.  

PubMed

To study the morphological effects of overexpression of catalase A in yeast, the gene coding for catalase A was introduced into Saccharomyces cerevisiae on a multicopy vector. After induction of microbody biogenesis and catalase A expression by growth on oleic acid as sole carbon source, cells were analyzed by immunofluorescence and immunoelectron microscopy. In addition, overexpression of catalase A was studied by quantitative immunoblotting and by activity measurement. Quantitative immunoblotting resulted in a 16-fold difference between immunoreactive material from transformed and non-transformed cells. An 18-fold increase of enzyme activity was measured in transformed cells due to overexpression of catalase A from plasmid pAH521. Immunofluorescent staining of semithin sections of Lowicryl HM20-embedded cells with anti-catalase localized peroxisomes and--at a low percentage--larger particles. By immunoelectron microscopy, these larger structures could be identified as agranular, electron-dense aggregates which are morphologically clearly distinct from the cytoplasm and not bounded by a membrane. These structures, which have been named inclusion bodies, contain catalase A but not other peroxisomal enzymes like thiolase. These findings suggest that cells are capable of compensating for overproduced proteins by formation of particular types of structures. PMID:1679011

Binder, M; Schanz, M; Hartig, A

1991-04-01

197

Catalase is a key enzyme in seed recovery from ageing during priming.  

PubMed

Ageing induces seed deterioration expressed as the loss of seed vigour and/or viability. Priming treatment, which consists in soaking of seeds in a solution of low water potential, has been shown to reinvigorate aged seeds. We investigate the importance of catalase in oxidation protection during accelerated ageing and repair during subsequent priming treatment of sunflower (Helianthus annuus L.) seeds. Seeds equilibrated to 0.29g H2Og(-1) dry matter (DM) were aged at 35°C for different durations and then primed by incubation for 7 days at 15°C in a solution of polyethylene glycol 8000 at -2MPa. Accelerated ageing affected seed germination and priming treatment reversed partially the ageing effect. The inhibition of catalase by the addition of aminotriazol during priming treatment reduced seed repair indicating that catalase plays a key role in protection and repair systems during ageing. Ageing was associated with H2O2 accumulation as showed by biochemical quantification and CeCl3 staining. Catalase was reduced at the level of gene expression, protein content and affinity. Interestingly, priming induced catalase synthesis by activating expression and translation of the enzyme. Immunocytolocalization of catalase showed that the enzyme co-localized with H2O2 in the cytosol. These results clearly indicate that priming induce the synthesis of catalase which is involved in seed recovery during priming. PMID:21763542

Kibinza, Serge; Bazin, Jérémie; Bailly, Christophe; Farrant, Jill M; Corbineau, Françoise; El-Maarouf-Bouteau, Hayat

2011-09-01

198

Catalase gene is associated with facial eczema disease resistance in sheep.  

PubMed

Facial eczema (FE) is a hepatogenous photosensitization disease of ruminant animals, particularly in sheep which vary widely in their susceptibility to the disease. The liver damage is caused by the mycotoxin, sporidesmin. There is evidence that the toxicity of sporidesmin is due to its ability to generate 'active oxygen' species. We evaluated the catalase gene, which encodes an enzyme with antioxidant functions, as a candidate for determining the susceptibility of sheep to the disease. Two microsatellite markers, OarSHP3 and OarSHP4, which flank the sheep catalase gene, were isolated from a Yeast Artificial Chromosome (YAC) clone. These markers mapped the catalase locus by linkage to ovine chromosome 15. Eleven informative markers spaced throughout chromosome 15, inclusive of the catalase marker OarSHP4, gave no significant linkage with the disease traits when analysed in four outcross resource pedigrees. However, OarSHP3 and OarSHP4 allele frequencies showed significant differences between FE resistant and susceptible selection-lines. Comparison of sequences of catalase cDNAs from sheep of resistant and susceptible lines showed only two silent mutations. A single nucleotide polymorphisms (KP1) in exon 6 of the catalase gene also showed significant differences in allele frequencies between the selection lines. The lack of evidence for linkage in outcross pedigrees, but the significant association in the genetic lines, implies that catalase is involved in determining the susceptibility of sheep to facial eczema, and that the candidate gene's effect is probably recessive or minor. PMID:10467703

Phua, S H; Dodds, K G; Morris, C A; Paterson, K A; McEwan, J C; Garmonsway, H G; Towers, N R; Crawford, A M

1999-08-01

199

Pex5p imports folded tetrameric catalase by interaction with Pex13p.  

PubMed

Human catalase forms a 240-kDa tetrameric complex and degrades H(2) O(2) in peroxisomes. Human catalase is targeted to peroxisomes by the interaction of its peroxisomal targeting signal type 1 (PTS1)-like KANL sequence with the cytosolic PTS1 receptor Pex5p. We show herein that human catalase tetramers are formed in the cytoplasm and that the expression of a PTS signal on each of the four subunits is not necessary for peroxisomal transport. We previously demonstrated that a Pex5p mutant defective in binding to Pex13p, designated Pex5p(Mut234), imports typical PTS1-type proteins but not catalase. This impaired catalase import is not rescued by replacing its C-terminal KANL sequence with a typical PTS1 sequence, SKL, indicating that the failure of catalase import in Mut234-expressing cells is not due to its weak PTS1. In contrast, several enzymatically inactive and monomeric mutants of catalase are efficiently imported in Mut234-expressing cells. Moreover, trimeric chloramphenicol acetyltransferase (CAT) harboring SKL is not imported in Pex5p(Mut234)-expressing cells, but CAT-SKL trimers are transported to peroxisomes in the wild-type cells. These findings suggest that the Pex5p-Pex13p interaction likely plays a pivotal role in the peroxisomal import of folded and oligomeric proteins. PMID:22747494

Otera, Hidenori; Fujiki, Yukio

2012-10-01

200

Improvement of insulin resistance by removal of systemic hydrogen peroxide by PEGylated catalase in obese mice.  

PubMed

Insulin resistance, a condition in which insulin action is impaired, is one of the characteristic features of type 2 diabetes. Excessive amounts of reactive oxygen species (ROS) interfere with the insulin signaling pathway, which leads to the progression of insulin resistance. To examine whether removal of systemic hydrogen peroxide is effective in improving insulin resistance, polyethylene glycol-conjugated catalase (PEG-catalase), a derivative with a long circulation half-life, was repeatedly injected into leptin-deficient ob/ob or high fat diet-induced obese mice for 16 or 10 consecutive weeks, respectively. Although ob/ob mice gradually gained weight with time irrespective of the treatment, repeated intraperitoneal injections of PEG-catalase significantly reduced glucose levels in the fed state. Glucose and insulin tolerance tests also showed PEG-catalase significantly improved glucose tolerance and insulin sensitivity in ob/ob mice, respectively. Similar but less marked results were obtained in the diet-induced obese mice. Treatment of 3T3-L1 adipocytes with glucose oxidase (GO) increased lipid hydroperoxide formation and reduced insulin-stimulated Akt phosphorylation. Addition of catalase or PEG-catalase significantly inhibited the GO-induced changes in adipocytes. These findings indicate that systemic removal of hydrogen peroxide by PEG-catalase activates the insulin signaling pathway and improves insulin resistance in obese mice. PMID:21033698

Ikemura, Mai; Nishikawa, Makiya; Hyoudou, Kenji; Kobayashi, Yuki; Yamashita, Fumiyoshi; Hashida, Mitsuru

2010-12-01

201

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

2013-04-01

202

The regulation of catalase activity by PPAR ? is affected by ?-synuclein  

PubMed Central

Objective While evidence for oxidative injury is frequently detected in brains of humans affected by Parkinson's disease (PD) and in relevant animal models, there is uncertainty regarding its cause. We tested the potential role of catalase in the oxidative injury that characterizes PD. Methods Utilizing brains of A53T ?-Syn and ntg mice, and cultured cells, we analyzed catalase activity and expression, and performed biochemical analyses of peroxisomal metabolites. Results Lower catalase expression and lower activity levels were detected in A53T ?-Syn brains and ?-Syn-expressing cells. The effect on catalase activity was independent of disease progression, represented by mouse age and ?-Syn mutation, suggesting a potential physiological function for ?-Syn. Notably, catalase activity and expression were unaffected in brains of mice modeling Alzheimer's disease. Moreover, we found that ?-Syn expression downregulate the peroxisome proliferator-activated receptor (PPAR)?, which controls catalase transcription. Importantly, activation of either PPAR?2, PPAR? or retinoic X receptor eliminated the inhibiting effect of ?-Syn on catalase activity. In addition, activation of these nuclear receptors enhanced the accumulation of soluble ?-Syn oligomers, resulting in a positive association between the degree of soluble ?-Syn oligomers and catalase activity. Of note, a comprehensive biochemical analysis of specific peroxisomal metabolites indicated no signs of dysfunction in specific peroxisomal activities in brains of A53T ?-Syn mice. Interpretation Our results suggest that ?-Syn expression may interfere with the complex and overlapping network of nuclear receptors transcription activation. In result, catalase activity is affected through mechanisms involved in the regulation of soluble ?-Syn oligomers. PMID:25356396

Yakunin, Eugenia; Kisos, Haya; Kulik, Willem; Grigoletto, Jessica; Wanders, Ronald J A; Sharon, Ronit

2014-01-01

203

Effects of pergolide mesylate on transduction efficiency of PEP-1-catalase protein  

SciTech Connect

Research highlights: {yields} We studied effects of pergolide mesylate (PM) on in vitro and in vivo transduction of PEP-1-catalase. {yields} PEP-1-catatase inhibited 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced inflammation. {yields} PM enhanced the transduction of PEP-1-catalase into HaCaT cells and skin tissue. {yields} PM increased anti-inflammatory activity of PEP-1-catalase. {yields} PM stimulated therapeutic action of anti-oxidant enzyme catalase in oxidative-related diseases. -- Abstract: The low transduction efficiency of various proteins is an obstacle to their therapeutic application. However, protein transduction domains (PTDs) are well-known for a highly effective tool for exogenous protein delivery to cells. We examined the effects of pergolide mesylate (PM) on the transduction of PEP-1-catalase into HaCaT human keratinocytes and mice skin and on the anti-inflammatory activity of PEP-1-catatase against 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced inflammation using Western blot and histological analysis. PM enhanced the time- and dose-dependent transduction of PEP-1-catalase into HaCaT cells without affecting the cellular toxicity. In a mouse edema model, PEP-1-catalase inhibited the increased expressions of inflammatory mediators and cytokines such as cyclooxygenase-2, inducible nitric oxide synthase, interleukin-6 and -1{beta}, and tumor necrosis factor-{alpha} induced by TPA. On the other hand, PM alone failed to exert any significant anti-inflammatory effects. However, the anti-inflammatory effect of co-treatment with PEP-1-catalase and PM was more potent than that of PEP-1-catalase alone. Our results indicate that PM may enhance the delivery of PTDs fusion therapeutic proteins to target cells and tissues and has potential to increase their therapeutic effects of such drugs against various diseases.

Sohn, Eun Jeong; Kim, Dae Won; Kim, Young Nam; Kim, So Mi [Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chunchon 200-702 (Korea, Republic of)] [Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chunchon 200-702 (Korea, Republic of); Lim, Soon Sung [Department of Food Science and Nutrition and RIC Center, Hallym University, Chunchon 200-702 (Korea, Republic of)] [Department of Food Science and Nutrition and RIC Center, Hallym University, Chunchon 200-702 (Korea, Republic of); Kang, Tae-Cheon [Department of Anatomy and Neurobiology, College of Medicine, Hallym University, Chunchon 200-702 (Korea, Republic of)] [Department of Anatomy and Neurobiology, College of Medicine, Hallym University, Chunchon 200-702 (Korea, Republic of); Kwon, Hyeok Yil [Department of Physiology, College of Medicine, Hallym University, Chunchon 200-702 (Korea, Republic of)] [Department of Physiology, College of Medicine, Hallym University, Chunchon 200-702 (Korea, Republic of); Kim, Duk-Soo [Department of Anatomy, College of Medicine, Soonchunhyang University, Cheonan-Si 330-090 (Korea, Republic of)] [Department of Anatomy, College of Medicine, Soonchunhyang University, Cheonan-Si 330-090 (Korea, Republic of); Cho, Sung-Woo [Department of Biochemistry and Molecular Biology, University of Ulsan College of Medicine, Seoul 138-736 (Korea, Republic of)] [Department of Biochemistry and Molecular Biology, University of Ulsan College of Medicine, Seoul 138-736 (Korea, Republic of); Han, Kyu Hyung; Park, Jinseu; Eum, Won Sik [Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chunchon 200-702 (Korea, Republic of)] [Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chunchon 200-702 (Korea, Republic of); Hwang, Hyun Sook, E-mail: wazzup@hallym.ac.kr [Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chunchon 200-702 (Korea, Republic of); Choi, Soo Young, E-mail: sychoi@hallym.ac.kr [Department of Biomedical Science and Research Institute of Bioscience and Biotechnology, Hallym University, Chunchon 200-702 (Korea, Republic of)

2011-03-18

204

Physicochemical peculiarities of iron porphyrin-containing electrodes in catalase- and peroxidase-type biomimetic sensors  

NASA Astrophysics Data System (ADS)

New catalase- and peroxidase-type iron porphyrin biomimetic electrodes have been developed for determining ultralow concentrations of H2O2 and C2H5OH in aqueous solutions. Their physicochemical features have been studied. A mechanism of catalase and peroxidase reactions was suggested. Biomimetic electrodes did not lose their activity for a long time under the action of the oxidant, intermediates, and the final products of the decomposition of H2O2. Potentiometric biomimetic sensors of catalase and peroxidase types have been designed and studied.

Sardarly, N. A.; Nagiev, T. M.

2009-08-01

205

704 THE EFFECT OF SARCOMA 37 ON THE INTRACELLULAR DISTRIBUTION OF MOUSE LIVER CATALASE From the  

E-print Network

MUCH work has been published on the effect on liver catalase of tumour growth, and of the injection of whole or semi-purified tumour homogenates, but in all these studies the sole criterion of activity has been a simple depression in catalase level. An increasingly large number of substances apparently unrelated to tumour tissue, have been shown to depress liver catalase activity on injection, e.g. methyl bis (B-chlorethyl) amine, 9: 10-dimethyl-1: 2-benzanthracene, butter yellow and its 3'methyl demative, 4'-amino-2: 3-dimethylaminoazobenzene, B-naphthylamine, benzpyrene (Adams and Roe, 1953), homogenised normal spleen

D. H. Adams

1959-01-01

206

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

207

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

2008-08-01

208

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. 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.; Mader, Marylou; Lazar, Jozef; Lazarova, Zelmira

2012-01-01

209

Evaluation of a catalase-based method for estimating the shelf-life of pasteurized whole milk  

E-print Network

for Detecting Mastitic Milk The presence of large quantities of catalase in milk has been the basis of many screening tests for estimating the extent of mastitic infection in the mammary glands of dairy cattle. The catalase test is probably the most 13...). Results from these procedures are based on the measurement of oxygen released from H202 by reaction with catalase. Paape et al. (32) determined a strong correlation (P&0. 01) between catalase test scores and total somatic cell counts. Catalase scores...

Dill, Susan Lee

2012-06-07

210

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

211

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

212

Catalase Activity of Mouse Liver and its Relation to the Condition of the Animal  

Microsoft Academic Search

IN papers dealing with methods of determining catalase activity in animal tissue, while dealing with the experimental conditions, usually little attention is paid to the condition of the animal. We have found the latter to be of utmost importance.

K. G. van Senden; J. de Jong

1960-01-01

213

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

214

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

Microsoft Academic Search

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\\u000a heme and has a molecular weight of 320 kDa with four 80 kDa subunits and an isoelectric point of 5.0. Catalase and phenol\\u000a oxidase activities were most

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

2008-01-01

215

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

216

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

217

Protective action of midgut catalase in lepidopteran larvae against oxidative plant defenses  

Microsoft Academic Search

Catalase activity was detected in the midgut tissues and regurgitate of several lepidopteran pests of the tomato plant. Greatest activity in the midgut was detected in larvalHelicoverpa zea, followed bySpodoptera exigua, Manduca sexta, andHeliothis virescens. We present evidence that catalase, in addition to removing toxic hydrogen peroxide, may inhibit the oxidation of plant phenolics mediated by plant peroxidases. Small amounts

Gary W. Felton; Sean S. Duffey

1991-01-01

218

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

219

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

220

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

221

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

222

Thermal Stability of Catalases Active in Dormant Saffron ( Crocus Sativus L. ) Corms  

Microsoft Academic Search

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°C, 45°C and 60°C, respectively, as given by Arrhenius plots. When stained for catalase activity gel electropherograms of extract revealed 3

J. Keyhani; E. Keyhani; J. Kamali

2002-01-01

223

Voltammetric study of the antioxidant properties of catalase and superoxide dismutase  

Microsoft Academic Search

The antioxidant properties of catalase and superoxide dismutase (SOD) have been studied by voltammetry. The effect of pH on\\u000a the antioxidant properties of catalase and SOD has been evaluated. It is established that the antioxidant activity of both\\u000a enzymes is maximum at pH 6.86. Mechanisms of the interaction of enzymes with reactive oxygen species are considered. Antioxidant\\u000a activity criterion (IC50)

E. I. Korotkova; O. I. Lipskikh; M. A. Kiseleva; V. V. Ivanov

2008-01-01

224

Adsorption and mass transfer studies of Catalase in IMAC chromatography by dynamics methods  

Microsoft Academic Search

The adsorption equilibrium constant and kinetic properties for Catalase on Cu–IDA–agarose matrix have been measured by an impulse chromatography technique.The experiments were performed at pHs of 7.00, 7.40 and 7.80 and flow rates of 1.56–2.66mlmin?1. The impulse chromatographic technique has been applied to determine the equilibrium and kinetic parameters for Catalase in the Cu(II)–IDA–agarose system. It was found that the

R. Gutiérrez; E. M. M. Del Valle; M. A. Galán

2006-01-01

225

Catalysis of Oxygen Reduction by Catalase and HRP on Glassy Carbon Electrodes : Comparison of the Mechanisms  

Microsoft Academic Search

Catalase and horseradish peroxidase (HRP) are both hemic enzymes containing Fe(III)-protoporphyrin as prosthetic group. Both enzymes usually work with hydrogen peroxide a s s ubstrate; catalase ca talyses the disproportionation of hydrogen peroxide into oxygen and water: 2 H2O2 O2 + 2 H2O and HRP catalyses the oxidation of numerous s ubstrates (noted SH2) by hydrogen peroxide, following the general

Alain BERGEL; Maria Elena LAI

226

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

227

Diperoxovanadate participates in peroxidation reactions of H 2O 2 in presence of abundant catalase  

Microsoft Academic Search

Vanadate forms a stable complex with H2O2 at pH 7.0 in competition with catalase and the product, diperoxovanadate, resists scavenger action of catalase. Diperoxovanadate can act as a substrate in a H2O2-user reaction, horseradish peroxidase and can take the place of H2O2 far more effectively in oxidatively inactivating glyceraldehyde-3-phosphate dehydrogenase. By forming peroxo-complexes vanadate can provide a way of preserving

Aparna V. S Rao; H. N Ravishankar; T Ramasarma

1998-01-01

228

Direct voltammetry and electrocatalytic properties of catalase incorporated in polyacrylamide hydrogel films  

Microsoft Academic Search

The direct voltammetry and electrocatalytic properties of catalase (Cat) in polyacrylamide (PAM) hydrogel films cast on pyrolytic graphite (PG) electrodes were investigated. Cat-PAM film electrodes showed a pair of well-defined and nearly reversible cyclic voltammetry peaks for Cat Fe(III)\\/Fe(II) redox couples at approximately ?0.46 V vs. SCE in pH 7.0 buffers. The electron transfer between catalase and PG electrodes was

Haiyun Lu; Zhen Li; Naifei Hu

2003-01-01

229

CATALASE ACTIVITY OF TWO STREPTOCOCCUS FAECALIS STRAINS AND ITS ENHANCEMENT BY AEROBIOSIS AND ADDED CATIONS1  

PubMed Central

Jones, Dorothy (American Meat Institute Foundation, Chicago, Ill.), R. H. Deibel, and C. F. Niven, Jr. Catalase activity of two Streptococcus faecalis strains and its enhancement by aerobiosis and added cations. J. Bacteriol. 88:602–610. 1964.—The nature of catalase activity noted in two unusual Streptococcus faecalis strains was determined. Enzyme activity was lost slowly when cultures were maintained by daily transfer in test tubes of broth media. Loss of activity could be prevented by aerobic culture. Supplementation of the growth medium with ferric, manganese, and zinc ions, as well as aerobiosis, enhanced catalase activity. However, addition of these cations to cell suspensions or to cell-free extracts did not increase catalase activity. Although oxygen was observed to be one of the reaction end products, the catalase activity was not inhibited by cyanide or azide, and the iron-porphyrin coenzyme of classical catalase was not detected. The enzyme was purified 185-fold by precipitation with ammonium sulfate, followed by chromotography on a diethylaminoethyl cellulose column. PMID:14208495

Jones, Dorothy; Deibel, R. H.; Niven, C. F.

1964-01-01

230

Leptospira interrogans catalase is required for resistance to H2O2 and for virulence.  

PubMed

Pathogenic Leptospira spp. are likely to encounter higher concentrations of reactive oxygen species induced by the host innate immune response. In this study, we characterized Leptospira interrogans catalase (KatE), the only annotated catalase found within pathogenic Leptospira species, by assessing its role in resistance to H(2)O(2)-induced oxidative stress and during infection in hamsters. Pathogenic L. interrogans bacteria had a 50-fold-higher survival rate under H(2)O(2)-induced oxidative stress than did saprophytic L. biflexa bacteria, and this was predominantly catalase dependent. We also characterized KatE, the only annotated catalase found within pathogenic Leptospira species. Catalase assays performed with recombinant KatE confirmed specific catalase activity, while protein fractionation experiments localized KatE to the bacterial periplasmic space. The insertional inactivation of katE in pathogenic Leptospira bacteria drastically diminished leptospiral viability in the presence of extracellular H(2)O(2) and reduced virulence in an acute-infection model. Combined, these results suggest that L. interrogans KatE confers in vivo resistance to reactive oxygen species induced by the host innate immune response. PMID:22927050

Eshghi, Azad; Lourdault, Kristel; Murray, Gerald L; Bartpho, Thanatchaporn; Sermswan, Rasana W; Picardeau, Mathieu; Adler, Ben; Snarr, Brendan; Zuerner, Richard L; Cameron, Caroline E

2012-11-01

231

Leptospira interrogans Catalase Is Required for Resistance to H2O2 and for Virulence  

PubMed Central

Pathogenic Leptospira spp. are likely to encounter higher concentrations of reactive oxygen species induced by the host innate immune response. In this study, we characterized Leptospira interrogans catalase (KatE), the only annotated catalase found within pathogenic Leptospira species, by assessing its role in resistance to H2O2-induced oxidative stress and during infection in hamsters. Pathogenic L. interrogans bacteria had a 50-fold-higher survival rate under H2O2-induced oxidative stress than did saprophytic L. biflexa bacteria, and this was predominantly catalase dependent. We also characterized KatE, the only annotated catalase found within pathogenic Leptospira species. Catalase assays performed with recombinant KatE confirmed specific catalase activity, while protein fractionation experiments localized KatE to the bacterial periplasmic space. The insertional inactivation of katE in pathogenic Leptospira bacteria drastically diminished leptospiral viability in the presence of extracellular H2O2 and reduced virulence in an acute-infection model. Combined, these results suggest that L. interrogans KatE confers in vivo resistance to reactive oxygen species induced by the host innate immune response. PMID:22927050

Eshghi, Azad; Lourdault, Kristel; Murray, Gerald L.; Bartpho, Thanatchaporn; Sermswan, Rasana W.; Picardeau, Mathieu; Adler, Ben; Snarr, Brendan; Zuerner, Richard L.

2012-01-01

232

Purification of Paracoccidioides brasiliensis catalase P: subsequent kinetic and stability studies.  

PubMed

Catalases are essential components of the cellular equipment to cope with oxidative stress. Here we have purified a highly abundant catalase P of Paracoccidioides brasiliensis (PbCatP) that is preferentially expressed in the parasitic yeast phase. This oxidative stress-induced protein was isolated from yeast cells grown in the presence of 15 mM of hydrogen peroxide (H(2)O(2)). We have used consecutive steps of protein precipitation and gel filtration chromatography to achieve the purified protein. Protein purification was validated using matrix-assisted laser desorption ionization time-of-flight mass spectrometry and bioinformatics analysis. The purified enzyme showed strong similarity to small-subunit catalases. Like most monofunctional catalases, PbCatP is a homotetramer, resistant to inactivation by acidic conditions, temperature and denaturants. Furthermore, the kinetic behaviour of catalase P was observed to be different at low compared to high H(2)O(2) concentrations. The results demonstrated that a purified PbCatP is a homotetrameric enzyme, classified as a small subunit catalase. PMID:19897569

Chagas, Ronney Fernandes; Bailão, Alexandre Melo; Fernandes, Kátia Flávia; Winters, Michael S; Pereira, Maristela; Soares, Célia Maria de Almeida

2010-03-01

233

A novel impedimetric nanobiosensor for low level determination of hydrogen peroxide based on biocatalysis of catalase.  

PubMed

A robust and effective nanocomposite film-glassy carbon modified electrode based on multi-walled carbon nanotubes and a room temperature ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate was prepared by a layer-by-layer self-assembly method. The fabricated modified electrode was used as a novel impedimetric catalase nanobiosensor for the determination of H(2)O(2). Direct electron transfer and electrocatalysis of catalase were fully investigated. The results suggested that catalase could be firmly adsorbed at the modified electrode. A pair of quasi-reversible redox peaks of catalase was observed in a 0.20 M degassed phosphate buffer solution of pH 7.0. The nanocomposite film showed a pronounced increase in direct electron transfer between catalase and the electrode. The immobilized catalase exhibited an excellent electrocatalytic activity towards the reduction of H(2)O(2). The electrochemical impedance spectroscopy measurements revealed that the charge transfer resistance decreases significantly after enzymatic reaction with hydrogen peroxide, so that the prepared modified electrode can be used for the detection of ultra traces of H(2)O(2) (5-1700 nM). PMID:21880554

Shamsipur, Mojtaba; Asgari, Mehdi; Maragheh, Mohammad Ghannadi; Moosavi-Movahedi, Ali Akbar

2012-02-01

234

Protecting Peroxidase Activity of Multilayer Enzyme-Polyion Films Using Outer Catalase Layers  

PubMed Central

Films constructed layer-by-layer on electrodes with architecture {protein/hyaluronic acid (HA)}n containing myoglobin (Mb) or horseradish peroxidase (HRP) were protected against protein damage by H2O2 by using outer catalase layers. Peroxidase activity for substrate oxidation requires activation by H2O2, but {protein/HA}n films without outer catalase layers are damaged slowly and irreversibly by H2O2. The rate and extent of damage were decreased dramatically by adding outer catalase layers to decompose H2O2. Comparative studies suggest that protection results from catalase decomposing a fraction of the H2O2 as it enters the film, rather than by an in-film diffusion barrier. The outer catalase layers controlled the rate of H2O2 entry into inner regions of the film, and biased the system to favor electrocatalytic peroxide reduction over enzyme damage. Catalase-protected {protein/HA}n films had an increased linear concentration range for H2O2 detection. This approach offers an effective way to protect biosensors from damage by H2O2. PMID:18052272

Lu, Haiyun; Rusling, James F.; Hu, Naifei

2008-01-01

235

Increased Expression of Catalase and Superoxide Dismutase 2 Reduces Cone Cell Death in Retinitis Pigmentosa  

PubMed Central

Oxidative and nitrosative damage are major contributors to cone cell death in retinitis pigmentosa (RP). In this study, we explored the effects of augmenting components of the endogenous antioxidant defense system in models of RP, rd1, and rd10 mice. Unexpectedly, overexpression of superoxide dismutase 1 (SOD1) in rd1 mice increased oxidative damage and accelerated cone cell death. With an elaborate mating scheme, genetically engineered rd10 mice with either inducible expression of SOD2, Catalase, or both in photoreceptor mitochondria were generated. Littermates with the same genetic background that did not have increased expression of SOD2 nor Catalase provided ideal controls. Coexpression of SOD2 and Catalase, but not either alone, significantly reduced oxidative damage in the retinas of postnatal day (P) 50 rd10 mice as measured by protein carbonyl content. Cone density was significantly greater in P50 rd10 mice with coexpression of SOD2 and Catalase together than rd10 mice that expressed SOD2 or Catalase alone, or expressed neither. Coexpression of SOD2 and Catalase in rd10 mice did not slow rod cell death. These data support the concept of bolstering the endogenous antioxidant defense system as a gene-based treatment strategy for RP, and also indicate that coexpression of multiple components may be needed. PMID:19293779

Usui, Shinichi; Komeima, Keiichi; Lee, Sun Young; Jo, Young-Joon; Ueno, Shinji; Rogers, Brian S; Wu, Zhihao; Shen, Jikui; Lu, Lili; Oveson, Brian C; Rabinovitch, Peter S; Campochiaro, Peter A

2009-01-01

236

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

237

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

238

Catalase HPII from Escherichia coli Exhibits Enhanced Resistance to Denaturation Jacek Switala, Joe O. O'Neil, and Peter C. Loewen*,  

E-print Network

Catalase HPII from Escherichia coli Exhibits Enhanced Resistance to Denaturation Jacek Switala, Joe 11, 1999 ABSTRACT: Catalase HPII from Escherichia coli is a homotetramer of 753 residue subunits of the enzyme. For comparison, catalase-peroxidase HPI of E. coli and bovine liver catalase are 50% inactivated

O'Neil, Joe

239

Reduction of Hydrogen Peroxide Accumulation and Toxicity by a Catalase from Mycoplasma iowae  

PubMed Central

Mycoplasma iowae is a well-established avian pathogen that can infect and damage many sites throughout the body. One potential mediator of cellular damage by mycoplasmas is the production of H2O2 via a glycerol catabolic pathway whose genes are widespread amongst many mycoplasma species. Previous sequencing of M. iowae serovar I strain 695 revealed the presence of not only genes for H2O2 production through glycerol catabolism but also the first documented mycoplasma gene for catalase, which degrades H2O2. To test the activity of M. iowae catalase in degrading H2O2, we studied catalase activity and H2O2 accumulation by both M. iowae serovar K strain DK-CPA, whose genome we sequenced, and strains of the H2O2-producing species Mycoplasma gallisepticum engineered to produce M. iowae catalase by transformation with the M. iowae putative catalase gene, katE. H2O2-mediated virulence by M. iowae serovar K and catalase-producing M. gallisepticum transformants were also analyzed using a Caenorhabditis elegans toxicity assay, which has never previously been used in conjunction with mycoplasmas. We found that M. iowae katE encodes an active catalase that, when expressed in M. gallisepticum, reduces both the amount of H2O2 produced and the amount of damage to C. elegans in the presence of glycerol. Therefore, the correlation between the presence of glycerol catabolism genes and the use of H2O2 as a virulence factor by mycoplasmas might not be absolute. PMID:25127127

Pritchard, Rachel E.; Prassinos, Alexandre J.; Osborne, John D.; Raviv, Ziv; Balish, Mitchell F.

2014-01-01

240

Cardiac-specific overexpression of catalase attenuates lipopolysaccharide-induced myocardial contractile dysfunction: role of autophagy.  

PubMed

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 complications 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. A Kaplan-Meier curve was constructed for survival after LPS treatment. Our results revealed a lower mortality in catalase mice compared with FVB mice after 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 O(2)(-), and protein carbonyl formation, the effects of which were significantly attenuated by catalase overexpression. Electron microscopy revealed focal myocardial damage characterized by mitochondrial injury after LPS treatment, which was less severe in catalase mice. Interestingly, LPS-induced cardiomyocyte contractile dysfunction was prevented by the antioxidant N-acetylcysteine 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. PMID:22902401

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

2012-09-15

241

Adeno-Associated Viral-Mediated Catalase Expression Suppresses Optic Neuritis in Experimental Allergic Encephalomyelitis  

NASA Astrophysics Data System (ADS)

Suppression of oxidative injury by viral-mediated transfer of the human catalase gene was tested in the optic nerves of animals with experimental allergic encephalomyelitis (EAE). EAE is an inflammatory autoimmune disorder of primary central nervous system demyelination that has been frequently used as an animal model for the human disease multiple sclerosis (MS). The optic nerve is a frequent site of involvement common to both EAE and MS. Recombinant adeno-associated virus containing the human gene for catalase was injected over the right optic nerve heads of SJL/J mice that were simultaneously sensitized for EAE. After 1 month, cell-specific catalase activity, evaluated by quantitation of catalase immunogold, was increased approximately 2-fold each in endothelia, oligodendroglia, astrocytes, and axons of the optic nerve. Effects of catalase on the histologic lesions of EAE were measured by computerized analysis of the myelin sheath area (for demyelination), optic disc area (for optic nerve head swelling), extent of the cellular infiltrate, extravasated serum albumin labeled by immunogold (for blood-brain barrier disruption), and in vivo H2O2 reaction product. Relative to control, contralateral optic nerves injected with the recombinant virus without a therapeutic gene, catalase gene inoculation reduced demyelination by 38%, optic nerve head swelling by 29%, cellular infiltration by 34%, disruption of the blood-brain barrier by 64%, and in vivo levels of H2O2 by 61%. Because the efficacy of potential treatments for MS are usually initially tested in the EAE animal model, this study suggests that catalase gene delivery by using viral vectors may be a therapeutic strategy for suppression of MS.

Guy, John; Qi, Xiaoping; Hauswirth, William W.

1998-11-01

242

Reduction of hydrogen peroxide accumulation and toxicity by a catalase from Mycoplasma iowae.  

PubMed

Mycoplasma iowae is a well-established avian pathogen that can infect and damage many sites throughout the body. One potential mediator of cellular damage by mycoplasmas is the production of H2O2 via a glycerol catabolic pathway whose genes are widespread amongst many mycoplasma species. Previous sequencing of M. iowae serovar I strain 695 revealed the presence of not only genes for H2O2 production through glycerol catabolism but also the first documented mycoplasma gene for catalase, which degrades H2O2. To test the activity of M. iowae catalase in degrading H2O2, we studied catalase activity and H2O2 accumulation by both M. iowae serovar K strain DK-CPA, whose genome we sequenced, and strains of the H2O2-producing species Mycoplasma gallisepticum engineered to produce M. iowae catalase by transformation with the M. iowae putative catalase gene, katE. H2O2-mediated virulence by M. iowae serovar K and catalase-producing M. gallisepticum transformants were also analyzed using a Caenorhabditis elegans toxicity assay, which has never previously been used in conjunction with mycoplasmas. We found that M. iowae katE encodes an active catalase that, when expressed in M. gallisepticum, reduces both the amount of H2O2 produced and the amount of damage to C. elegans in the presence of glycerol. Therefore, the correlation between the presence of glycerol catabolism genes and the use of H2O2 as a virulence factor by mycoplasmas might not be absolute. PMID:25127127

Pritchard, Rachel E; Prassinos, Alexandre J; Osborne, John D; Raviv, Ziv; Balish, Mitchell F

2014-01-01

243

Intron loss and gain during evolution of the catalase gene family in angiosperms.  

PubMed Central

Angiosperms (flowering plants), including both monocots and dicots, contain small catalase gene families. In the dicot, Arabidopsis thaliana, two catalase (CAT) genes, CAT1 and CAT3, are tightly linked on chromosome 1 and a third, CAT2, which is more similar to CAT1 than to CAT3, is unlinked on chromosome 4. Comparison of positions and numbers of introns among 13 angiosperm catalase genomic sequences indicates that intron positions are conserved, and suggests that an ancestral catalase gene common to monocots and dicots contained seven introns. Arabidopsis CAT2 has seven introns; both CAT1 and CAT3 have six introns in positions conserved with CAT2, but each has lost a different intron. We suggest the following sequence of events during the evolution of the Arabidopsis catalase gene family. An initial duplication of an ancestral catalase gene gave rise to CAT3 and CAT1. CAT1 then served as the template for a second duplication, yielding CAT2. Intron losses from CAT1 and CAT3 followed these duplications. One subclade of monocot catalases has lost all but the 5'-most and 3'-most introns, which is consistent with a mechanism of intron loss by replacement of an ancestral intron-containing gene with a reverse-transcribed DNA copy of a fully spliced mRNA. Following this event of concerted intron loss, the Oryza sativa (rice, a monocot) CAT1 lineage acquired an intron in a novel position, consistent with a mechanism of intron gain at proto-splice sites. PMID:9584109

Frugoli, J A; McPeek, M A; Thomas, T L; McClung, C R

1998-01-01

244

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

2007-03-01

245

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

246

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

247

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

248

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

249

Development of a new catalase activity assay for biological samples using optical CUPRAC sensor  

NASA Astrophysics Data System (ADS)

A novel catalase activity assay was developed for biological samples (liver and kidney tissue homogenates) using a rapid and low-cost optical sensor-based ‘cupric reducing antioxidant capacity' (CUPRAC) method. The reagent, copper(II)-neocuproine (Cu(II)-Nc) complex, was immobilized onto a cation-exchanger film of Nafion, and the absorbance changes associated with the formation of the highly-colored Cu(I)-Nc chelate as a result of reaction with hydrogen peroxide (H2O2) was measured at 450 nm. When catalase was absent, H2O2 produced the CUPRAC chromophore, whereas catalase, being an effective H2O2 scavenger, completely annihilated the CUPRAC signal due to H2O2. Thus, the CUPRAC absorbance due to H2O2 oxidation concomitant with Cu(I)-Nc formation decreased proportionally with catalase. The developed sensor gave a linear response over a wide concentration range of H2O2 (0.68-78.6 ?M). This optical sensor-based method applicable to tissue homogenates proved to be efficient for low hydrogen peroxide concentrations (physiological and nontoxic levels) to which the widely used UV method is not accurately responsive. Thus, conventional problems of the UV method arising from relatively low sensitivity and selectivity, and absorbance disturbance due to gaseous oxygen evolution were overcome. The catalase findings of the proposed method for tissue homogenates were statistically alike with those of HPLC.

Bekde?er, Burcu; Özyürek, Mustafa; Güçlü, Kubilay; Alkan, Fulya Üstün; Apak, Re?at

2014-11-01

250

Targeting Catalase but Not Peroxiredoxins Enhances Arsenic Trioxide-Induced Apoptosis in K562 Cells  

PubMed Central

Despite considerable efficacy of arsenic trioxide (As2O3) in acute promyelocytic leukemia (APL) treatment, other non-APL leukemias, such as chronic myeloid leukemia (CML), are less sensitive to As2O3 treatment. However, the underlying mechanism is not well understood. Here we show that relative As2O3-resistant K562 cells have significantly lower ROS levels than As2O3-sensitive NB4 cells. We compared the expression of several antioxidant enzymes in these two cell lines and found that peroxiredoxin 1/2/6 and catalase are expressed at high levels in K562 cells. We further investigated the possible role of peroxirdoxin 1/2/6 and catalase in determining the cellular sensitivity to As2O3. Interestingly, knockdown of peroxiredoxin 1/2/6 did not increase the susceptibility of K562 cells to As2O3. On the contrary, knockdown of catalase markedly enhanced As2O3-induced apoptosis. In addition, we provide evidence that overexpression of BCR/ABL cannot increase the expression of PRDX 1/2/6 and catalase. The current study reveals that the functional role of antioxidant enzymes is cellular context and treatment agents dependent; targeting catalase may represent a novel strategy to improve the efficacy of As2O3 in CML treatment. PMID:25115845

Wang, Wei-Wei; Wei, Wei; Ma, Chun-Min; Wen, Dong-Hua; Lei, Hu; Xu, Han-Zhang; Wu, Ying-Li

2014-01-01

251

Reactive Oxygen Species Scavenging by Catalase Is Important for Female Lutzomyia longipalpis Fecundity and Mortality  

E-print Network

The phlebotomine sand fly Lutzomyia longipalpis is the most important vector of American visceral leishmaniasis (AVL), the disseminated and most serious form of the disease in Central and South America. In the natural environment, most female L. longipalpis are thought to survive for less than 10 days and will feed on blood only once or twice during their lifetime. Successful transmission of parasites occurs when a Leishmania-infected female sand fly feeds on a new host. Knowledge of factors affecting sand fly longevity that lead to a reduction in lifespan could result in a decrease in parasite transmission. Catalase has been found to play a major role in survival and fecundity in many insect species. It is a strong antioxidant enzyme that breaks down toxic reactive oxygen species (ROS). Ovarian catalase was found to accumulate in the developing sand fly oocyte from 12 to 48 hours after blood feeding. Catalase expression in ovaries as well as oocyte numbers was found to decrease with age. This reduction was not found in flies when fed on the antioxidant ascorbic acid in the sugar meal, a condition that increased mortality and activation of the prophenoloxidase cascade. RNA interference was used to silence catalase gene expression in female Lu. longipalpis. Depletion of catalase led to a significant increase of mortality and a reduction in the number of developing oocytes produced after blood feeding. These results demonstrate the central role

Hector Diaz-albiter; Roanna Mitford; O A. Genta; Mauricio R. V. Sant’anna; Rod J. Dillon

2010-01-01

252

Development of a new catalase activity assay for biological samples using optical CUPRAC sensor.  

PubMed

A novel catalase activity assay was developed for biological samples (liver and kidney tissue homogenates) using a rapid and low-cost optical sensor-based 'cupric reducing antioxidant capacity' (CUPRAC) method. The reagent, copper(II)-neocuproine (Cu(II)-Nc) complex, was immobilized onto a cation-exchanger film of Nafion, and the absorbance changes associated with the formation of the highly-colored Cu(I)-Nc chelate as a result of reaction with hydrogen peroxide (H2O2) was measured at 450 nm. When catalase was absent, H2O2 produced the CUPRAC chromophore, whereas catalase, being an effective H2O2 scavenger, completely annihilated the CUPRAC signal due to H2O2. Thus, the CUPRAC absorbance due to H2O2 oxidation concomitant with Cu(I)-Nc formation decreased proportionally with catalase. The developed sensor gave a linear response over a wide concentration range of H2O2 (0.68-78.6 ?M). This optical sensor-based method applicable to tissue homogenates proved to be efficient for low hydrogen peroxide concentrations (physiological and nontoxic levels) to which the widely used UV method is not accurately responsive. Thus, conventional problems of the UV method arising from relatively low sensitivity and selectivity, and absorbance disturbance due to gaseous oxygen evolution were overcome. The catalase findings of the proposed method for tissue homogenates were statistically alike with those of HPLC. PMID:24887508

Bekde?er, Burcu; Özyürek, Mustafa; Güçlü, Kubilay; Alkan, Fulya Üstün; Apak, Re?at

2014-11-11

253

Distribution of a Nocardia brasiliensis Catalase Gene Fragment in Members of the Genera Nocardia, Gordona, and Rhodococcus  

Microsoft Academic Search

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

LUCIO VERA-CABRERA; WENDY M. JOHNSON; OLIVERIO WELSH; FRANCISCO L. RESENDIZ-URESTI; MARIO C. SALINAS-CARMONA

1971-01-01

254

Catalase is a sink for H2O2 and is indispensable for stress defence in C3 plants  

Microsoft Academic Search

Hydrogen peroxide (H2O2) has been implicated in many stress conditions. Control of H2O2 levels is complex and dissection of mechanisms generating and relieving H2O2 stress is difficult, particularly in intact plants. We have used transgenic tobacco with ?10% wild-type catalase activity to study the role of catalase and effects of H2O2 stress in plants. Catalase-deficient plants showed no visible disorders

Hilde Willekens; Sangpen Chamnongpol; Mark Davey; Martina Schraudner; Christian Langebartels; Dirk Inzé; Wim Van Camp; Marc Van Montagu

1997-01-01

255

A novel analytical method to evaluate directly catalase activity of microorganisms and mammalian cells by ESR oximetry.  

PubMed

Electron spin resonance (ESR) oximetry technique was applied for analysis of catalase activity in the present study. Catalase activity was evaluated by measuring oxygen from the reaction between hydrogen peroxide (H(2)O(2)) and catalase-positive cells. It was demonstrated that the ESR spectra of spin-label probes, 4-hydroxy-2,2,6,6-tetramethylpiperidine 1-oxyl (TEMPOL), 4-oxo-2,2,6,6-tetramethyl-1-piperidinyloxy (4-oxo-TEMPO) and 4-maleimido-2,2,6,6-tetramethyl-1-piperidinyloxy (4-maleimido-TEMPO) in the presence of H(2)O(2) were broadened with the concentrations of catalase. It was possible to make a calibration curve for catalase activity by peak widths of the spectra of each spin-label probe, which are broadened dependently on catalase concentrations. The broadened ESR spectra were also observed when the catalase-positive micro-organisms or the mammalian cells originally from circulating monocytes/macrophages were mixed with TEMPOL and H(2)O(2). Meanwhile, catalase-negative micro-organisms caused no broadening change of ESR spectra. The present study indicates that it is possible to evaluate directly the catalase activity of various micro-organisms and mammalian cells by using an ESR oximetry technique. PMID:20815766

Nakamura, Keisuke; Kanno, Taro; Mokudai, Takayuki; Iwasawa, Atsuo; Niwano, Yoshimi; Kohno, Masahiro

2010-09-01

256

Synergistic effects between catalase inhibitors and modulators of nitric oxide metabolism on tumor cell apoptosis.  

PubMed

Inhibitors of catalase (such as ascorbate, methyldopa, salicylic acid and neutralizing antibodies) synergize with modulators of nitric oxide (NO) metabolism (such as arginine, arginase inhibitor, NO synthase-inducing interferons and NO dioxygenase inhibitors) in the singlet oxygen-mediated inactivation of tumor cell protective catalase. This is followed by reactive oxygen species (ROS)-dependent apoptosis induction. TGF-beta, NADPH oxidase-1, NO synthase, dual oxidase-1 and caspase-9 are characterized as essential catalysts in this process. The FAS receptor and caspase-8 are required for amplification of ROS signaling triggered by individual compounds, but are dispensable when the synergistic effect is established. Our findings explain the antitumor effects of catalase inhibitors and of compounds that target NO metabolism, as well as their synergy. These data may have an impact on epidemiological studies related to secondary plant compounds and open new perspectives for the establishment of novel antitumor drugs and for the improvement of established chemotherapeutics. PMID:25275027

Scheit, Katrin; Bauer, Georg

2014-10-01

257

[Study on interaction between sulfonylurea herbicides and catalase by fluorescence spectroscopy].  

PubMed

The binding of Sulfonylurea herbicides to catalase in aqueous solution was studied using fluorescence spectroscopy. It was shown that herbicides have a strong ability to quench the catalase fluorescence mainly through a static quenching procedure. The binding constant K and the number of binding site n were calculated according to the fluorescence quenching results. For chlorsufuron, K=8.69 x 10(5) L x mol(-1) and n = 1.16; for metsufuron methyl, K = 1.01 x 10(6) L x mol(-1) and n = 1.21; and for bensufuron methyl, K = 3.52 x 10(3) L x mol(-1), n = 0.77. It is clear that the binding of metsufuron methyl with catalase is stronger than that of chlorsufuron, while the binding of chlorsufuron stronger than that of bensufuron methyl. PMID:17112047

Ye, Fa-Bing; Dong, Yuan-Yan; Zhou, Peng; Mo, Xiao-Man; Hu, Xian-Wen

2006-09-01

258

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

259

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

260

Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH.  

PubMed

A catalase from a peroxide resistant mutant of Proteus mirabilis binds NADPH tightly. Interestingly, this enzyme can be stripped of NADPH without loss of the catalatic activity. It is the only known non-mammalian catalase able to bind NADPH. The structure without cofactor was solved by molecular replacement using the structure of beef liver catalase as a model. The structure was refined to an R-factor of 19.3% in the range 8 to 2.2 A resolution. According to the sequence, a methionine sulphone was positioned in the haem active site. This oxidized form of methionine is particular to Proteus mirabilis catalase and likely to produce some steric hindrance in the active site. Two important water molecules are positioned in the haem distal site. These two water molecules are not located in the structure of beef liver catalase, but are supposed to account for the catalytic mechanism. The liganded form was obtained by soaking crystals of the unliganded form into an NADPH solution. The structure was refined to an R-factor of 15.9% in the range of 8 to 3.1 A resolution using the unliganded structure as a model. The NADPH was clearly located in the electron density map with the same conformation as in beef liver catalase. The NADPH binding induces slight structural changes. However, the imidazole ring of a histidine residue (His284) rotates about 50 degrees to accommodate the cofactor. The electron transfer from NADPH to the haem molecule was examined and several pathways are proposed. PMID:7791219

Gouet, P; Jouve, H M; Dideberg, O

1995-06-23

261

Vascular endothelium-specific overexpression of human catalase in cloned pigs  

PubMed Central

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 (H2O2), an important regulator of vascular tone that contributes to diseases such as atherosclerosis and preeclampsia. A large animal model to study reduced endothelium-derived H2O2 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 H2O2 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 H2O2 in vasodilation and in the mechanisms underlying vascular health and disease. PMID:21170678

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.

2012-01-01

262

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

263

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

2011-10-01

264

Coordination modes of bridge carboxylates in dinuclear manganese compounds determine their catalase-like activities.  

PubMed

To explore the role of bridge carboxylate coordination modes on the catalase-like activities of dinuclear manganese compounds, [Mn(II)2(bpmapa)2(H2O)2](ClO4)2 (1), [Mn(II)2(pbpmapa)2(H2O)2](ClO4)2 (2), and [Mn(II)2(bpmaa)2(H2O)3](ClO4)2 (3) (bpmapa = [bis(2-pyridylmethyl)amino]propionic acid, pbpmapa = alpha-phenyl-beta-[bis(2-pyridylmethyl)amino]propionic acid, and bpmaa = [bis(2-pyridylmethyl)amino]acetic acid), in which Mn(II)-Mn(II) centers have a similar coordination sphere but different carboxylate-Mn bridging modes have been synthesized and structurally characterized by single X-ray diffraction, UV-visible, IR, and EPR spectroscopies, and their catalase-like activities were investigated. Studies of their catalytic activities and the influence of the nitrogenous bases on their catalytic activities indicated that the carboxylate-Mn coordination mode was crucial in H2O2 deprotonation, and eventually in H2O2 disproportionation. Compound 1 with a bidentate carboxylate bridge showed higher catalase-like activity than 2 and 3, in which the carboxylate groups have a monodentate bridging mode. The deprotonation ability of the carboxylate anion was determined by the O-C-O angle and the distance between the weakly bound oxygen of the bridging carboxylate to the manganese ion. The smaller the angle, and the shorter the distance, the stronger the basicity that the carboxylate anion exhibits. The bidentate mu-1,1 bridging coordination mode functionally mimicked the glutamate residues at the manganese catalase active site. Our results suggested that increasing the basicity of the bridging carboxylate ligand of the catalase model compounds will increase their deprotonation ability and lead to more active catalase mimics. PMID:19809747

Jiang, Xiaojun; Liu, Hui; Zheng, Bing; Zhang, Jingyan

2009-10-28

265

Subchronic exposure to high-dose ACE-inhibitor moexipril induces catalase activity in rat liver.  

PubMed

The long-term clinical effects of ACE-inhibitors have similarities with those of both fibrates and glitazones, activators of peroxisome proliferator activator receptor (PPAR) alpha and gamma, respectively. The antioxidant enzyme catalase, a heme protein that degrades hydrogen peroxide, is found at high concentrations in peroxisomes. Catalase activity is one of the recognized surrogate markers indicative of PPAR activation in the rat liver. The purpose of the study was to establish the effect of moexipril on catalase activity and to compare it with the effect of both saline controls and that of the known PPAR agonist clofibrate (positive control). Three groups of seven rats were used. All substances were applied i.p. daily for 5 days, followed by a 2-day break. The cycle was repeated eight times. After the final cycle (day 56) the animals were sacrificed and liver tissue collected. The number of catalase positive cells in both moexipril group (95% CI 57-61) and clofibrate group (95% CI 72-80) is higher than in controls (95% CI 3-16) (p < or = 0.01). The number of catalase positive cells in the clofibrate group is higher than in the moexipril group (p < or = 0.01). High-dose subchronic exposure to the ACE-inhibitor moexipril induces catalase activity in the rat liver to an extent comparable to fibrates. We suggest that some of the long-term advantages of ACE inhibitor use - beyond mere BP lowering - might be due to a PPAR mediated effect. PMID:16311918

Adeghate, E; Hasan, M Y; Ponery, A S; Nurulain, S M; Petroianu, G A

2005-12-01

266

Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy.  

PubMed

Various enzymes use semi-stable ferryl intermediates and free radicals during their catalytic cycle, amongst them haem catalases. Structures for two transient intermediates (compounds I and II) of the NADPH-dependent catalase from Proteus mirabilis (PMC) have been determined by time-resolved X-ray crystallography and single crystal microspectrophotometry. The results show the formation and transformation of the ferryl group in the haem, and the unexpected binding of an anion during this reaction at a site distant from the haem. PMID:8901874

Gouet, P; Jouve, H M; Williams, P A; Andersson, I; Andreoletti, P; Nussaume, L; Hajdu, J

1996-11-01

267

Transient upregulation of PGC-1? diminishes cardiac ischemia tolerance via upregulation of ANT1  

PubMed Central

Prolonged cardiac overexpression of the mitochondrial biogenesis regulatory transcriptional coactivator PGC-1? disrupts cardiac contractile function and its genetic ablation limits cardiac capacity to enhance work-load. In contrast, transient induction of PGC-1? alleviates neuronal cell oxidative stress and enhances skeletal myotube antioxidant defenses. We explored whether transient upregulation of PGC-1? in the heart protects against ischemia-reperfusion injury. The transient induction of PGC-1? in the cardiac-restricted inducible PGC-1? transgenic mouse, increased PGC-1? protein levels 5-fold. Following 25 minutes of ischemia and 2 hours of reperfusion on a Langendorff perfusion apparatus, contractile recovery and the rate pressure product was significantly blunted in mice overexpressing PGC-1? vs. controls. Affymetrix gene array analysis showed a 3-fold PGC-1?-mediated upregulation of adenine nucleotide translocase 1 (ANT1). As ANT1 upregulation induces cardiomyocyte cell death we investigated whether the induction of ANT1 by PGC-1? contributes to this enhanced ischemia-stress susceptibility. Infection with adenovirus harboring PGC-1? into cardiac-derived H9c2 cells significantly upregulates ANT1 without changing basal cell viability. In response to anoxia-reoxygenation injury cell death is significantly increased following PGC-1? overexpression. This detrimental effect is abolished following siRNA knockdown of ANT1. Similarly, the attenuation of ANT-1 in the presence of PGC-1? overexpression preserves the mitochondrial membrane potential in response to hydrogen-peroxide stress. Interestingly, the isolated knockdown of ANT1 also protects H9c2 cells from anoxia-reoxygenation injury. Taken together these data suggest that transient induction of PGC-1? in the murine heart decreases ischemia-reperfusion contractile recovery and diminishes anoxia-reoxygenation tolerance in H9c2 cells. These adverse phenotypes appear to be mediated, in part, by PGC-1? induced upregulation of ANT1. PMID:20600099

Lynn, Edward G.; Stevens, Mark V.; Wong, Renee P.; Carabenciov, Darin; Jacobson, Jeremy; Murphy, Elizabeth; Sack, Michael N.

2010-01-01

268

Heme oxygenase up-regulation in ultraviolet-B irradiated soybean plants involves reactive oxygen species.  

PubMed

Ultraviolet-B (UV-B) radiation has a negative impact on plant cells, and leads to the generation of reactive oxygen species (ROS). Heme oxygenase (HO, EC 1.14.99.3) plays a protective role against oxidative stress in mammals, but little is known about this issue in plants. Here, we report for the first time the response of HO in leaves of soybean (Glycine max L.) plants subjected to UV-B radiation. Under 7.5 and 15 kJ m(-2 )UV-B doses, HO, catalase (CAT, EC 1.11.1.6) and ascorbate peroxidase (APX, EC 1.11.1.11) activities were increased and the production of thiobarbituric acid reactive substances (TBARS) regain control values after 4 h of plant recuperation. Treatment with 30 kJ m(-2) UV-B provoked a decrease in these antioxidant enzyme activities. Immunoblot analysis showed a 4.3 and 3.7-fold increase in HO-1 protein expression after irradiation with 7.5 and 15 kJ m(-2), respectively. HO-1 transcript levels were enhanced (up to 77%) at these doses, as assessed by semi-quantitative RT-PCR. These data demonstrated that increased HO activity was associated with augmented protein expression and transcript levels. Plants pre-treated with the antioxidant ascorbic acid did not show the UV-B-induced up-regulation of HO-1 mRNA, but hydrogen peroxide treatment could mimic this reaction. Our results indicate that HO is up-regulated in a dose-depending manner as a mechanism of cell protection against oxidative damage and that such response occurred as a consequence of HO-1 mRNA enhancement involving ROS. PMID:16703357

Yannarelli, Gustavo G; Noriega, Guillermo O; Batlle, Alcira; Tomaro, Maria L

2006-10-01

269

Hydrogen-peroxide-induced heme degradation in red blood cells: the protective roles of catalase and glutathione peroxidase  

Microsoft Academic Search

Catalase and glutathione peroxidase (GSHPX) react with red cell hydrogen peroxide. A number of recent studies indicate that catalase is the primary enzyme responsible for protecting the red cell from hydrogen peroxide. We have used flow cytometry in intact cells as a sensitive measure of the hydrogen-peroxide-induced formation of fluorescent heme degradation products. Using this method, we have been able

Enika Nagababu; Francis J. Chrest; Joseph M. Rifkind

2003-01-01

270

MJD05-018 revised version July 22, 2005 1 Association of CAT polymorphisms with catalase activity and  

E-print Network

MJD05-018 revised version July 22, 2005 1 Association of CAT polymorphisms with catalase activity; 39 1345-50 #12;MJD05-018 revised version July 22, 2005 2 Abstract We tested the hypotheses that catalase activity is modified by CAT single nucleotide polymorphisms (SNPs) (­262

Paris-Sud XI, Université de

271

Identification of a functional peroxisome proliferator-activated receptor response element in the rat catalase promoter. Molecular Endocrinology  

E-print Network

has been shown to decrease the inflammatory response via transrepression of proinflammatory transcription factors. However, the identity of PPAR ? responsive genes that decrease the inflammatory response has remained elusive. Because generation of the reactive oxygen species hydrogen peroxide (H 2O 2) plays a role in the inflammatory process and activation of proinflammatory transcription factors, we wanted to determine whether the antioxidant enzyme catalase might be a PPAR ? target gene. We identified a putative PPAR response element (PPRE) containing the canonical direct repeat 1 motif, AG-GTGA-A-AGTTGA, in the rat catalase promoter. In vitro translated PPAR ? and retinoic X receptor-? proteins were able to bind to the catalase PPRE. Promoter deletion analysis revealed that the PPRE was functional, and a heterologous promoter construct containing a multimerized catalase PPRE demonstrated that the PPRE was necessary and sufficient for PPAR?-mediated activation. Treatment of microvascular endothelial cells with PPAR ? ligands led to increases in catalase mRNA and activity. These results demonstrate that PPAR ? can alter catalase expression; this occurs via a PPRE in the rat catalase promoter. Thus, in addition to transrepression of proinflammatory transcription factors, PPAR ? may also be modulating catalase expression, and hence down-regulating the inflammatory response via scavenging of reactive oxygen species. (Molecular Endocrinology 16: 2793–2801, 2002)

Geoffrey D. Girnun; Frederick E. Domann; Steven A. Moore; Mike E. C. Robbins

2002-01-01

272

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

273

A study of the inhibition of catalase by dipotassium trioxohydroxytetrafluorotriborate K?[B?O?F?OH].  

PubMed

In the development of boronic acid-based enzyme inhibitors as potential pharmaceutical drugs, dipotassium trioxohydroxytetrafluorotriborate K2[B3O3F4OH] was listed as a promising new therapeutic for treatment of these diseases. The catalase-mediated conversion of hydrogen peroxide, in the presence and absence of K2[B3O3F4OH] was studied. The kinetics conformed to the Michaelis-Menten model. Lineweaver-Burk plots were linear and plotted the family of straight lines intersected on the abscissa indicating non-competitive inhibition of the catalase. It appears that in the absence of inhibitor, catalase operates the best at conditions around pH 7.1 and in the presence of K2[B3O3F4OH] the optimum is around pH 6.2. The uncatalyzed reaction of hydrogen peroxide decomposition generally has a value of activation energy of 75?kJ?mole(-1), whereas catalase, in the absence of inhibitor, lowers the value to 11.2?kJ?mole(-1), while in the presence 69?mmoles?L(-1) of K2[B3O3F4OH] it was 37.8?kJ?mole(-1). PMID:24506205

Islamovic, Safija; Galic, Borivoj; Milos, Mladen

2014-10-01

274

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

275

Simulations of electron transfer in the NADPH-bound catalase from Proteus mirabilis PR.  

PubMed

Catalase-bound NADPH both prevents and reverses the accumulation of compound II, an inactive form of catalase that is generated from the normal active intermediate form (compound I) when catalase is exposed to a steady flow of hydrogen peroxide. The mechanism for the regeneration reaction is unknown although NADPH could act either as a one-electron or a two-electron donor. Recently, a reaction scheme has been proposed in which the formation of compound II from compound I generates a neighboring radical species within the protein. NADPH would then donate two electrons, one to compound II for reduction of the iron and the other to the protein free radical. In this paper, we report calculations to find the dominant electron tunneling pathways between NADPH and the heme iron in the catalase from the peroxide-resistant mutant of Proteus mirabilis. Two major tunneling pathways are found which fuse together on Ser-196. It is suggested that the sequence Gly-Ser of the loop that divides the beta 5-strand is the key element for shielding a radical amino acid. PMID:7548161

Bicout, D J; Field, M J; Gouet, P; Jouve, H M

1995-09-27

276

Low dose X -ray effects on catalase activity in animal tissue  

NASA Astrophysics Data System (ADS)

This study was intended to investigate the effect of low-dose X ray-irradiation upon the activity of catalase (CAT) in freshly excised chicken tissues (liver, kidney, brain, muscle). The tissue samples were irradiated with 0.5Gy and 2Gy respectively, in a 6 MV photon beam produced by a clinical linear accelerator (VARIAN CLINAC 2100SC). The dose rate was of 260.88cGy/min. at 100 cm source to sample distance. The catalase level was assayed spectrophotometrically, based on reaction kinetics, using a catalase UV assay kit (SIGMA). Catalase increased activity in various tissue samples exposed to the studied X ray doses (for example with 24 % in the liver cells, p<0.05) suggested the stimulation of the antioxidant enzyme biosynthesis within several hours after exposure at doses of 0.5 Gy and 2 Gy; the putative enzyme inactivation could also occur (due to the injuries on the hydrogen bonds that ensure the specificity of CAT active site) but the resulted balance of the two concurrent processes indicates the cell ability of decomposing the hydrogen peroxide-with benefits for the cell physiology restoration for the chosen low dose radiation.

Focea, R.; Nadejde, C.; Creanga, D.; Luchian, T.

2012-12-01

277

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

278

Adeno-Associated Viral-Mediated Catalase Expression Suppresses Optic Neuritis in Experimental Allergic Encephalomyelitis  

Microsoft Academic Search

Suppression of oxidative injury by viral-mediated transfer of the human catalase gene was tested in the optic nerves of animals with experimental allergic encephalomyelitis (EAE). EAE is an inflammatory autoimmune disorder of primary central nervous system demyelination that has been frequently used as an animal model for the human disease multiple sclerosis (MS). The optic nerve is a frequent site

John Guy; Xiaoping Qi; William W. Hauswirth

1998-01-01

279

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

280

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

281

Protective role of extracellular catalase (KatA) against UVA radiation in Pseudomonas aeruginosa biofilms.  

PubMed

One of the more stressful factors that Pseudomonas aeruginosa must face in nature is solar UVA radiation. In this study, the protective role of KatA catalase in both planktonic cells and biofilms of P. aeruginosa against UVA radiation was determined by using the wild-type (PAO1) and an isogenic catalase deficient strain (katA). The katA strain was more sensitive than the wild-type, especially in the case of biofilms. Moreover, the wild-type biofilm was more resistant than its planktonic counterpart, but this was not observed in the katA strain. Striking KatA activity was detected in the matrix of katA(+) strains, and to our knowledge, this is the first report of this activity in the matrix of P. aeruginosa biofilms. Provision of bovine catalase or KatA to the matrix of a katA biofilm significantly increased its UVA tolerance, demonstrating that extracellular KatA is essential to optimal defense against UVA in P. aeruginosa biofilms. Efficiency of photocatalytic treatments using TiO2 and UVA was lower in biofilms than in planktonic cells, but KatA and KatB catalases seem not to be responsible for the higher resistance of the sessile cells to this treatment. PMID:24491420

Pezzoni, Magdalena; Pizarro, Ramón A; Costa, Cristina S

2014-02-01

282

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

E-print Network

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 concentration of diaminobenzidine, barium peroxide as the source of peroxide, and pH of 8.5. Ultrastructurally, the enzyme was seen to permeate the endothelial fenestrae and basement membranes of tubular and glomerular capillaries of the kidney. The urinary space and tubular lumina contained no reaction product. In the myocardial capillaries, the tracer filled the pinocytotic vesicles but did not diffuse across the intercellular clefts of the endothelium. In liver, uptake of catalase was seen both in hepatocytes and in Kupffer cells. Crystalline beef liver catalase, a heme protein with a molecular weight of 240,000 (26), is known to split hydrogen peroxide to water and oxygen.

M A Venkatachalam; H Dariush Fahimi

283

310 THE EFFECT OF THE DEGREE OF HOMOGENIZATION ON THE CATALASE ACTIVITY OF LIVER "HOMOGENATES"  

E-print Network

THERE seems at present to be no general agreement amongst workers on liver catalase concerning either the best method of estimating the enzyme, or of preparing the homogenates in which the enzyme is measured. It is well known that the results of catalase activity measurements are considerably affected by such variables as temperature, hydrogen peroxide concentration, length of time for which the enzyme and substrate are allowed to remain in contact, and whether the measurements are of oxygen evolution or hydrogen peroxide disappearance. However, little attention seems to have been paid to the possibility that some discrepancies in the results obtained by various authors may depend as much on the method by which liver homogenates are prepared as on the method of enzyme assay. An example of an apparently complete disagreement in the literature concerns the question of a sex difference in liver catalase activity in mice and rats. Adams (1950, 1952) reported that a sex difference was present in the livers of the heterogenous strains of mice used, the catalase level in males being higher than in

D. H. Adams; E. Ann Burgess

1957-01-01

284

Analysis of allelic variants in the catalase gene in patients with the skin depigmenting disorder vitiligo  

Microsoft Academic Search

Vitiligo is an acquired hypomelanotic skin disorder characterised by circumscribed depigmented macules resulting from the loss of functional melanocytes from the cutaneous epidermis. Conditions that might result in epidermal oxidative stress and consequently damage to pigment cells have been reported in the skin of vitiligo patients, including low catalase activity and increases in hydrogen peroxide levels. However, the cause of

Nikos G. Gavalas; Samia Akhtar; David J. Gawkrodger; Philip F. Watson; Anthony P. Weetman; E. Helen Kemp

2006-01-01

285

Catalase activity measured with a micro oxygen electrode in a pressurized reaction vessel. [Mice, rats  

Microsoft Academic Search

The assembly and the use of a simple airtight pressurized reaction vessel are described for the measurement of catalase activity with a micro oxygen electrode in an optically heterogenous medium. The oxygen concentration is expressed as the ratio of observed current to the current in an air-saturated solution. Thus, an individual standard can be obtained for each measurement and the

Halbach

1977-01-01

286

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...

287

Effect of Mixing Conditions on the Behavior of Lipoxygenase, Peroxidase, and Catalase in Wheat Flour Doughs  

Microsoft Academic Search

Cereal Chem. 75(1):85-93 The effect of mixing has been tested on the extractable activities of lipoxygenase, peroxidase, and catalase from dough after 2, 5, and 20 min of mixing, and 30 min of rest period after 20 min of mixing. Different mixing conditions have been studied including temperature, atmosphere, speed, amount of water added to the dough, buffer solutions between

Jean-François Delcros; Lalatiana Rakotozafy; Aline Boussard; Sylvie Davidou; Catherine Porte; Jacques Potus; Jacques Nicolas

1998-01-01

288

Effect of Iron Deficiency on Gas Exchange and Catalase and Peroxidase Activity in Citrus  

Microsoft Academic Search

The effects of iron (Fe) deficiency on catalase and peroxidase activity, net photosynthesis (Pn), stomatal conductance (gs), plant water relations, and specific leaf weight, were studied under greenhouse conditions in two sweet orange (C. sinensis) cultivars grafted on sour orange (Citrus aurantium) and Swingle citrumelo (C. paradisi × P. trifoliata). Iron deficiency caused by the absence of Fe in the Hoagland nutrient

Vassilios Chouliaras; Ioannis Therios; Athanassios Molassiotis; Angelos Patakas; Gregorios Diamantidis

2005-01-01

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

Hydrogen peroxide homeostasis: activation of plant catalase by calcium/calmodulin  

NASA Technical Reports Server (NTRS)

Environmental stimuli such as UV, pathogen attack, and gravity can induce rapid changes in hydrogen peroxide (H(2)O(2)) levels, leading to a variety of physiological responses in plants. Catalase, which is involved in the degradation of H(2)O(2) into water and oxygen, is the major H(2)O(2)-scavenging enzyme in all aerobic organisms. A close interaction exists between intracellular H(2)O(2) and cytosolic calcium in response to biotic and abiotic stresses. Studies indicate that an increase in cytosolic calcium boosts the generation of H(2)O(2). Here we report that calmodulin (CaM), a ubiquitous calcium-binding protein, binds to and activates some plant catalases in the presence of calcium, but calcium/CaM does not have any effect on bacterial, fungal, bovine, or human catalase. These results document that calcium/CaM can down-regulate H(2)O(2) levels in plants by stimulating the catalytic activity of plant catalase. Furthermore, these results provide evidence indicating that calcium has dual functions in regulating H(2)O(2) homeostasis, which in turn influences redox signaling in response to environmental signals in plants.

Yang, T.; Poovaiah, B. W.

2002-01-01

291

Direct evidence for catalase activity of [Ru(V)(edta)(O)](-).  

PubMed

Reported is the first example of a ruthenium(iii) complex, Ru(III)(edta) (edta(4-) = ethylenediaminetetraacetate), that catalyzes the disproportion of H2O2 to O2 and water in resemblance to catalase activity, and shedding light on the possible mechanism of action of the [Ru(V)(edta)(O)](-) formed in the reacting system. PMID:25307989

Chatterjee, Debabrata; Jaiswal, Namita; Franke, Alicja; van Eldik, Rudi

2014-10-28

292

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)] [INRS, Vandoeuvre-les-Nancy (France); Schmitt, P. [Association InterEntreprises de Medecine du Travail du Bas-Rhin, Strasbourg (France)] [Association InterEntreprises de Medecine du Travail du Bas-Rhin, Strasbourg (France)

1996-06-07

293

Mycobacterium tuberculosis catalase and peroxidase activities and resistance to oxidative killing in human monocytes in vitro.  

PubMed

Mycobacterium tuberculosis has a relatively high resistance to killing by hydrogen peroxide and organic peroxides. Resistance may be mediated by mycobacterial catalase-peroxidase (KatG) and possibly by alkyl hydroperoxide reductase (AhpC). To determine the interrelationship between sensitivity to H2O2, catalase and peroxidase activities, and bacillary growth rates measured both intracellularly in human monocytes and in culture medium, we examined one laboratory strain, two clinical isolates, and three recombinant strains of M. tuberculosis with differing levels of KatG and AhpC. Five of the mycobacterial strains had intracellular doubling times of 27 to 32 h, while one KatG-deficient clinical isolate (ATCC 35825) doubled in approximately 76 h. Killing of mycobacteria by exogenously added H2O2 was more pronounced for intracellular bacilli than for those bacilli derived from disrupted monocytes. Strains with no detectable KatG expression or catalase activity were relatively sensitive to killing (43 to 67% killing) by exogenous H2O2. However, once even minimal catalase activity was present, mycobacterial catalase activity over a 10-fold range (0.56 to 6.2 U/mg) was associated with survival of 85% of the bacilli. Peroxidase activity levels correlated significantly with resistance of the mycobacterial strains to H2O2-mediated killing. An endogenous oxidative burst induction by 4beta-phorbol 12beta-myristate 13alpha-acetate treatment of infected monocytes reduced the viability of the KatG null strain (H37Rv Inhr) but not the KatG-overexpressing strain [H37Rv(pMH59)]. These results suggest that mycobacterial resistance to oxidative metabolites (including H2O2 and other peroxides) may be an important mechanism of bacillary survival within the host phagocyte. PMID:9864198

Manca, C; Paul, S; Barry, C E; Freedman, V H; Kaplan, G

1999-01-01

294

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

2008-11-01

295

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

296

LESION SIMULATING DISEASE1 Interacts with Catalases to Regulate Hypersensitive Cell Death in Arabidopsis1[C][W  

PubMed Central

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

2013-01-01

297

Purification and characterization of a catalase from photosynthetic bacterium Rhodospirillum rubrum S1 grown under anaerobic conditions.  

PubMed

The photosynthetic bacterium, Rhodospirillum rubrum S1, when grown under anaerobic conditions, generated three different types of catalases. In this study, we purified and characterized the highest molecular weight catalase from the three catalases. The total specific catalase activity of the crude cell extracts was 88 U/mg. After the completion of the final purification step, the specific activity of the purified catalase was 1,256 U/mg. The purified catalase evidenced an estimated molecular mass of 318 kDa, consisting of four identical subunits, each of 79 kDa. The purified enzyme exhibited an apparent Km value of 30.4 mM and a Vmax of 2,564 U against hydrogen peroxide. The enzyme also exhibited a broad optimal pH (5.0-9.0), and remained stable over a broad temperature range (20 degrees C-60 degrees C). It maintained 90% activity against organic solvents (ethanol/chloroform) known hydroperoxidase inhibitors, and exhibited no detectable peroxidase activity. The catalase activity of the purified enzyme was reduced to 19% of full activity as the result of the administration of 10 mM 3-amino-1,2,4-triazole, a heme-containing catalase inhibitor. Sodium cyanide, sodium azide, and hydroxylamine, all of which are known heme protein inhibitors, inhibited catalase activity by 50% at concentrations of 11.5 microM, 0.52 microM, and 0.11 microM, respectively. In accordance with these findings, the enzyme was identified as a type of monofunctional catalase. PMID:16728955

Kang, Yoon-Suk; Lee, Dong-Heon; Yoon, Byoung-Jun; Oh, Duck-Chul

2006-04-01

298

Effect of starvation and refeeding on catalase and superoxide dismutase activities in skeletal and cardiac muscles from 12-month-old rats  

Microsoft Academic Search

Summary Catalase and superoxide dismutase (SOD) activities were determined in muscles from 12-month-old rats after severe starvation and after subsequent refeeding. Catalase increased in most muscles after starvation and decreased after refeeding, while SOD remained unchanged.

C. J. Lammi-Keefe; P. V. J. Hegarty; P. B. Swan

1981-01-01

299

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

300

Hesperidin protects against cyclophosphamide-induced hepatotoxicity by upregulation of PPAR? and abrogation of oxidative stress and inflammation.  

PubMed

The most important reason for the non-approval and withdrawal of drugs by the Food and Drug Administration is hepatotoxicity. Therefore, this study was undertaken to evaluate the protective effects of hesperidin against cyclophosphamide (CYP)-induced hepatotoxicity in Wistar rats. The rats received a single intraperitoneal dose of CYP of 200 mg/kg body mass, followed by treatment with hesperidin, orally, at doses of 25 and 50 mg/kg for 11 consecutive days. CYP induced hepatic damage, as evidenced by the significantly elevated levels of serum pro-inflammatory cytokines, serum transaminases, liver lipid peroxidation, and nitric oxide. As a consequence, there was reduced glutathione content, and the activities of the antioxidant enzymes superoxide dismutase, catalase, and glutathione peroxidase, were markedly reduced. In addition, CYP administration induced a considerable downregulation of peroxisome proliferator activated receptor gamma (PPAR?) and upregulation of nuclear factor-kappa B (NF-?B) and inducible nitric oxide synthase (iNOS) mRNA expression. Hesperidin, in a dose-dependent manner, rejuvenated the altered markers to an almost normal state. In conclusion, hesperidin showed a potent protective effect against CYP-induced oxidative stress and inflammation leading to hepatotoxicity. The study suggests that hesperidin exerts its protective effect against CYP-induced hepatotoxicity through upregulation of hepatic PPAR? expression and abrogation of inflammation and oxidative stress. PMID:25079140

Mahmoud, Ayman M

2014-09-01

301

Benzothiazole aniline tetra(ethylene glycol) and 3-amino-1,2,4-triazole inhibit neuroprotection against amyloid peptides by catalase overexpression in vitro.  

PubMed

Alzheimer's disease, Familial British dementia, Familial Danish dementia, Type 2 diabetes mellitus, plus Creutzfeldt-Jakob disease are associated with amyloid fibril deposition and oxidative stress. The antioxidant enzyme catalase is a neuroprotective amyloid binding protein. Herein the effects of catalase overexpression in SH-SY5Y neuronal cells on the toxicity of amyloid-? (A?), amyloid-Bri (ABri), amyloid-Dan (ADan), amylin (IAPP), and prion protein (PrP) peptides were determined. Results showed catalase overexpression was neuroprotective against A?, ABri, ADan, IAPP, and PrP peptides. The catalase inhibitor 3-amino-1,2,4-triazole (3-AT) and catalase-amyloid interaction inhibitor benzothiazole aniline tetra(ethylene glycol) (BTA-EG4) significantly enhanced neurotoxicity of amyloid peptides in catalase overexpressing neuronal cells. This suggests catalase neuroprotection involves breakdown of hydrogen peroxide (H2O2) plus a direct binding interaction between catalase and the A?, ABri, ADan, IAPP, and PrP peptides. Kisspeptin 45-50 had additive neuroprotective actions against the A? peptide in catalase overexpressing cells. The effects of 3-AT had an intracellular site of action, while catalase-amyloid interactions had an extracellular component. These results suggest that the 3-AT and BTA-EG4 compounds may be able to inhibit endogenous catalase mediated neuroprotection. Use of BTA-EG4, or compounds that inhibit catalase binding to amyloid peptides, as potential therapeutics for Neurodegenerative diseases may therefore result in unwanted effects. PMID:23968537

Chilumuri, Amrutha; Odell, Mark; Milton, Nathaniel G N

2013-11-20

302

Benzothiazole Aniline Tetra(ethylene glycol) and 3-Amino-1,2,4-triazole Inhibit Neuroprotection against Amyloid Peptides by Catalase Overexpression in Vitro  

PubMed Central

Alzheimer’s disease, Familial British dementia, Familial Danish dementia, Type 2 diabetes mellitus, plus Creutzfeldt-Jakob disease are associated with amyloid fibril deposition and oxidative stress. The antioxidant enzyme catalase is a neuroprotective amyloid binding protein. Herein the effects of catalase overexpression in SH-SY5Y neuronal cells on the toxicity of amyloid-? (A?), amyloid-Bri (ABri), amyloid-Dan (ADan), amylin (IAPP), and prion protein (PrP) peptides were determined. Results showed catalase overexpression was neuroprotective against A?, ABri, ADan, IAPP, and PrP peptides. The catalase inhibitor 3-amino-1,2,4-triazole (3-AT) and catalase-amyloid interaction inhibitor benzothiazole aniline tetra(ethylene glycol) (BTA-EG4) significantly enhanced neurotoxicity of amyloid peptides in catalase overexpressing neuronal cells. This suggests catalase neuroprotection involves breakdown of hydrogen peroxide (H2O2) plus a direct binding interaction between catalase and the A?, ABri, ADan, IAPP, and PrP peptides. Kisspeptin 45–50 had additive neuroprotective actions against the A? peptide in catalase overexpressing cells. The effects of 3-AT had an intracellular site of action, while catalase-amyloid interactions had an extracellular component. These results suggest that the 3-AT and BTA-EG4 compounds may be able to inhibit endogenous catalase mediated neuroprotection. Use of BTA-EG4, or compounds that inhibit catalase binding to amyloid peptides, as potential therapeutics for Neurodegenerative diseases may therefore result in unwanted effects. PMID:23968537

2013-01-01

303

Apollon/Bruce is upregulated by Humanin.  

PubMed

Humanin, a short bioactive peptide, inhibits a variety of cell deaths. Humanin-mediated inhibition of neuronal cell death, caused by an Alzheimer's disease (AD)-linked mutant gene occurs via binding of Humanin to its heterotrimeric Humanin receptor (htHNR), which results in the activation of the Janus-associated kinases (JAKs) and signal transducer and activator and transcription 3 (STAT3) signaling pathway. A previous study demonstrated that the Humanin-induced activation of the htHNR/JAK2/STAT3 signaling pathway leads to increased expression of SH3 domain-binding protein 5 (SH3BP5), which is an essential effector of Humanin's anti-cell death activity in some cultured neuronal cells. However, it remains unknown whether SH3BP5 is the sole effector of the Humanin signaling pathway via htHNR/JAKs/STAT3. Here we show that the Humanin signaling pathway via htHNR/JAKs/STAT3 increased the expression levels of mRNA and protein of Apollon/Bruce, an unusual member of the inhibitors of apoptosis proteins, and that overexpression of Apollon/Bruce inhibits neuronal death, caused by a London-type familial AD-linked mutant (V642I) of amyloid ? precursor protein. Overall, the results indicate that expression of Apollon/Bruce is upregulated by Humanin, and Apollon/Bruce could be an effector of Humanin in a context-dependent manner. PMID:25138702

Hashimoto, Yuichi; Takeshita, Yuji; Naito, Mikihiko; Uchino, Hiroyuki; Matsuoka, Masaaki

2014-12-01

304

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

305

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. PMID:8819328

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

1996-01-01

306

Hydrogen peroxide determination in pharmaceutical formulations and cosmetics using a new catalase biosensor.  

PubMed

The possibility of evaluating the content of hydrogen peroxide in several authentic matrices, such as cosmetic and pharmaceutical formulations, was studied. A new catalase biosensor fabricated using an amperometric gas-diffusion oxygen sensor as electrochemical transducer and the catalase enzyme immobilized in kappa-carrageenan gel and capable of operating in both aqueous and non aqueous solvents was developed and tested for this purpose. Creams, emulsions and disinfectant solutions were analysed. To this end, a preliminary check was needed to establish the best conditions to analyse these matrices; the choice of solvent was one of the most important points studied. The solvents considered included dioxane, water-dioxane mixtures, water saturated chloroform and aqueous solutions. The different solubility properties of the matrices analysed were taken into account. PMID:9863948

Campanella, L; Roversi, R; Sammartino, M P; Tomassetti, M

1998-10-01

307

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

2013-07-11

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

2007-06-01

309

Ergot cluster-encoded catalase is required for synthesis of chanoclavine-I in Aspergillus fumigatus.  

PubMed

Genes required for ergot alkaloid biosynthesis are clustered in the genomes of several fungi. Several conserved ergot cluster genes have been hypothesized, and in some cases demonstrated, to encode early steps of the pathway shared among fungi that ultimately make different ergot alkaloid end products. The deduced amino acid sequence of one of these conserved genes (easC) indicates a catalase as the product, but a role for a catalase in the ergot alkaloid pathway has not been established. We disrupted easC of Aspergillus fumigatus by homologous recombination with a truncated copy of that gene. The resulting mutant (?easC) failed to produce the ergot alkaloids typically observed in A. fumigatus, including chanoclavine-I, festuclavine, and fumigaclavines B, A, and C. The ?easC mutant instead accumulated N-methyl-4-dimethylallyltryptophan (N-Me-DMAT), an intermediate recently shown to accumulate in Claviceps purpurea strains mutated at ccsA (called easE in A. fumigatus) (Lorenz et al. Appl Environ Microbiol 76:1822-1830, 2010). A ?easE disruption mutant of A. fumigatus also failed to accumulate chanoclavine-I and downstream ergot alkaloids and, instead, accumulated N-Me-DMAT. Feeding chanoclavine-I to the ?easC mutant restored ergot alkaloid production. Complementation of either ?easC or ?easE mutants with the respective wild-type allele also restored ergot alkaloid production. The easC gene was expressed in Escherichia coli, and the protein product displayed in vitro catalase activity with H(2)O(2) but did not act, in isolation, on N-Me-DMAT as substrate. The data indicate that the products of both easC (catalase) and easE (FAD-dependent oxidoreductase) are required for conversion of N-Me-DMAT to chanoclavine-I. PMID:21409592

Goetz, Kerry E; Coyle, Christine M; Cheng, Johnathan Z; O'Connor, Sarah E; Panaccione, Daniel G

2011-06-01

310

Adenovirus-mediated catalase gene transfer reduces oxidant stress in human, porcine and rat pancreatic islets  

Microsoft Academic Search

Summary   Susceptibility of pancreatic islets to oxidant stress may affect islet viability and contribute to primary non function of\\u000a allo- or xenogenic grafts. We investigated the influence of overexpression of catalase (CAT) on the viability of human, porcine\\u000a and rat islets, as well as INS-1 beta-cell line. Islets were transfected with a replication-deficient adenovirus vector containing\\u000a human CAT cDNA under

P. Y. Benhamou; C. Moriscot; M. J. Richard; O. Beatrix; L. Badet; F. Pattou; J. Kerr-Conte; J. Chroboczek; P. Lemarchand; S. Halimi

1998-01-01

311

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

312

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

313

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

314

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

315

Sulfite increases lipoperoxidation and decreases the activity of catalase in brain of rats  

Microsoft Academic Search

The main objective of this study was to investigate the in vitro effects of sulfite, a metabolite accumulated in isolated\\u000a sulfite oxidase deficiency, on Na +, K +-ATPase activity and on some parameters of oxidative stress, namely thiobarbituric acid-reactive substances (TBARS) and catalase\\u000a activity (antioxidant enzyme) in cerebral cortex, striatum and hippocampus from 10- and 60-day-old rats. Results showed that

Fábria Chiarani; Caren S. Bavaresco; Carlos S. Dutra-Filho; Carlos Alexandre Netto; Angela T. S. Wyse

2008-01-01

316

Catalase and sulfur in the rice rhizosphere: An ultrastructural histochemical demonstration of a symbiotic relationship  

Microsoft Academic Search

An ultrastructural study has been made of a symbiotic association between a sulfur bacterium and the roots of the rice plant (Oryza saliva L.). This association is proposed to have useful economic consequences in ameliorating hydrogen sulfide toxicity and associated Akiochi or Straighthead disease in lowland rice cultivation. The presence of catalase (E.C. 1.11.1.6) in rice roots and in some

Alan D. Heritage; Ralph C. Foster

1984-01-01

317

Catalase enzyme activity is related to tolerance of mandarin fruits to chilling  

Microsoft Academic Search

The effect of a postharvest hot-water dip treatment (HWT) at 53°C for 3 min and a 3-day heat-conditioning treatment at 37°C with air (HAT) at 90–95% RH on chilling tolerance and catalase (CAT) activity was compared in ‘Fortune’ mandarins. The HWT treatment increased CAT activity in the fruit, but after they were removed from high temperature to cold storage a

Jose M Sala; Mar??a T Lafuente

2000-01-01

318

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

319

The roles of CATALASE2 in abscisic acid signaling in Arabidopsis guard cells.  

PubMed

We investigated the roles of catalase (CAT) in abscisic acid (ABA)-induced stomatal closure using a cat2 mutant and an inhibitor of CAT, 3-aminotriazole (AT). Constitutive reactive oxygen species (ROS) accumulation due to the CAT2 mutation and AT treatment did not affect stomatal aperture in the absence of ABA, whereas ABA-induced stomatal closure, ROS production, and [Ca(2+)](cyt) oscillation were enhanced. PMID:21979081

Jannat, Rayhanur; Uraji, Misugi; Morofuji, Miho; Hossain, Mohammad Anowar; Islam, Mohammad Muzahidul; Nakamura, Yoshimasa; Mori, Izumi C; Murata, Yoshiyuki

2011-01-01

320

Human Erythrocyte Catalase: 2-D Crystal Nucleation and Production of Multiple Crystal Forms  

Microsoft Academic Search

Negatively stained electron microscope images are presented, showing the nucleation of two-dimensional (2-D) crystals of human erythrocyte catalase produced on mica by the negative staining-carbon film technique. Examples of the formation of partially ordered 2-D arrays and more ordered 2-D crystals are shown and the conditions required for the production of large well-ordered 2-D crystals discussed. The structural transformation of

J. Robin Harris; Andreas Holzenburg

1995-01-01

321

Probing the two-domain structure of homodimeric prokaryotic and eukaryotic catalase–peroxidases  

Microsoft Academic Search

Catalase–peroxidases (KatGs) are ancestral bifunctional heme peroxidases found in archaeons, bacteria and lower eukaryotes. In contrast to homologous cytochrome c peroxidase (CcP) and ascorbate peroxidase (APx) homodimeric KatGs have a two-domain monomeric structure with a catalytic N-terminal heme domain and a C-terminal domain of high sequence and structural similarity but without obvious function. Nevertheless, without its C-terminal counterpart the N-terminal

Srijib Banerjee; Marcel Zamocky; Paul G. Furtmüller; Christian Obinger

2010-01-01

322

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

323

Purification and characterization of a mesohalic catalase from the halophilic bacterium Halobacterium halobium.  

PubMed

When subjected to the stress of growth in a relatively low-salt environment (1.25 M NaCl), the halophilic bacterium Halobacterium halobium induces a catalase. The protein has been purified to electrophoretic homogeneity and has an M(r) of 240,000 and a subunit size of approximately 62,000. The enzyme is active over a broad pH range of 6.5 to 10.0, with a peak in activity at pH 7.0. It has an isoelectric point of 4.0. This catalse, which is not readily reduced by dithionite, shows a Soret peak at 406 nm. Cyanide and azide inhibit the enzyme at micromolar concentrations, whereas maleimide is without effect. The addition of 20 mM 3-amino-1,2,4-triazole results in a 33% inhibition in enzymatic activity. The tetrameric protein binds NADP in a 1:1 ratio but does not peroxidize NADPH, NADH, or ascorbate. Although the enzymatic activity is maximal when assayed in a 50 mM potassium phosphate buffer with no NaCl, prolonged incubation in a buffer lacking NaCl results in inactive enzyme. Moreover, purification must be performed in the presence of 2 M NaCl. Equally as effective in retaining enzymatic function are NaCl, LiCl, KCl, CsCl, and NH4Cl, whereas divalent salts such as MgCl2 and CaCl2 result in the immediate loss of activity. The catalase is stained by pararosaniline, which is indicative of a glycosidic linkage. The Km for H2O2 is 60 mM, with inhibition observed at concentrations in excess of 90 mM. Thus, the mesohalic catalase purified from H. halobium seems to be similar to other catalases, except for the salt requirements, but differs markedly from the constitutive halobacterial hydroperoxidase. PMID:7814327

Brown-Peterson, N J; Salin, M L

1995-01-01

324

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

325

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

Microsoft Academic Search

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

Vicki S. Thompson; Kastli D. Schaller; William A. Apel

2003-01-01

326

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

327

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

328

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

329

Probing the two-domain structure of homodimeric prokaryotic and eukaryotic catalase-peroxidases.  

PubMed

Catalase-peroxidases (KatGs) are ancestral bifunctional heme peroxidases found in archaeons, bacteria and lower eukaryotes. In contrast to homologous cytochrome c peroxidase (CcP) and ascorbate peroxidase (APx) homodimeric KatGs have a two-domain monomeric structure with a catalytic N-terminal heme domain and a C-terminal domain of high sequence and structural similarity but without obvious function. Nevertheless, without its C-terminal counterpart the N-terminal domain exhibits neither catalase nor peroxidase activity. Except some hybrid-type proteins all other members of the peroxidase-catalase superfamily lack this C-terminal domain. In order to probe the role of the two-domain monomeric structure for conformational and thermal stability urea and temperature-dependent unfolding experiments were performed by using UV-Vis-, electronic circular dichroism- and fluorescence spectroscopy, as well as differential scanning calorimetry. Recombinant prokaryotic (cyanobacterial KatG from Synechocystis sp. PCC6803) and eukaryotic (fungal KatG from Magnaporthe grisea) were investigated. The obtained data demonstrate that the conformational and thermal stability of bifunctional KatGs is significantly lower compared to homologous monofunctional peroxidases. The N- and C-terminal domains do not unfold independently. Differences between the cyanobacterial and the fungal enzyme are relatively small. Data will be discussed with respect to known structure and function of KatG, CcP and APx. PMID:20654740

Banerjee, Srijib; Zamocky, Marcel; Furtmüller, Paul G; Obinger, Christian

2010-11-01

330

Ethanol metabolism in rat brain homogenates by a catalase-H2O2 system.  

PubMed

Homogenates of perfused rat brains incubated in the presence of ethanol (50-100 mM) and glucose (10 mM) were found to oxidize ethanol to acetaldehyde. The addition of glucose oxidase, a known hydrogen peroxide generator, to the incubation medium, significantly (P less than 0.05) increased the generation of acetaldehyde. The presence in the incubation medium of metyrapone, an inhibitor of cytochrome P450, or pyrazole, an alcohol dehydrogenase inhibitor, did not affect the levels of acetaldehyde obtained. Conversely, the presence of 3-amino-1,2,4-triazole, a known catalase inhibitor, induced a concentration-dependent reduction of the amount of acetaldehyde generated after incubation, even in the presence of glucose oxidase. Homogenates of perfused brains of rats treated with 3-amino-1,2,4-triazole or cyanamide (another H2O2-dependent catalase blocker) also showed a dose-dependent reduction of the acetaldehyde obtained. These findings support the notion that a catalase-mediated oxidation of ethanol is present in rat brain homogenates. It is suggested that this local oxidation of ethanol may have important biological implications. The data of both studies increase support for the notion that acetaldehyde is produced directly in the brain and that it may be the agent mediating some of the psychopharmacological properties of ethanol and be one of the factors determining the propensity of an animal to voluntarily consume ethanol. PMID:1632841

Aragon, C M; Rogan, F; Amit, Z

1992-07-01

331

Amperometric biosensor for the detection of hydrogen peroxide using catalase modified electrodes in polyacrylamide.  

PubMed

A simple biosensor for the detection of hydrogen peroxide in organic solvents has been developed and coupled to a flow injection analysis (FIA) system. Catalase was entrapped in polyacrylamide gel and placed on the surface of platinum (working electrode) fixed in a Teflon holder with Ag-wire (auxiliary electrode), followed by addition of filter paper soaked in KCl. The entrapped catalase gel was held on the electrode using membranes. The effects of cellulose and polytetrafluroethylene (PTFE) membranes on the electrode response towards hydrogen peroxide have been studied. The modified electrode has been used to study the detection of hydrogen peroxide in solvents like water, dimethyl sulfoxide (DMSO), and 1,4-dioxane using amperometric techniques like cyclic voltammetry (CV) and FIA. The CV of modified catalase electrode showed a broad oxidation peak at -150 mV and a clear reduction peak at -212 mV in the presence of hydrogen peroxide. Comparison of CV with hydrogen peroxide in various solvents has been carried out. The electrode showed an irreversible kinetics with DMSO as the solvent. A flow cell has been designed in order to carry on FIA studies to obtain calibration plots for hydrogen peroxide with the modified electrode. The calibration plots in several solvents such as water, dimethyl sulfoxide, 1,4-dioxane have been obtained. The throughput of the enzyme electrode was 10 injections per hour. Due to the presence of membrane the response time of the electrode is concentration dependent. PMID:16099064

Varma, Shailly; Mattiasson, Bo

2005-09-23

332

CATALASE ACTIVITY OF LIVER AND KIDNEY IN FROGS WITH SPONTANEOUS RENAL CARCINOMA*  

E-print Network

There is now abundant evidence that tumors of cold blooded vertebrates are essentially similar in morphology and behavior to the corresponding types of tumors in birds and mammals, including man (1, 2). Little, however, is known about their chemical activities. A promising approach to investigations in this field is the study of enzymatic properties of tumors. For these purposes the kidney carcinoma of the leopard frog (Rana pipiens) is excellent material; it occurs as a "spontaneous " tumor in frogs living under natural conditions (3); it is readily available and attains a size adequate for analysis; the frogs can be maintained over a wide range of environmental temperature, the effects of which upon enzymatic processes can thus be determined. The present study deals with the enzyme catalase, whose properties have been thoroughly investigated in cancer of warm blooded animals, chiefly mice and rats (4). In mammals two main changes in catalase activity with respect to cancer have been found. First, the catalase activity of any kind of neoplastic tissue is uniformly low. Second, any kind of cancer no matter where located, if

B Balduin Lucki; Mary Berwick

333

Turning points in the evolution of peroxidase-catalase superfamily: molecular phylogeny of hybrid heme peroxidases.  

PubMed

Heme peroxidases and catalases are key enzymes of hydrogen peroxide metabolism and signaling. Here, the reconstruction of the molecular evolution of the peroxidase-catalase superfamily (annotated in pfam as PF00141) based on experimentally verified as well as numerous newly available genomic sequences is presented. The robust phylogenetic tree of this large enzyme superfamily was obtained from 490 full-length protein sequences. Besides already well-known families of heme b peroxidases arranged in three main structural classes, completely new (hybrid type) peroxidase families are described being located at the border of these classes as well as forming (so far missing) links between them. Hybrid-type A peroxidases represent a minor eukaryotic subfamily from Excavates, Stramenopiles and Rhizaria sharing enzymatic and structural features of ascorbate and cytochrome c peroxidases. Hybrid-type B peroxidases are shown to be spread exclusively among various fungi and evolved in parallel with peroxidases in land plants. In some ascomycetous hybrid-type B peroxidases, the peroxidase domain is fused to a carbohydrate binding (WSC) domain. Both here described hybrid-type peroxidase families represent important turning points in the complex evolution of the whole peroxidase-catalase superfamily. We present and discuss their phylogeny, sequence signatures and putative biological function. PMID:24846396

Zámocký, Marcel; Gasselhuber, Bernhard; Furtmüller, Paul G; Obinger, Christian

2014-12-01

334

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

335

Nitric oxide and catalase-sensitive relaxation by scutellarin in the mouse thoracic aorta.  

PubMed

The vascular activity of scutellarin (SCU), a flavonoid isolated from a Chinese traditional medicinal plant, was investigated in isolated thoracic aortic rings of mice. SCU-induced dose-dependent relaxation of phenylephrine (1 microM) stimulated contractions. This relaxation was reduced by endothelium removal, significantly reduced by both the nitric oxide synthase inhibitor (Nomega-nitro-L-arginine methylester, 300 microM) and slightly limited by the soluble guanylyl cyclase inhibitor (1 H-[1,2,4] oxidazolol [4,3-a] quinoxalin-1-one, 100 microM). The catalase inhibitor (3-amino-1,2,4-triazole, 50 mM) augmented the constriction and blocked the lowest SCU concentration relaxation, whereas catalase addition was without effect. Preincubation with 300 and 1000 microM SCU significantly suppressed the contractile dose-response to phenylephrine, causing both a significant rise in half maximal effective concentration and a decrease in the maximal developed force. Western blot analysis showed that SCU inhibition of contraction was independent of reductions in myosin light chain phosphorylation. These results suggested that SCU relaxation was predominantly endothelium dependent and likely involved the catalase-sensitive nitric oxide synthase signaling pathway, without loss of myosin phosphorylation. The potential clinical use of SCU may prove to be effective in increasing vasoreactivity, independently of smooth muscle contractile activity that is mediated by the 20-kDa myosin light chain phosphorylation. PMID:19129733

Yang, Weimin; Lust, Robert M; Bofferding, April; Wingard, Christopher J

2009-01-01

336

Specific Function of the Met-Tyr-Trp Adduct Radical and Residues Arg-418 and Asp-137 in the Atypical Catalase Reaction of Catalase-Peroxidase KatG*  

PubMed Central

Catalase activity of the dual-function heme enzyme catalase-peroxidase (KatG) depends on several structural elements, including a unique adduct formed from covalently linked side chains of three conserved amino acids (Met-255, Tyr-229, and Trp-107, Mycobacterium tuberculosis KatG numbering) (MYW). Mutagenesis, electron paramagnetic resonance, and optical stopped-flow experiments, along with calculations using density functional theory (DFT) methods revealed the basis of the requirement for a radical on the MYW-adduct, for oxyferrous heme, and for conserved residues Arg-418 and Asp-137 in the rapid catalase reaction. The participation of an oxyferrous heme intermediate (dioxyheme) throughout the pH range of catalase activity is suggested from our finding that carbon monoxide inhibits the activity at both acidic and alkaline pH. In the presence of H2O2, the MYW-adduct radical is formed normally in KatG[D137S] but this mutant is defective in forming dioxyheme and lacks catalase activity. KatG[R418L] is also catalase deficient but exhibits normal formation of the adduct radical and dioxyheme. Both mutants exhibit a coincidence between MYW-adduct radical persistence and H2O2 consumption as a function of time, and enhanced subunit oligomerization during turnover, suggesting that the two mutations disrupting catalase turnover allow increased migration of the MYW-adduct radical to protein surface residues. DFT calculations showed that an interaction between the side chain of residue Arg-418 and Tyr-229 in the MYW-adduct radical favors reaction of the radical with the adjacent dioxyheme intermediate present throughout turnover in WT KatG. Release of molecular oxygen and regeneration of resting enzyme are thereby catalyzed in the last step of a proposed catalase reaction. PMID:22918833

Zhao, Xiangbo; Khajo, Abdelahad; Jarrett, Sanchez; Suarez, Javier; Levitsky, Yan; Burger, Richard M.; Jarzecki, Andrzej A.; Magliozzo, Richard S.

2012-01-01

337

Coordination modes of tyrosinate-ligated catalase-type heme enzymes: Magnetic circular dichroism studies of Plexaura homomalla allene oxide synthase, Mycobacterium avium ssp . Paratuberculosis protein-2744c, and bovine liver catalase in their ferric and ferrous states  

Microsoft Academic Search

Bovine liver catalase (BLC), catalase-related allene oxide synthase (cAOS) from Plexaura homomalla, and a recently isolated protein from the cattle pathogen Mycobacterium avium ssp. paratuberculosis (MAP-2744c (MAP)) are all tyrosinate-ligated heme enzymes whose crystal structures have been reported. cAOS and MAP have low (<20%) sequence similarity to, and significantly different catalytic functions from, BLC. cAOS transforms 8R-hydroperoxy-eicosatetraenoic acid to an

D. M. Indika Bandara; Masanori Sono; Grant S. Bruce; Alan R. Brash; John H. Dawson

338

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. PMID:8769411

1996-01-01

339

Evaluation of criteria used in the identification of actinomyces bovis with particular reference to the catalase reaction  

Microsoft Academic Search

The identification of smooth typeActinomyces bovis is an extremely difficult one to make. By a well selected set of criteria, including the catalase test, it is generally possible to make an unquestionable identification.

Loyal S. Suter

1956-01-01

340

Changes in the activities of catalase, peroxidase, and polyphenol oxidase in apple buds during bud break induced by thidiazuron  

Microsoft Academic Search

The breaking of dormancy in apple buds (Malus domestica Borkh cv. York Imperial) by thidiazuron (N-phenyl-N?-1,2,3,-thidiazol-5-ylurea) was investigated in relation to catalase, peroxidase, and polyphenol oxidase activities and their\\u000a isoenzyme patterns. The activity and number of isoenzymic components of catalase increased progressively during bud break,\\u000a then decreased after buds started to grow. Peroxidase activity was highest during dormancy and declined

Shiow Y. Wang; Hong J. Jiao; Miklos Faust

1991-01-01

341

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

PubMed

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 -0.05 V vs. SCE at pH 7, characteristic of the heme Fe (III)/Fe (II) redox couple. The formal potential of catalase in nickel oxide film were linearly varied in the range 1-12 with slope of 58.426 mV/pH, indicating that the electron transfer is accompanied by single proton transportation. The electron transfer between catalase and electrode surface, (k(s)) of 3.7(+/-0.1) s(-1) was greatly facilitated in the microenvironment of nickel oxide film. The electrocatalytic reduction of hydrogen peroxide at glassy carbon electrode modified with nickel oxide nano-scale islands and catalase enzyme has been studied. The embedded catalase in NiO nanoparticles showed excellent electrocatalytic activity toward hydrogen peroxide reduction. Also the modified rotating disk electrode shows good analytical performance for amperometric determination of hydrogen peroxide. The resultant catalase/nickel oxide modified glassy carbon electrodes exhibited fast amperometric response (within 2 s) to hydrogen peroxide reduction (with a linear range from 1 microM to 1 mM), excellent stability, long term life and good reproducibility. The apparent Michaelis-Menten constant is calculated to be 0.96(+/-0.05)mM, which shows a large catalytic activity of catalase in the nickel oxide film toward hydrogen peroxide. The excellent electrochemical reversibility of redox couple, high stability, technical simplicity, lake of need for mediators and short preparations times are advantages of this electrode. Finally the activity of biosensor for nitrite reduction was also investigated. PMID:17166647

Salimi, Abdollah; Sharifi, Ensiyeh; Noorbakhsh, Abdollah; Soltanian, Saied

2007-02-01

342

Molecular Medicine © 2000 The Picower Institute Press Peroxynitrite Formation and Decreased Catalase Activity in Autoimmune MRL-lpr/lpr Mice  

E-print Network

Background: (MRL)-lpr/lpr mice spontaneously develop autoimmune disease characterized by arthritis and glomerulonephritis. Nitric oxide is postulated to play a role in the disease pathogenesis, as mice treated with the nitric oxide synthase inhibitor N G-monomethyl-L-arginine (NMMA) show markedly reduced manifestations of the disease. The purpose of this study was to examine the role of peroxynitrite in disease development in MRL-lpr/lpr mice. Materials and Methods: We examined kidney extracts from control and MRL-lpr/lpr mice for nitrotyrosine by immunoblot with a rabbit polyclonal anti-nitrotyrosine antibody. Catalase activity was determined spectrophotometrically or by activity staining of native polyacrylamide gels. In some experiments, we studied the ability of peroxynitrite and other agents to modify purified catalase in vitro. Results: Kidney extracts from diseased mice had elevated levels of nitrotyrosine, and decreased levels of catalase activity and protein, relative to control mice. MRL-lpr/lpr mice treated with NMMA in vivo had decreased levels of nitrotyrosine, and demonstrated a partial restoration of both catalase activity and protein levels. Treatment of catalase in vitro with peroxynitrite or tetranitromethane at pH 8.0 resulted in protein nitration and a decrease in catalase activity. 1,3-morpholinosydnonimine (SIN-1), a peroxynitrite generator, also decreased the activity of catalase. Conclusions: These observations suggest that peroxynitrite formation, with an associated decrease in catalase activity and general decrease in antioxidant enzyme activity, may result in increased levels of hydrogen peroxide and other oxidants that can contribute to the pathogenesis of disease in MRL-lpr/lpr mice.

Teresa Keng; Christopher T. Privalle; Gary S. Gilkeson; J. Brice Weinberg

2000-01-01

343

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

344

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

345

Use of cadmium hydroxide gel for isolation of extracellular catalases from Penicillium piceum and characterization of purified enzymes  

Microsoft Academic Search

We optimized the conditions for isolation of extracellular catalases from Penicillium piceum F-648 and P. piceum A3 by means of volume chromatography with cadmium hydroxide gel. Our study showed that 55–57 mg wet gel are sufficient for\\u000a the maximum sorption of catalase from 1 ml of culture fluid. This gel was formed in 1 ml 70 mM Cd(NO3)2 after addition

A. N. Eremin; I. V. Moroz; R. V. Mikhailova

2008-01-01

346

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

347

Voltammetric measurements at the surface of cotton: absorption and catalase reactivity of a dinuclear manganese complex.  

PubMed

Voltammetric measurements at the surface of cotton fabric were conducted after impregnating the surface of the textile with graphite flakes. The resulting conducting surface contact was connected to a conventional basal plane pyrolytic graphite substrate electrode and employed both in stagnant solution and in rotating disc voltammetry mode. Diffusion through the immobilized cotton sample (inter-fiber) is probed with the aqueous Fe(CN)6(4-/3-) redox system. With a small amount of platinum immobilized at the cotton surface, catalase reactivity toward hydrogen peroxide was observed and used to further quantify the diffusion (intra- and inter-fiber) into the reactive zone at the graphite-cotton interface. A well-known catalase model system, the dinuclear manganese metal complex [Mn(IV)2(micro-O)3L2](PF6)2 (with L=1,4,7-trimethyl-1,4,7-triazacyclononane), is investigated in aqueous 0.1 M carbonate buffer at pH 9.8 in contact with cotton fabric. Absorption of the metal complex is monitored and quantified by voltammetric methods. A Langmurian binding constant of approximately K=2x103 M-1 was determined. Voltammetric measurements of the adsorbed metal complex reveal strong absorption and chemically irreversible reduction characteristics similar to those observed in solution. In the presence of hydrogen peroxide, catalyst coverage dependent anodic catalase activity was observed approximately following the rate law rate=k[catalyst]surface[H2O2]solution and with k=3x104 dm3 s-1 mol-1. The catalyst reactivity was modified by the presence of cotton. PMID:17279720

Marken, Frank; Taylor, James E; Bonné, Michael J; Helton, Matthew E; Parry, Matthew L; McKee, Vickie

2007-02-13

348

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

349

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

350

High-catalase strains of Mycobacterium kansasii isolated from water in Texas.  

PubMed Central

Isolation techniques with membrane-filtered potable water samples resulted in the isolation of potentially pathogenic high-catalase strains of Mycobacterium kansasii from 8 of 19 representative outlets in a small central Texas town. Mycobacterium gordonae was isolated from all samples, and Mycobacterium fortuitum was isolated from two samples. Data on chlorine levels are presented along with a possible explanation for the unusually high numbers of mycobacteria in these potable water samples. Findings suggest that water is a source of M. kansasii and may be an important link in the epidemiological picture of the disease. PMID:7381016

Steadham, J E

1980-01-01

351

Temperature dependence of oxygen evolution through catalase-like activity of horseradish peroxidase  

NASA Astrophysics Data System (ADS)

By experimental investigations of the temperature dependence of catalase-like activity of horseradish peroxidase in the temperature range 278 328 K, different kinetic profiles for oxygen evolution were found below and above 298 K. Extension of the model is proposed to account for these observations. By numeric simulations of the reaction kinetics at different temperatures, it was found that enhanced evaporation of molecular oxygen from the reaction solution is the main root through which oxygen is lost at elevated temperatures in laboratory conditions.

Popovi?-Bijeli?, A.; Bijeli?, G.; Kolar-Ani?, Lj.; Vukojevi?, V.

2007-09-01

352

Catalase-negative Staphylococcus aureus isolated from a diabetic foot ulcer  

PubMed Central

We report a catalase-negative Staphylococcus aureus isolated from a 56-year-old male diabetic patient with foot ulcer who attended our surgery ward. Species identification was confirmed by Gram staining, standard biochemical tests and PCR amplification of the nuc and fem genes. Antibiotic susceptibility showed that the strain was sensitive to imepenem, chloramphenicol, amoxicillin, vancomycin and resistant to oxacillin, penicillin, ceftriaxone, erythromycin, clindamycin, and amikacin. Clinicians and microbiologists must be encouraged to identify and report these atypical strains and the infections associated with them in order to establish their role in pathogenesis. PMID:22347567

Dezfulian, A; Salehian, MT; Amini, V; Dabiri, H; Azimirad, M; Aslani, MM; Zali, MR; Fazel, I

2010-01-01

353

Light Dependence of Catalase Synthesis and Degradation in Leaves and the Influence of Interfering Stress Conditions 1  

PubMed Central

The enzyme catalase (EC 1.11.1.6) is light sensitive and subject to a rapid turnover in light, similar to the D1 reaction center protein of photosystem II. After 3 h of preadaptation to darkness or to different light intensities (90 and 520 ?mol m?2 s?1 photosynthetic photon flux density), sections of rye leaves (Secale cereale L.) were labeled for 4 h with l-[35S]methionine. From leaf extracts, catalase was immunoprecipitated with an antiserum prepared against the purified enzyme from rye leaves. Both incorporation into catalase and degradation of the enzyme polypeptide during a subsequent 16-h chase period increased with light intensity. At a photon flux density of 520 ?mol m?2 s?1, the apparent half-time of catalase in rye leaves was 3 to 4 h, whereas that of the D1 protein was much shorter, about 1.5 h. Exposure to stress conditions, such as 0.6 m NaCl or a heat-shock temperature of 40°C, greatly suppressed both total protein synthesis and incorporation of the label into catalase and into the D1 protein. Immunoblotting assays indicated that in light, but not in darkness, steady-state levels of catalase and of the D1 protein strongly declined during treatments with salt, heat shock, or translation inhibitors that block repair synthesis. Because of the common property of rapid photodegradation and the resulting dependence on continuous repair, declines in catalase as well as of the D1 protein represent specific and sensitive indicators for stress conditions that suppress the translational activities of leaves. Images Figure 1 Figure 2 Figure 4 Figure 5 Figure 7 Figure 8 PMID:16653156

Hertwig, Birgit; Streb, Peter; Feierabend, Jurgen

1992-01-01

354

Cardiac-specific catalase overexpression rescues anthrax lethal toxin-induced cardiac contractile dysfunction: role of oxidative stress and autophagy  

PubMed Central

Background Lethal and edema toxins secreted by Bacillus anthracis during anthrax infection were found to incite serious cardiovascular complications. However, the underlying mechanisms in anthrax lethal toxin-induced cardiac anomalies remain unknown. This study was designed to evaluate the impact of antioxidant enzyme catalase in anthrax lethal toxin-induced cardiomyocyte contractile dysfunction. Methods Wild type (WT) and cardiac-specific catalase overexpression mice were challenged with lethal toxin (2 ?g/g, intraperotineally (i.p.)). Cardiomyocyte contractile and intracellular Ca2+ properties were assessed 18 h later using an IonOptix edge-detection system. Proteasome function was assessed using chymotrypsin-like and caspase-like activities. GFP-LC3 puncta and Western blot analysis were used to evaluate autophagy and protein ubiquitination. Results Lethal toxin exposure suppressed cardiomyocyte contractile function (suppressed peak shortening, maximal velocity of shortening/re-lengthening, prolonged duration of shortening/re-lengthening, and impaired intracellular Ca2+ handling), the effects of which were alleviated by catalase. In addition, lethal toxin triggered autophagy, mitochondrial and ubiquitin-proteasome defects, the effects of which were mitigated by catalase. Pretreatment of cardiomyocytes from catalase mice with the autophagy inducer rapamycin significantly attenuated or ablated catalase-offered protection against lethal toxin-induced cardiomyocyte dysfunction. On the other hand, the autophagy inhibitor 3-MA ablated or significantly attenuated lethal toxin-induced cardiomyocyte contractile anomalies. Conclusions Our results suggest that catalase is protective against anthrax lethal toxin-induced cardiomyocyte contractile and intracellular Ca2+ anomalies, possibly through regulation of autophagy and mitochondrial function. PMID:23134810

2012-01-01

355

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

356

Two independent peroxisomal targeting signals in catalase A of Saccharomyces cerevisiae.  

PubMed

In contrast to many other peroxisomal proteins catalase A contains at least two peroxisomal targeting signals each sufficient to direct reporter proteins to peroxisomes. One of them resides at the extreme carboxy terminus constituting a new variant of this signal, -SSNSKF, not active in monkey kidney cells (Gould, S. J., G. A. Keller, N. Hosken, J. Wilkinson, and S. Subramani 1989. J. Cell Biol. 108:1657-1664). However, this signal is completely dispensable for import of catalase A itself. In its amino-terminal third this protein contains another peroxisomal targeting signal sufficient to direct reporter proteins into microbodies. This internal signal depends on the context. The nature of this targeting signal might be a short defined sequence or a structural feature recognized by import factors. In addition, we have demonstrated that the carboxy-terminal seven amino acids of citrate synthase of Saccharomyces cerevisiae encoded by CIT2 and containing the canonical -SKL represents a targeting signal sufficient to direct reporter proteins to peroxisomes. PMID:8425895

Kragler, F; Langeder, A; Raupachova, J; Binder, M; Hartig, A

1993-02-01

357

Modulation of reactive oxygen species by Rac1 or catalase prevents asbestos-induced pulmonary fibrosis  

PubMed Central

The release of reactive oxygen species (ROS) and cytokines by alveolar macrophages has been demonstrated in asbestos-induced pulmonary fibrosis, but the mechanism linking alveolar macrophages to the pathogenesis is not known. The GTPase Rac1 is a second messenger that plays an important role in host defense. In this study, we demonstrate that Rac1 null mice are protected from asbestos-induced pulmonary fibrosis, as determined by histological and biochemical analysis. We hypothesized that Rac1 induced pulmonary fibrosis via generation of ROS. Asbestos increased TNF-? and ROS in a Rac1-dependent manner. TNF-? was elevated only 1 day after exposure, whereas ROS generation progressively increased in bronchoalveolar lavage cells obtained from wild-type (WT) mice. To determine whether ROS generation contributed to pulmonary fibrosis, we overexpressed catalase in WT monocytes and observed a decrease in ROS generation in vitro. More importantly, administration of catalase to WT mice attenuated the development of fibrosis in vivo. For the first time, these results demonstrate that Rac1 plays a crucial role in asbestos-induced pulmonary fibrosis. Moreover, it suggests that a simple intervention may be useful to prevent progression of the disease. PMID:19684199

Murthy, Shubha; Adamcakova-Dodd, Andrea; Perry, Sarah S.; Tephly, Linda A.; Keller, Richard M.; Metwali, Nervana; Meyerholz, David K.; Wang, Yongqiang; Glogauer, Michael; Thorne, Peter S.

2009-01-01

358

Catalase-like activity studies of the manganese(II) adsorbed zeolites  

NASA Astrophysics Data System (ADS)

Preparation of manganese(II) adsorbed on zeolite 3A, 4A, 5A. AW-300, ammonium Y zeolite, organophilic, molecular sieve and catalase-like enzyme activity of manganese(II) adsorbed zeolites are reported herein. Firstly zeolites are activated at 873 K for two hours before contact manganese(II) ions. In order to observe amount of adsorption, filtration process applied for the solution. The pure zeolites and manganese(II) adsorbed zeolites were analysed by FT-IR. As a result according to the FT-IR spectra, the incorporation of manganese(II) cation into the zeolite structure causes changes in the spectra. These changes are expected particularly in the pseudolattice bands connected with the presence of alumino and silicooxygen tetrahedral rings in the zeolite structure. Furthermore, the catalytic activities of the Mn(II) adsorbed zeolites for the disproportionation of hydrogen peroxide were investigated in the presence of imidazole. The Mn(II) adsorbed zeolites display efficiency in the disproportion reactions of hydrogen peroxide, producing water and dioxygen in catalase-like activity.

?içek, Ekrem; Dede, Bülent

2013-12-01

359

Immobilization of catalase onto chitosan and cibacron blue F3GA attached chitosan beads  

E-print Network

In this study, chitosan beads (Ch-bead) and cibacron blue F3GA attached chitosan beads (CB-Ch-bead) were prepared. Their characteristics were investigated with experiments of swelling, thermogravimetric analysis and Fourier transform infrared (FTIR) spectroscopic analysis. Catalase (CAT) was immobilized onto these beads. The adsorption isotherms have a Langmuirian shape for Ch-beads and CB-Ch-beads. The CAT adsorption capacity of Ch-beads is higher than that of CB-Ch-beads, but CB-Ch-CAT showed better activity according to the Ch-CAT. The values of apparent Km were found to be 18 and 41 mM for Ch-CAT and CB-Ch-CAT, respectively. However, Vmax values were calculated as 4800 and 14,250 ?mol (mg protein) ?1 min ?1 for Ch-CAT and CB-Ch-CAT, respectively. Furthermore, various characteristics of immobilized catalase, such as the temperature profile, thermal stability, optimum pH, operational stability and storage stability were evaluated. Optimum temperature and optimum pH values were found as 35 ? C and 7.0 for maximum activity of Ch-CAT and CB-Ch-CAT. It was observed that thermal, storage and operational stabilities of the enzyme were increased with immobilization.

S¸enay Akkus Çetinus A; H. Nursevin Öztop A; Dursun Sarayd?n B

2007-01-01

360

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. PMID:21449849

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

361

Ability of recombinant human catalase to suppress inflammation of the murine lung induced by influenza A.  

PubMed

Influenza A virus pandemics and emerging antiviral resistance highlight the urgent need for novel generic pharmacological strategies that reduce both viral replication and inflammation of the lung. We have previously investigated the therapeutic efficacy of recombinant human catalase (rhCAT) against viral pneumonia in mice, but the protection mechanisms involved were not explored. In the present study, we have performed a more in-depth analysis covering survival, lung inflammation, immune cell responses, production of cytokines, and inflammation signaling pathways in mice. Male imprinting control region mice were infected intranasally with high pathogenicity (H1N1) influenza A virus followed by treatment with recombinant human catalase. The administration of rhCAT resulted in a significant reduction in inflammatory cell infiltration (e.g., macrophages and neutrophils), inflammatory cytokine levels (e.g., IL-2, IL-6, TNF-?, IFN-?), the level of the intercellular adhesion molecule 1 chemokine and the mRNA levels of toll-like receptors TLR-4, TLR-7, and NF-?B, as well as partially maintaining the activity of the antioxidant enzymes system. These findings indicated that rhCAT might play a key protective role in viral pneumonia of mice via suppression of inflammatory immune responses. PMID:24385240

Shi, Xunlong; Shi, Zhihui; Huang, Hai; Zhu, Hongguang; Zhou, Pei; Zhu, Haiyan; Ju, Dianwen

2014-06-01

362

A bifunctional enzyme from Rhodococcus erythropolis exhibiting secondary alcohol dehydrogenase-catalase activities.  

PubMed

Alcohol dehydrogenases have long been recognized as potential biocatalyst for production of chiral fine and bulk chemicals. They are relevant for industry in enantiospecific production of chiral compounds. In this study, we identified and purified a nicotinamide adenine dinucleotide (NAD)-dependent secondary alcohol dehydrogenase (SdcA) from Rhodococcus erythropolis oxidizing ?-lactols into ?-lactones. SdcA showed broad substrate specificity on ?-lactols; secondary aliphatic alcohols with 8 and 10 carbon atoms were also substrates and oxidized with (2S)-stereospecificity. The enzyme exhibited moderate stability with a half-life of 5 h at 40 °C and 20 days at 4 °C. Mass spectrometric identification revealed high sequence coverage of SdcA amino acid sequence to a highly conserved catalase from R. erythropolis. The corresponding encoding gene was isolated from genomic DNA and subsequently overexpressed in Escherichia coli BL21 DE3 cells. In addition, the recombinant SdcA was purified and characterized in order to confirm that the secondary alcohol dehydrogenase and catalase activity correspond to the same enzyme. PMID:24846734

Martinez-Rojas, Enriqueta; Kurt, Tutku; Schmidt, Udo; Meyer, Vera; Garbe, Leif-Alexander

2014-11-01

363

Genes Up-Regulated in Tolerant Cavendish Banana Roots in Response to Fusarium oxysporum f. sp. cubense Infection1  

E-print Network

Programme, Scottish Crop Research Institute, Invergowrie, Dundee, DD2 5DA, UK Keywords: catalase, defence-associated genes (catalase 2, pectin acetyl esterase (PAE), PR-1 and PR-3) were selected for expression profile, xylanase inhibitor, peroxidase, catalase 2, metallothionein, response regulator 6 and tripsin inhibitor

364

Expression of the catalase gene katA in starter culture Lactobacillus plantarum TISTR850 tolerates oxidative stress and reduces lipid oxidation in fermented meat product  

Microsoft Academic Search

The catalase gene katA of Lactobacillus sakei SR911 was cloned and expressed in Escherichia coli UM2 and Lactobacillus plantarum TISTR850 under strong lactococcal promoter P59 in E. coli–lactococcus expression vector pIL1020. The L. plantarum TISTR850 is a catalase-deficient strain isolated from local fermented meat product. The recombinant L. plantarum TISTR850 was shown to decompose hydrogen peroxide, and catalase activity approximately

W Noonpakdee; S Sitthimonchai; S Panyim; S Lertsiri

2004-01-01

365

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

366

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

367

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

2013-10-15

368

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. PMID:20697694

Oliveira, Jose Henrique M.; Nogueira, Eduardo M.; Guedes, Helma V.; Oliveira, Pedro L.; Camara, Fernando; Baldani, Jose I.; Martins, Orlando B.

2010-01-01

369

Up-Regulated Expression of AOS-LOXa and Increased Eicosanoid Synthesis in Response to Coral Wounding  

PubMed Central

In octocorals, a catalase–like allene oxide synthase (AOS) and an 8R-lipoxygenase (LOX) gene are fused together encoding for a single AOS-LOX fusion protein. Although the AOS-LOX pathway is central to the arachidonate metabolism in corals, its biological function in coral homeostasis is unclear. Using an acute incision wound model in the soft coral Capnella imbricata, we here test whether LOX pathway, similar to its role in plants, can contribute to the coral damage response and regeneration. Analysis of metabolites formed from exogenous arachidonate before and after fixed time intervals following wounding indicated a significant increase in AOS-LOX activity in response to mechanical injury. Two AOS-LOX isoforms, AOS-LOXa and AOS-LOXb, were cloned and expressed in bacterial expression system as active fusion proteins. Transcription levels of corresponding genes were measured in normal and stressed coral by qPCR. After wounding, AOS-LOXa was markedly up-regulated in both, the tissue adjacent to the incision and distal parts of a coral colony (with the maximum reached at 1 h and 6 h post wounding, respectively), while AOS-LOXb was stable. According to mRNA expression analysis, combined with detection of eicosanoid product formation for the first time, the AOS-LOX was identified as an early stress response gene which is induced by mechanical injury in coral. PMID:24551239

Lohelaid, Helike; Teder, Tarvi; Toldsepp, Kadri; Ekins, Merrick; Samel, Nigulas

2014-01-01

370

A kinetic method for para -nitrophenol determination based on its inhibitory effect on the catalatic reaction of catalase  

Microsoft Academic Search

The inhibitory effect of para-nitrophenol on the catalytic reaction of catalase was investigated. Michaelis-Menten kinetic parameters were determined from\\u000a Lineweaver-Burk plots obtained in the absence or in the presence of the inhibitor. The inhibitor pattern, revealed by the\\u000a Lineweaver-Burk plots, suggested a fully mixed inhibition mechanism. Spectrophotometric monitoring of the indicator reaction:\\u000a $$H_2 O_2 \\\\xrightarrow{{catalase,para - nitrophenol}}H_2 O + \\\\tfrac{1}{2}O_2

Claudia Mure?anu; Lucian Copolovici; Florina Pogùacean

2005-01-01

371

Structural analysis of compound I in hemoproteins: study on Proteus mirabilis catalase.  

PubMed

Ferryl catalysis has attracted considerable interest, because a diverse variety of enzymes use ferryl intermediates to perform difficult chemistry. The structure of the reactional intermediate compound I of Proteus mirabilis catalase (PMC) has been solved using time-resolved X-ray diffraction techniques and single crystal microspectrophotometry. Formation of compound I is characterized by significant changes in the absorbance spectrum, and the creation of an oxoferryl group on the distal side of the heme. This group is clearly visible in the X-ray electron density maps. An unidentified electron density, likely to be an anion because of the nature of its environment, appears during the reaction, in a site distant from the heme. The structure of compound I in PMC is compared with that of compound I in cytochrome c peroxidase (CCP). PMID:9479449

Jouve, H M; Andreoletti, P; Gouet, P; Hajdu, J; Gagnon, J

1997-11-01

372

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

373

Catalase-positive microperoxisomes in rat soleus and extensor digitorum longus muscle fiber types  

NASA Technical Reports Server (NTRS)

The size, distribution, and content of catalase-reactive microperoxisomes were investigated cytochemically in three types of muscle fibers from the soleus and the extensor digitorum longus (EDL) of male rats. Muscle fibers were classified on the basis of the mitochondrial content and distribution, the Z-band widths, and the size and shape of myofibrils as the slow-twitch oxidative (SO), the fast-twitch oxidative glycolytic (FOG), and the fast-twitch glycolytic (FG) fibers. It was found that both the EDL and soleus SO fibers possessed the largest microperoxisomes. A comparison of microperoxisome number per muscle fiber area or the microperoxisome area per fiber area revealed following ranking, starting from the largest number and the area-ratio values: soleus SO, EDL SO, EDL FOG, and EDL FG.

Riley, Danny A.; Bain, James L. W.; Ellis, Stanley

1988-01-01

374

Predominant Catalase-negative Soil Bacteria. II. Occurrence and Characterization of Actinomyces humiferus, sp. N1  

PubMed Central

A microorganism resembling an Actinomyces species was found to be a numerically predominant inhabitant of various organically rich soils. This organism forms a hyphal-like structure with true branching that fragments into gram-positive diphtheroid and coccoid elements. Its cells ferment carbohydrates and contain both lysine and ornithine as the major basic amino acids of the cell wall. It is catalase-negative, microaerophilic to aerobic, and sensitive to lysozyme, and it is dependent on an organic nitrogen source and incubation at 30 C for optimum growth. Based on these characteristics, a new species, Actinomyces humiferus, is proposed. The ecological and medical implications of a large soil population of this microorganism are discussed. Images PMID:5803624

Gledhill, William E.; Casida, L. E.

1969-01-01

375

Sixty years from discovery to solution: crystal structure of bovine liver catalase form III  

SciTech Connect

The crystallization and structural characterization of bovine liver catalase (BLC) has been intensively studied for decades. Forms I and II of BLC have previously been fully characterized using single-crystal X-ray diffraction. Form III has previously been analyzed by electron microscopy, but owing to the thinness of this crystal form an X-ray crystal structure had not been determined. Here, the crystal structure of form III of BLC is presented in space group P212121, with unit-cell parameters a = 68.7, b = 173.7, c = 186.3 {angstrom}. The asymmetric unit is composed of the biological tetramer, which is packed in a tetrahedron motif with three other BLC tetramers. This higher resolution structure has allowed an assessment of the previously published electron-microscopy studies.

Foroughi, Leila M.; Kang, You-Na; Matzger, Adam J. (Michigan)

2012-03-27

376

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. PMID:13936221

Mossel, D. A. A.

1962-01-01

377

Catalase ameliorates polychlorinated biphenyl-induced cytotoxicity in non-malignant human breast epithelial cells  

PubMed Central

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 non-malignant 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, 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 pre-treated 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.

2008-01-01

378

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

379

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

380

Original Contribution The induction of human superoxide dismutase and catalase in vivo: A fundamentally new approach to antioxidant therapy  

Microsoft Academic Search

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

Sally K. Nelson; Swapan K. Bose; Gary K. Grunwald; Paul Myhill; Joe M. McCord

381

The induction of human superoxide dismutase and catalase in vivo: A fundamentally new approach to antioxidant therapy  

Microsoft Academic Search

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

Sally K. Nelson; Swapan K. Bose; Gary K. Grunwald; Paul Myhill; Joe M. McCord

2006-01-01

382

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

383

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

384

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

385

Inhibition of peroxidase and catalase activities and modulation of hydrogen peroxide level by inositol phosphoglycan-like compounds.  

PubMed

Inositol phosphoglycan-like compounds are produced by the hydrolysis of the membrane bound glycosyl phosphoinositides. Besides being short term mediators of insulin action, they inhibit peroxidases and catalase, increasing the concentration of cellular hydrogen peroxide. Although high concentrations of hydrogen peroxide are toxic, moderate increases of its basal level are signals for different metabolic pathways. The inhibitor, localized in the cytosol of the cell, acts on peroxidases and catalase of the same tissue (homologous action) and of other tissues or organisms (heterologous action). The inositol phosphoglycan-like compound inhibits peroxidases with different prosthetic groups, i.e. containing iron such as: thyroid peroxidase, lactoperoxidase, horseradish peroxidase, soy bean peroxidase; and containing selenium such as glutathione peroxidase and 2-cys peroxiredoxin with no prosthetic group. Besides peroxidases, the inositol phosphoglycan-like compound inhibits catalase, another heme enzyme. The inhibition kinetics demonstrates a noncompetitive effect. The site of action is not the prosthetic group, given that the inhibitor does not produce any effect on the peak in the Soret region in the presence or absence of hydrogen peroxide. In conclusion, the inositol phosphoglycan-like compound is the general inhibitor of peroxidases and catalase involved in the modulation of hydrogen peroxide level that acts in different metabolic pathways as a signal transducer. PMID:17226108

Thomasz, L; Aran, M; Pizarro, R A; Ibañez, J; Pisarev, M A; Converso, D; Juvenal, G J; Krawiec, L

2007-01-01

386

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

387

Isolation of a Novel Peroxisomal Catalase Gene from Sugarcane, Which Is Responsive to Biotic and Abiotic Stresses  

PubMed Central

Catalase is an iron porphyrin enzyme, which serves as an efficient scavenger of reactive oxygen species (ROS) to avoid oxidative damage. In sugarcane, the enzymatic activity of catalase in a variety (Yacheng05–179) resistant to the smut pathogen Sporisorium scitamineum was always higher than that of the susceptible variety (Liucheng03–182), suggesting that catalase activity may have a positive correlation with smut resistance in sugarcane. To understand the function of catalase at the molecular level, a cDNA sequence of ScCAT1 (GenBank Accession No. KF664183), was isolated from sugarcane infected by S. scitamineum. ScCAT1 was predicted to encode 492 amino acid residues, and its deduced amino acid sequence shared a high degree of homology with other plant catalases. Enhanced growth of ScCAT1 in recombinant Escherichia coli Rosetta cells under the stresses of CuCl2, CdCl2 and NaCl indicated its high tolerance. Q-PCR results showed that ScCAT1 was expressed at relatively high levels in the bud, whereas expression was moderate in stem epidermis and stem pith. Different kinds of stresses, including S. scitamineum challenge, plant hormones (SA, MeJA and ABA) treatments, oxidative (H2O2) stress, heavy metal (CuCl2) and hyper-osmotic (PEG and NaCl) stresses, triggered a significant induction of ScCAT1. The ScCAT1 protein appeared to localize in plasma membrane and cytoplasm. Furthermore, histochemical assays using DAB and trypan blue staining, as well as conductivity measurement, indicated that ScCAT1 may confer the sugarcane immunity. In conclusion, the positive response of ScCAT1 to biotic and abiotic stresses suggests that ScCAT1 is involved in protection of sugarcane against reactive oxidant-related environmental stimuli. PMID:24392135

Ling, Hui; Chen, Shanshan; Wang, Shanshan; Xu, Liping; Allan, Andrew C.; Que, Youxiong

2014-01-01

388

Cardiac-Specific Overexpression of Catalase Attenuates Paraquat-Induced Myocardial Geometric and Contractile Alteration: Role of ER Stress  

PubMed Central

Paraquat, a quarternary nitrogen herbicide, is a highly toxic prooxidant resulting in multi-organ failure including 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 H2O2, on paraquat-induced myocardial geometric and functional alterations, with a focus on ER stress. FVB and catalase transgenic mice were administrated paraquat for 48 hrs. 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 LV end-diastolic and systolic diameters, increased LV mass and resting myocyte length, reduced fractional shortening, cardiomyocyte peak shortening, maximal velocity of shortening/relengthening and prolonged relengthening duration in FVB group. While 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 phosphorylation of JNK, IRE1? and eIF2?, all were ablated by 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 via alleviating JNK-mediated ER stress. PMID:20937379

Ge, We; Zhang, Yingmei; Han, Xuefeng; Ren, Jun

2010-01-01

389

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

390

Potential toxicity of sarafloxacin to catalase: spectroscopic, ITC and molecular docking descriptions.  

PubMed

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. PMID:23871971

Cao, Zhaozhen; Liu, Rutao; Yang, Bingjun

2013-11-01

391

Antioxidant effects of black rice extract through the induction of superoxide dismutase and catalase activities.  

PubMed

Our ex vivo study revealed that BRE had significantly stronger ability to inhibit LDL oxidation than white rice extract (WRE). The purpose of this study was to investigate whether black rice extract (BRE) supplementation might ameliorate oxidative stress and enhance antioxidant enzyme activities in HepG2 cells and in C57BL/6 mice. In the cellular study, superoxide anions (O2*-) and reactive oxygen species (ROS) in the BRE group were significantly suppressed. The BRE group also showed significant increases in superoxide dismutase (SOD) and catalase (CAT) activities by 161.6% and 73.4%, respectively. The major components responsible for the free-radical-scavenging and antioxidative properties might be cyanidin-3-O-glucoside chloride and peonidin-3-O-glucuside chloride. In the animal study, male C57BL/6 mice were divided into three groups (control, BRE, and WRE). Plasma HDL-cholesterol was significantly higher, and thiobarbituric, acid-reactive substances were significantly lower in the BRE group, whereas plasma levels of total cholesterol and triglyceride were not affected by BRE supplementation. Increased hepatic SOD and CAT activities were observed in BRE-treated mice as compared to the control mice. However, no changes were detected for the protein expression of antioxidant enzymes by Western blot analysis. Our data suggest that antioxidative effects exerted by BRE are mediated through decreases in free-radical generation as well as increases in SOD and CAT activities both in vitro and in vivo. PMID:17120934

Chiang, An-Na; Wu, Hua-Lin; Yeh, Hung-I; Chu, Chi-Shuen; Lin, Hui-Chiao; Lee, Wei-Chin

2006-08-01

392

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

393

The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals.  

PubMed

Electron beam damage is the fundamental limit to resolution in electron cryomicroscopy (cryo-EM) of frozen, hydrated specimens. Radiation damage increases with the number of electrons used to obtain an image and affects information at higher spatial frequencies before low-resolution information. For the experimentalist, a balance exists between electron exposures sufficient to obtain a useful signal-to-noise ratio (SNR) in images and exposures that limit the damage to structural features. In single particle cryo-EM this balance is particularly delicate: low-resolution features must be imaged with a sufficient SNR to allow image alignment so that high-resolution features recorded below the noise level can be recovered by averaging independent images. By measuring the fading of Fourier components from images obtained at 200 kV of thin crystals of catalase embedded in ice, we have determined the electron exposures that will maximize the SNR at resolutions between 86 and 2.9A. These data allow for a rational choice of exposure for single particle cryo-EM. For example, for 20A resolution, the SNR is maximized at approximately 20e(-)/A(2), whereas for 3A resolution, it is maximized at approximately 10 e(-)/A(2). We illustrate the effects of exposure in single particle cryo-EM with data collected at approximately 12-15 and approximately 24-30 e(-)/A(2). PMID:19958834

Baker, Lindsay A; Smith, Eric A; Bueler, Stephanie A; Rubinstein, John L

2010-03-01

394

Analysis of Oxidative Stress Status, Catalase and Catechol-O-Methyltransferase Polymorphisms in Egyptian Vitiligo Patients  

PubMed Central

Vitiligo is the most common depigmentation disorder of the skin. Oxidative stress is implicated as one of the probable events involved in vitiligo pathogenesis possibly contributing to melanocyte destruction. Evidence indicates that certain genes including those involved in oxidative stress and melanin synthesis are crucial for development of vitiligo. This study evaluates the oxidative stress status, the role of catalase (CAT) and catechol-O-Methyltransferase (COMT) gene polymorphisms in the etiology of generalized vitiligo in Egyptians. Total antioxidant capacity (TAC) and malondialdehyde (MDA) levels as well as CAT exon 9 T/C and COMT 158 G/A polymorphisms were determined in 89 patients and 90 age and sex-matched controls. Our results showed significantly lower TAC along with higher MDA levels in vitiligo patients compared with controls. Meanwhile, genotype and allele distributions of CAT and COMT polymorphisms in cases were not significantly different from those of controls. Moreover, we found no association between both polymorphisms and vitiligo susceptibility. In conclusion, the enhanced oxidative stress with the lack of association between CAT and COMT polymorphisms and susceptibility to vitiligo in our patients suggest that mutations in other genes related to the oxidative pathway might contribute to the etiology of generalized vitiligo in Egyptian population. PMID:24915010

Mehaney, Dina A.; Darwish, Hebatallah A.; Hegazy, Rehab A.; Nooh, Mohammed M.; Tawdy, Amira M.; Gawdat, Heba I.; El-Sawalhi, Maha M.

2014-01-01

395

Flavonoid-induced conversion of catalase to its inactive form-Compound II.  

PubMed

Abstract Flavonoids (FlaOHs), plant polyphenols, are ubiquitous components of human diet and are known as antioxidants. However, their prooxidant activity has also been reported. We have recently found that FlaOHs inhibit catalase, the heme enzyme which catalyzes the decomposition of hydrogen peroxide (H2O2) into water and molecular oxygen. The catalytic cycle proceeds with the formation of the intermediate, Compound I (Cpd I), an oxoferryl porphyrin ?-cation radical, the two-electron oxidation product of a heme group. Under conditions of low H2O2 fluxes and in the presence of an appropriate substrate, Cpd I can undergo one-electron reduction to inactive Compound II (Cpd II), oxoferryl derivative without radical site. Here we show that in vitro, under low fluxes of H2O2, FlaOHs reduce Cpd I to inactive Cpd II. Measurable amounts of Cpd II can be formed even in the presence of reduced nicotinamide adenine dinucleotide phosphate (NADPH) at concentration comparable with the investigated FlaOHs. Possible mechanisms of electron transfer from FlaOH molecule to the heme are discussed. PMID:25111015

Krych, J; Gebicki, J L; Gebicka, L

2014-11-01

396

Effect of salts and organic solvents on the activity of Halobacterium cutirubrum catalase.  

PubMed

Catalase in extracts of the extreme halophile Halobacterium cutirubrum exhibits up to threefold stimulation by 0.5 to 1.5 m monovalent salts and by 0.1 m divalent salts. Above these concentrations, inhibition of enzyme activity is observed. The inhibitory effect, and to some extent the stimulation, is salt-specific; the effectiveness of a salt in inhibiting enzyme activity depends on both cation and anion. Thus, the order of effectiveness is MgCl(2) > LiCl > NaCl > KCl > NH(4)Cl, and LiCl > LiNO(3) > Li(2)SO(4). The magnitude of enzyme inhibition for the salts tested is positively correlated with their molar vapor pressure depression in aqueous solution. Stimulation of enzyme activity was observed when one salt was added at its optimal concentration in the presence of inhibiting concentrations of another salt, indicating that the effect on the enzyme is not due to changing water activity but probably to enzyme-salt interaction. Aqueous solutions of ethylene glycol, glycerol, and dimethyl sulfoxide containing no ions influence enzyme activity in the same manner as do salts. PMID:5784214

Lanyi, J K; Stevenson, J

1969-05-01

397

Mechanism of manganese catalase peroxide disproportionation: determination of manganese oxidation states during turnover.  

PubMed

X-ray absorption near-edge structure (XANES) spectroscopy has been used to determine the oxidation state composition of the Mn site in Mn catalase under turnover conditions. The XANES data are consistent with parallel assignments based on electron paramagnetic resonance (EPR). However, a major advantage of the XANES assignments is that they permit the direct determination of the average oxidation states for derivatives that are EPR silent. In agreement with earlier work [Khangulov, S. V., Barynin, V. V., & Antonyuk-Barynina, S. V. (1990) Biochim. Biophys. Acta 1020, 25-33], these data show that the binuclear Mn site is reduced to Mn(II)/Mn(II) when peroxide is added in the presence of halide inhibitors. In addition, the present data provide the first direct evidence that the reduced enzyme is oxidized if peroxide is added in the absence of inhibitors. Under turnover conditions, the enzyme contains approximately a 2:1 ratio of Mn(II) and Mn(III). Similar results are obtained following incubation with dioxygen. These results are consistent with a Mn(II)/Mn(II)<==>Mn(III)/Mn(III) catalytic cycle and demonstrate that halide inhibition involves trapping the enzyme in the reduced state. PMID:7849009

Waldo, G S; Penner-Hahn, J E

1995-02-01

398

Bioaccumulation of fullerene (C60) and corresponding catalase elevation in Lumbriculus variegatus.  

PubMed

Fullerene (C(60)), with its unique physical properties and nanometer size, has been mass-produced for many applications in recent decades. The increased likelihood of direct release into the environment has raised interest in understanding both the environmental fate and corresponding biological effects of fullerenes to living organisms. Because few studies have emphasized fullerene uptake and resulting biochemical responses by living organisms, a toxicity screening test and a 28-d bioaccumulation test for Lumbriculus variegatus were performed. No mortality was observed in the range of 0.05?mg?C(60) /kg dry sediment to 11.33?mg?C(60) /kg dry sediment. A biota-sediment accumulation factor of micron-sized fullerene agglomerates (µ-C(60)) was 0.032?±?0.008 at day 28, which is relatively low compared with pyrene (1.62?±?0.22). Catalase (CAT) activity, an oxidative stress indicator, was elevated significantly on day 14 for L. variegatus exposed to µ-C(60) (p?=?0.034). This peak CAT activity corresponded to the highest body residues observed in the present study, 199?±?80?µg?C(60) /kg dry weight sediment. Additionally, smaller C(60) agglomerate size increased bioaccumulation potential in L. variegatus. The relationship between C(60) body residue and the increased CAT activity followed a linear regression. All results suggest that C(60) has a lower bioaccumulation potential than pyrene but a higher potential to induce oxidative stress in L. variegatus. PMID:24477927

Wang, Jiafan; Wages, Mike; Yu, Shuangying; Maul, Jonathan D; Mayer, Greg; Hope-Weeks, Louisa; Cobb, George P

2014-05-01

399

Purification and properties of goat liver catalase: two pH optima.  

PubMed

Goat liver catalase (EC 1.11.1.6) has been purified to homogeneity using the techniques of ammonium sulfate fractionation, DEAE-cellulose chromatography and gel-filtration through Ultrogel AcA-34 involving two alternating steps of column chromatography. The homogeneity of the purified enzyme was tested by native and sodium dodecyl sulfate polyacrylamide gel electrophoresis, immunodiffusion and immunoelectrophoresis. The enzyme is a tetramer having a subunit molecular weight of 58,000 +/- 3000, contains six sulfhydryl groups per mole of the enzyme and shows pH optima at pH 6.8 and 7.7. The kinetic data show no cooperativity between the substrate binding sites. Tryptophan, indoleacetic acid, cysteine, formaldehyde and sodium azide inhibit the enzyme non-competitively with Ki values of 4 +/- 1, 2.5 +/- 0.8, 6 +/- 1.5, 0.48 +/- 0.15 and 0.0013 +/- 0.0003 mM, respectively. Sulfhydryl group binding agents as well as thiol reagents inhibit the enzyme activity. PMID:2620909

Chatterjee, U; Kumar, A; Sanwal, G G

1989-06-01

400

Spin Trapping Investigation of Peroxide- and Isoniazid-Induced Radicals in Mycobacterium tuberculosis Catalase-Peroxidase†  

PubMed Central

A new approach, the immuno-spin trapping assay, used a novel rabbit polyclonal anti-DMPO (5,5-dimethyl-1-pyrroline N-oxide) antiserum to detect protein radical-derived DMPO nitrone adducts in the hemoprotein Mycobacterium tuberculosis catalase-peroxidase (KatG). This work demonstrates that the formation of protein nitrone adducts is dependent on the concentrations of tert-BuOOH and DMPO as shown by Western blotting and an enzyme-linked immunosorbent assay (ELISA). We have also detected protein-protein cross-links formed during turnover of Mtb KatG driven by tert-butyl peroxide (tert-BuOOH) or enzymatic generation of hydrogen peroxide. DMPO inhibits this dimerization due to its ability to trap the amino acid radicals responsible for the cross-linkage. Chemical modifications by tyrosine and tryptophan blockage suggest that tyrosine residues are one site of formation of the dimers. The presence of the tuberculosis drug isoniazid (INH) also prevented cross-linking as a result of its competition for the protein radical. Protein-DMPO nitrone adducts were also generated by a continuous flux of hydrogen peroxide. These findings demonstrated that the protein-based radicals were formed not only during Mtb KatG turnover with alkyl peroxides but also in the presence of hydrogen peroxide. Furthermore, the formation of protein-DMPO nitrone adducts was accelerated in the presence of isoniazid. PMID:18831539

Ranguelova, Kalina; Suarez, Javier; Magliozzo, Richard S.; Mason, Ronald P.

2009-01-01

401

The periplasmic, group III catalase of Vibrio fischeri is required for normal symbiotic competence and is induced both by oxidative stress and approach to stationary phase  

E-print Network

The catalase gene, katA, of the sepiolid squid symbiont Vibrio fischeri has been cloned and sequenced. The predicted amino acid sequence of KatA has a high degree of similarity to the recently defined group III catalases, including those found in Haemophilus influenzae, Bacteroides fragilis, and Proteus mirabilis. Upstream of the predicted start codon of katA is a sequence that closely matches the consensus sequence for promoters regulated in Escherichia coli by the alternative sigma factor encoded by rpoS. Further, the level of expression of the cloned katA gene in an E. coli rpoS mutant is much lower than in wild-type E. coli. Catalase activity is induced three- to fourfold both as growing V. fischeri cells approach stationary phase and upon the addition of a small amount of hydrogen peroxide during logarithmic growth. The catalase activity was localized in the periplasm of wild-type V. fischeri cells, where its role could be to detoxify hydrogen peroxide coming from the external environment. No significant catalase activity could be detected in a katA null mutant strain, demonstrating that KatA is the predominately expressed catalase in V. fischeri and indicating that V. fischeri carries only a single catalase gene. The catalase mutant was defective in its ability to competitively colonize the light organs of juvenile squids in coinoculation experiments with the parent strain, suggesting that the catalase enzyme plays an important role in the symbiosis between V. fischeri and its squid host. The luminous marine bacterium Vibrio fischeri occupies a

Karen L. Visick; Edward; G. Ruby

1998-01-01

402

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

2009-05-01

403

Dynamics of erythrocyte count, hemoglobin, and catalase activity in rat blood in hypokinesia, muscular activity and restoration  

NASA Technical Reports Server (NTRS)

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 increased with an increase in the duration of swimming, but only up to 6 hr; with 7-9 hr of swimming as well as in hypodynamia, catalase activity decreased. It was also observed that under hypodynamia as well as in 3, 5 and 6 hr exertion (swimming) the color index of blood decreased. Pressure chamber treatment (for 8 min each day for one week), alternating a 2 min negative pressure up to 35 mm Hg with 1 min positive pressure, increased the erythrocyte count and hemoglobin content.

Taneyeva, G. V.; Potapovich, G. M.; Voloshko, N. A.; Uteshev, A. B.

1980-01-01

404

Targeting of human catalase to peroxisomes is dependent upon a novel COOH-terminal peroxisomal targeting sequence  

E-print Network

Abstract. 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

P. Edward Purdue; Paul B. Lazarow

1996-01-01

405

Effects of Single-Dose Ultraviolet Radiation on Skin Superoxide Dismutase, Catalase, and Xanthine Oxidase in Hairless Mice  

Microsoft Academic Search

The effects of a single exposure to UVB radiation on skin antioxidant enzymes and superoxide-generating xanthine oxidase were examined in Skh:HR-1 hairless mice. Significant decreases in superoxide dismutase (SOD) and catalase (CAT) were observed by 12 h after UV irradiation and remained depressed for up to 72 h. No induction of xanthine dehydrogenase (XD) or xanthine oxidase (XO) occurred with

Barbara C. Pence; Mark F. Naylor

1990-01-01

406

recA and catalase in H sub 2 O sub 2 -mediated toxicity in Neisseria gonorrhoeae  

SciTech Connect

Neisseria gonorrhoeae cells defective in the biosynthesis of the recA gene product are no more sensitive to hydrogen peroxide than wild-type cells. Although gonococci possess nearly 100-fold-greater catalase levels than Escherichia coli, they are more susceptible to hydrogen peroxide than this organism. The natural niche of gonococci undoubtedly results in exposure to oxidant stress; however, they do not demonstrate particularly efficient antioxidant defense systems.

Hassett, D.J.; Charniga, L.; Cohen, M.S. (Univ. of North Carolina, Chapel Hill (USA))

1990-12-01

407

Response of peroxidase and catalase to acid rain stress during seed germination of rice, wheat, and rape  

Microsoft Academic Search

Seed germination of plants with various acid-resistance display different responses to acid rain. To understand the reason\\u000a why such differences occur, the effects of simulated acid rain (pH 2.5–5.0) on the activities of peroxidase (POD) and catalase\\u000a (CAT) during seed germination of rice (O. sativa), wheat (T. aestivum), and rape (B. chinensis var. oleifera) were investigated. Results indicated that the

Lihong Wang; Xiaohua Huang; Qing Zhou

2008-01-01

408

Transgenic canola plants over-expressing bacterial catalase exhibit enhanced resistance to Peronospora parasitica and Erysiphe polygoni  

Microsoft Academic Search

Transgenic canola (Brassica napus.L) plants express ing the bacterial catalase katE in the chloroplasts were obtained by the Agrobacterium-med iated transformation method. Resistance and susceptibility of the transgenic canola plants were evaluated against the airborne pathogenic fungi, Peronospora parasitica causing downy mildew and Ery siphe polygon causing powdery mildew under artificial infection in the greenhouse. The b ioassays of the

Mohamed El-Awady; E. A. Moghaieb Reda; Waffaa Haggag; S. Youssef

409

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

410

Heme content of recombinant catalase from Psychrobacter sp. T-3 altered by host Escherichia coli cell growth conditions  

Microsoft Academic Search

The catalase gene of Psychrobacter sp. T-3 was cloned, and the gene product (PktA) was overexpressed in Escherichia coli. The specific activity of the purified PktA was slightly lower than that of the native purified enzyme obtained from Psychrobacter sp. T-3. Spectrophotometric measurements of the purified enzymes suggested that the recombinant PktA contains a mixture of heme b and d,

Hideyuki Kimoto; Hidetoshi Matsuyama; Isao Yumoto; Kazuaki Yoshimune

2008-01-01

411

Regulation of Catalase-Peroxidase KatG Is OxyR Dependent and Fur Independent in Caulobacter crescentus?  

PubMed Central

Most organisms that grow in the presence of oxygen possess catalases and/or peroxidases, which are necessary for scavenging the H2O2 produced by aerobic metabolism. In this work we investigate the pathways that regulate the Caulobacter crescentus katG gene, encoding the only enzyme with catalase-peroxidase function in this bacterium. The transcriptional start site of the katG gene was determined, showing a short 5? untranslated region. The katG regulatory region was mapped by serial deletions, and the results indicate that there is a single promoter, which is responsible for induction at stationary phase. An oxyR mutant strain was constructed; it showed decreased katG expression, and no KatG protein or catalase-peroxidase activity was detected in stationary-phase cell extracts, implying that OxyR is the main positive regulator of the C. crescentus katG gene. Purified OxyR protein bound to the katG regulatory region between nucleotides ?42 and ?91 from the transcription start site, as determined by a DNase I footprinting assay, and a canonical OxyR binding site was found in this region. Moreover, OxyR binding was shown to be redox dependent, given that only oxidized proteins bound adjacent to the ?35 sequence of the promoter and the katG P1 promoter was activated by OxyR in an H2O2-dependent manner. On the other hand, this work showed that the iron-responsive regulator Fur does not regulate C. crescentus katG, since a fur mutant strain presented wild-type levels of katG transcription and catalase-peroxidase production and activity, and the purified Fur protein was not able to bind to the katG regulatory region. PMID:21257767

Italiani, Valeria C. S.; da Silva Neto, Jose F.; Braz, Vania S.; Marques, Marilis V.

2011-01-01

412

Cloning, expression and physiological analysis of broccoli catalase gene and Chinese cabbage ascorbate peroxidase gene under heat stress  

Microsoft Academic Search

The objectives of this work were to clone the catalase (CAT) gene from broccoli (Brassica oleracea) and the ascorbate peroxidase (APX) gene from Chinese cabbage and measure the regulation of CAT and APX gene expressions\\u000a under heat-stress conditions. Different genotypes responded differently to heat stress according to their various antioxidant\\u000a enzymes and physiological parameters. CAT and APX gene expression profiles

Kuan-Hung Lin; Ho-Chang Huang; Ching-Yun Lin

2010-01-01

413

Direct voltammetry of catalase immobilized on silica sol–gel and cysteine modified gold electrode and its application  

Microsoft Academic Search

The direct voltammetry of catalase (CAT) immobilized in silica sol–gel film in the presence of cysteine on gold electrode was investigated. The CAT electrode showed a pair of well-defined and quasi-reversible cyclic voltammetry peaks. It can be used as an electrochemical biosensor for the determination of hydrogen peroxide. The calibration range of H2O2 was from 1 to 30?molL?1 and the

Junwei Di; Min Zhang; Kaian Yao; Shuping Bi

2006-01-01

414

Synthesis conditions for encapsulating cytochrome c and catalase in SiO 2 sol-gel materials  

Microsoft Academic Search

The encapsulation of biological molecules in sol-gel materials has led to the development of a new class of chemical and biomedical sensors. The influence of sol-gel synthesis conditions on the stability, chemical function, and enzymatic reactivity for horse heart cytochrome c and bovine liver catalase encapsulated in silica sol-gel materials was studied. The effects of synthesis pH, alcohol\\/alkoxide ratio, and

J. M. Miller; B. Dunn; J. S. Valentine; J. I. Zink

1996-01-01

415

Catalase in fluvial biofilms: a comparison between different extraction methods and example of application in a metal-polluted river  

Microsoft Academic Search

Antioxidant enzymes are involved in important processes of cell detoxification during oxidative stress and have, therefore,\\u000a been used as biomarkers in algae. Nevertheless, their limited use in fluvial biofilms may be due to the complexity of such\\u000a communities. Here, a comparison between different extraction methods was performed to obtain a reliable method for catalase\\u000a extraction from fluvial biofilms. Homogenization followed

Chloé Bonnineau; Berta Bonet; Natàlia Corcoll; Helena Guasch

2011-01-01

416

Selective peracetic acid determination in the presence of hydrogen peroxide using a label free enzymatic method based on catalase  

Microsoft Academic Search

Peracetic acid (PAA) is selectively determined in the presence of hydrogen peroxide (H2O2) by using the self-indicating UV–Vis molecular absorption properties of catalase. The PAA reacts with the protein giving\\u000a an intermediate (Cat-I) which is reduced back by the aminoacid core surrounding the hemegroup. Since the original form of\\u000a the enzyme and the Cat-I have different UV–Vis absorption properties, the

Javier Galbán; Vanesa Sanz; Susana de Marcos

2010-01-01

417

Peroxidase and catalase changes during in vitro adventitious shoot organogenesis from hypocotyls of Albizia odoratissima L.f. (Benth)  

Microsoft Academic Search

Hypocotyls of Albizia odoratissima cultured on shoot induction medium (MS medium with 7.5 ?M BAP and 0.5 ?M NAA) showed adventitious shoot organogenesis under\\u000a light with 16 h photoperiod. Similar cultures under total darkness produced non-morphogenic calli. The changes in the specific\\u000a peroxidase and catalase activity, total protein content and acidic isoperoxidase pattern were compared between the culture\\u000a showing shoot organogenesis and culture

V. Rajeswari; Kailash Paliwal

2008-01-01

418

High Levels of Catalase and Glutathione Peroxidase Activity Dampen H2O2 Signaling in Human Alveolar Macrophages  

Microsoft Academic Search

Results are presented which support the hypothesis that adequate steady-state levels of hydrogen peroxide (H2O2) are required to overcome the effects of high catalase and glutathione peroxidase (GPx) expression for p38 mitogen-activated protein (MAP) kinase activation and tumor necrosis factor (TNF)- gene expression in human alveolar macrophages stimulated with asbestos. We found significant differences in the types and amounts of

A. Brent Carter; Linda A. Tephly; Sujatha Venkataraman; Larry W. Oberley; Yuping Zhang; Garry R. Buettner; Douglas R. Spitz; Gary W. Hunninghake

2004-01-01

419

cDNA cloning and expression patterns of a peroxiredoxin, a catalase and a glutathione peroxidase from Haemonchus contortus  

Microsoft Academic Search

The range of antioxidant enzyme systems available to Haemonchus contortus for detoxification of hydrogen peroxide was investigated using cDNA cloning of candidate genes. PCR with primers based on conserved amino acid regions and spliced leader sequences was used to obtain full-length sequences for a 2-Cys peroxiredoxin, a catalase, and a selenium-independent glutathione peroxidase, indicating that H. contortus expresses a number

N. H. Bagnall; A. C. Kotze

2004-01-01

420

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

421

Electron pathways in catalase and peroxidase enzymic catalysis. Metal and macrocycle oxidations of iron porphyrins and chlorins  

Microsoft Academic Search

Charge iterative extended Hueckel calculations are presented for compound II, the one-electron oxidation intermediate of horseradish peroxidase (HRP), and for compounds I, the two-electron oxidation transients of HRP and catalase (CAT) observed in the catalytic cycles of the hydroperoxidase enzymes. Compound II is described in terms of a ferryl configuration (O = Fe\\/sup IV\\/), and compounds I are described as

Louise Karle Hanson; Chi K. Chang; Mary S. Davis; Jack Fajer

1981-01-01

422

Induction of New Isoforms of Superoxide Dismutase and Catalase Enzymes in the Flag Leaf of Wheat during Monocarpic Senescence  

Microsoft Academic Search

Leaf senescence is a programmed cell death phenomenon and involves oxidative stress. Superoxide dismutase (SOD, EC 1.15.1.1) and catalase (CAT EC 1.11.1.6) activities were studied in the flag leaf of Triticum aestivum cv. Kundan at different stages of grain development. Both SOD and CAT activities showed a decline during monocarpic senescence. Three SOD isozymes were observed in the cytosol, of

B. Srivalli; Renu Khanna-Chopra

2001-01-01

423

Salicylic acid is a modulator of catalase isozymes in chickpea plants infected with Fusarium oxysporum f. sp. ciceri.  

PubMed

The relationship between salicylic acid level catalases isoforms chickpea cv. ICCV-10 infected with Fusarium oxysporum f. sp. ciceri was investigated. Pathogen-treated chickpea plants showed high levels of SA compared with the control. Two isoforms of catalases in shoot extract (CAT-IS and CAT-IIS) and single isoform in root extract (CAT-R) were detected in chickpea. CAT-IS and CAT-R activities were inhibited in respective extracts treated with pathogen whereas, CAT-IIS activity was not inhibited. These isoforms were purified and their kinetic properties studied in the presence or absence of SA. The molecular mass determined by SDS-PAGE of CAT-IS, CAT-IIS and CAT-R was found to be 97, 40 and 66 kDa respectively. Kinetic studies indicated that Km and V(max) of CAT-IS were 0.2 mM and 300 U/mg, 0.53 mM and 180 U/mg for CAT-IIS and 0.25 mM and 280 U/mg for CAT-R, respectively. CAT-IS and CAT-R were found to be more sensitive to SA and 50% of their activities were inhibited at 6 and 4 ?M respectively, whereas CAT-IIS was insensitive to SA up to 100 ?M. Quenching of the intrinsic tryptophan fluorescence of purified catalases were used to quantitate SA binding; the estimated K(d) value for CAT-IS, CAT-IIS and CAT-R found to be 2.3 ?M, 3.1 mM and 2.8 ?M respectively. SA is a modulator of catalase isozymes activity, supports its role in establishment of SAR in chickpea plants infected with the pathogen. PMID:22245913

Gayatridevi, S; Jayalakshmi, S K; Sreeramulu, K

2012-03-01

424

Ionic-liquid\\/NH 2-MWCNTs as a highly sensitive nano-composite for catalase direct electrochemistry  

Microsoft Academic Search

A nano-composite material consisting of amine functionalized multi-walled carbon nanotubes and a room temperature ionic-liquid (1-butyl-3-methylimidazolium tetrafluoroborate) was prepared and used to construct a novel catalase (Ct) based biosensor for the determination of hydrogen peroxide. The modified electrode exhibited a quasi-reversible cyclic voltammogram corresponding to the Fe(II)\\/Fe(III) redox couple in the heme prosthetic group of Ct with a formal potential

Parvaneh Rahimi; Hossain-Ali Rafiee-Pour; Hedayatollah Ghourchian; Parviz Norouzi; Mohammad Reza Ganjali

2010-01-01

425

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 (CAT), glutathione S-transferase

Anita Jemec; Damjana Drobne; Tatjana Tišler; Kristina Sep?i?

2010-01-01

426

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

427

A catalase-peroxidase from a newly isolated thermoalkaliphilic Bacillus sp. with potential for the treatment of textile bleaching effluents  

Microsoft Academic Search

A new thermoalkaliphilic bacterium was isolated from a textile wastewater drain and identified as a new Bacillus sp. (Bacillus SF). Because of its high pH stability and thermostability, a catalase-peroxidase (CP) from this strain has potential for the treatment of textile bleaching effluents. The CP from Bacillus SF was purified to more than 70.3-fold homogeneity using fractionated ammonium sulfate precipitation,

Marinka Gudelj; Gilbert Fruhwirth; Andreas Paar; Fritz Lottspeich; Karl-Heinz Robra; Artut Cavaco-Paulo; Georg Gübitz

2001-01-01

428

Structural studies of Proteus mirabilis catalase in its ground state, oxidized state and in complex with formic acid.  

PubMed

The structure of Proteus mirabilis catalase in complex with an inhibitor, formic acid, has been solved at 2.3 A resolution. Formic acid is a key ligand of catalase because of its ability to react with the ferric enzyme, giving a high-spin iron complex. Alternatively, it can react with two transient oxidized intermediates of the enzymatic mechanism, compounds I and II. In this work, the structures of native P. mirabilis catalase (PMC) and compound I have also been determined at high resolution (2.0 and 2.5 A, respectively) from frozen crystals. Comparisons between these three PMC structures show that a water molecule present at a distance of 3.5 A from the haem iron in the resting state is absent in the formic acid complex, but reappears in compound I. In addition, movements of solvent molecules are observed during formation of compound I in a cavity located away from the active site, in which a glycerol molecule is replaced by a sulfate. These results give structural insights into the movement of solvent molecules, which may be important in the enzymatic reaction. PMID:14646074

Andreoletti, Pierre; Pernoud, Anaïs; Sainz, Germaine; Gouet, Patrice; Jouve, Hélène Marie

2003-12-01

429

Manganese L-edge X-ray absorption spectroscopy of manganese catalase from Lactobacillus plantarum and mixed valence manganese complexes  

SciTech Connect

The first Mn L-edge absorption spectra of a Mn metalloprotein are presented in this paper. Both reduced and superoxidized Mn catalase have been examined by fluorescence-detected soft X-ray absorption spectroscopy, and their Mn L-edge spectra are dramatically different. The spectrum of reduced Mn(II)Mn(II) catalase has been interpreted by ligand field atomic multiplet calculations and by comparison to model compound spectra. The analysis finds a 10 Dq value of nearly 1.1 eV, consistent with coordination by predominately nitrogen and oxygen donor ligands. For interpretation of mixed valence Mn spectra, an empirical simulation procedure based on the addition of homovalent model compound spectra has been developed and was tested on a variety of Mn complexes and superoxidized Mn catalase. This routine was also used to determine the oxidation state composition of the Mn in [Ba{sub 8}Na{sub 2}ClMn{sub 16}(OH){sub 8}(CO{sub 3}){sub 4}L{sub 8}] .53 H{sub 2}O (L=1,3-diamino-2-hydroxypropane-N,N,N`N`-tetraacetic acid). 27 refs., 6 figs.

Grush, M.M.; Chen, J.; George, S.J. [Univ. of California, Davis, CA (United States)] [and others] [Univ. of California, Davis, CA (United States); and others

1996-01-10

430

Catalase inhibition into the fourth cerebral ventricle affects bradycardic parasympathetic response to increase in arterial pressure without changing the baroreflex.  

PubMed

Exogenous catalase influences neural control of cardiovascular system; however, we do not know yet if its inhibition into the fourth cerebral ventricle (4(th) V) influences baroreflex regulation. We evaluated the effects of central catalase inhibition on baroreflex in conscious Wistar rats. We used males Wistar rats (320-370 g), which were implanted with a stainless steel guide cannula into 4(th) V. The femoral artery and vein were cannulated for mean arterial pressure (MAP) and heart rate (HR) measurement and drug infusion, respectively. After basal MAP and HR recordings, the baroreflex was tested with a pressor dose of phenylephrine (PHE, 8 ?g/kg, bolus) and a depressor dose of sodium nitroprusside (SNP, 50 ?g/kg, bolus). Baroreflex was evaluated before 5, 15, 30 and 60 minutes after 3-amino-1, 2, 4-triazole (ATZ, 0.001 g/100 ?L) injection into the 4(th) V. Vehicle treatment did not change baroreflex responses. ATZ attenuated bradycardic peak and reduced HR range at 30 minutes. ATZ into the 4(th) V reduced bradycardic and tachycardic reflex responses to increase and decrease MAP, respectively (p<0.05) 30 minutes after its microinjection without significantly changing the basal MAP and HR. In conclusion, central catalase inhibition influenced the highest parasympathetic response to MAP increase in conscious Wistar rats without change baroreflex gain. PMID:21425479

Valenti, Vitor E; De Abreu, Luiz Carlos; Sato, Monica A; Fonseca, Fernando L A; Riera, Andrés R Pérez; Ferreira, Celso

2011-03-01

431

The effects of catalase inhibition into the fourth cerebral ventricle on the Bezold-Jarisch reflex in spontaneously hypertensive rats.  

PubMed

Many studies have investigated the role of oxidative stress on cardiovascular system in the brainstem of spontaneously hypertensive rats (SHR). However, we do not know yet if catalase inhibition influences cardiopulmonary reflex (Bezol-Jarisch reflex). Thus, we aimed to evaluate the effects of central catalase inhibition on cardiopulmonary reflex in SHR. Males Wistar Kyoto (WKY) rats and SHR were implanted with a stainless steel guide cannula into the fourth cerebral ventricle (4th V). The femoral artery and vein were cannulated for mean arterial pressure (MAP) and heart rate (HR) measurement and drug infusion, respectively. The cardiopulmonary reflex was tested with phenylbiguanide (PBG, 8 ?g/kg, bolus, i.v.). Cardiopulmonary reflex was evaluated before and 15 minutes after 3-amino-1,2,4-triazole (ATZ, 0.01 g/100 ?L) injection into the 4th V. Vehicle treatment did not change basal MAP and HR and cardiopulmonary reflex responses in SHR and WKY rats. Central ATZ increased hypotensive (p=0.038) responses without influencing the bradycardic reflex (p=0.287) in WKY rats. In SHR, ATZ increased hypotension (p=0.0004) and bradycardic (p=0.04) responses to i.v. PBG. No changes were observed regarding basal MAP and HR after ATZ injection in SHR and WKY rats. We suggest central catalase inhibition affects cardiopulmonary reflex with more intensity in SHR compared to WKY rats. PMID:22262536

Cisternas, José Raul; Valenti, Vitor E; Sato, Monica A; Fonseca, Fernando L A; Saldiva, Paulo H N; De Mello Monteiro, Carlos B; Neto, Modesto Leite Rolim; Rodrigues, Luciano M R; De Abreu, Luiz Carlos

2011-12-01

432

Ethanol injected into the hypothalamic arcuate nucleus induces behavioral stimulation in rats: an effect prevented by catalase inhibition and naltrexone.  

PubMed

It is suggested that some of the behavioral effects of ethanol, including its psychomotor properties, are mediated by beta-endorphin and opioid receptors. Ethanol-induced increases in the release of hypothalamic beta-endorphin depend on the catalasemic conversion of ethanol to acetaldehyde. Here, we evaluated the locomotor activity in rats microinjected with ethanol directly into the hypothalamic arcuate nucleus (ArcN), the main site of beta-endorphin synthesis in the brain and a region with high levels of catalase expression. Intra-ArcN ethanol-induced changes in motor activity were also investigated in rats pretreated with the opioid receptor antagonist, naltrexone (0-2 mg/kg) or the catalase inhibitor 3-amino-1,2,4-triazole (AT; 0-1 g/kg). We found that ethanol microinjections of 64 or 128, but not 256 microg, produced locomotor stimulation. Intra-ArcN ethanol (128 microg)-induced activation was prevented by naltrexone and AT, whereas these compounds did not affect spontaneous activity. The present results support earlier evidence indicating that the ArcN and the beta-endorphinic neurons of this nucleus are necessary for ethanol to induce stimulation. In addition, our data suggest that brain structures that, as the ArcN, are rich in catalase may support the formation of ethanol-derived pharmacologically relevant concentrations of acetaldehyde and, thus be of particular importance for the behavioral effects of ethanol. PMID:18797246

Pastor, Raúl; Aragon, Carlos M G

2008-10-01

433

Combination of heterogeneous catalase and superoxide dismutase protects Bifidobacterium longum strain NCC2705 from oxidative stress.  

PubMed

Bifidobacteria are generally sensitive to oxidative stress caused by reactive oxygen species (ROS). To improve oxidative-stress tolerance, the superoxide dismutase (SOD) gene from Streptococcus thermophilus (StSodA) and the heme-dependent catalase (KAT) gene from Lactobacillus plantarum (LpKatL) were heterologously expressed in Bifidobacterium longum strain NCC2705. Three types of strain NCC2705 transformants were obtained: with transgenic SOD expression, with transgenic KAT expression, and with coexpression of the two genes. Intracellular expression of the genes and their functional role in oxidative-stress resistance were evaluated. In response to oxidative stress, B. longum NCC2705/pDP401-LpKatL (expressing LpKatL) and NCC2705/pDP-Kat-Sod (coexpressing LpKatL and StSodA) rapidly degraded exogenous H2O2 and the peroxides generated as a byproduct of aerobic cultivation, preventing oxidative damage to DNA and RNA. Individual expression of StSodA or LpKatL both improved B. longum NCC2705 cell viability. Survival rate of strain NCC2705 was further improved by combining SOD and KAT expression. The two enzymes played complementary roles in ROS-scavenging pathways, and coexpression led to a synergistic beneficial effect under conditions of intensified oxidative stress. Our results illustrate that heterogeneous expression of heme-dependent KAT and Mn(2+)-dependent SOD is functional in the B. longum oxidative-stress response, and synergistic protection is achieved when their expressions are combined. PMID:24903816

Zuo, Fanglei; Yu, Rui; Feng, Xiujuan; Khaskheli, Gul Bahar; Chen, Lili; Ma, Huiqin; Chen, Shangwu

2014-09-01

434

Synthesis and characterisation of low valent Mn-complexes as models for Mn-catalases.  

PubMed

In this work we report the synthesis of two novel manganese complexes, [L1(3)Mn(II)(6)](ClO(4))(6) (1·(ClO(4))(6)) and [L2Mn(II)(2)(?-OAc)(?-Cl)](ClO(4))(2) (2·(ClO(4))(2)), where L1(2-) is the 2,2'-(1,3-phenylenebis(methylene))bis((2-(bis(pyridin-2-ylmethyl)amino)ethyl)azanediyl)diacetic acid anion and L2 is N1,N1'-(1,3-phenylenebis(methylene))bis(N2,N2'-bis(pyridin-2-ylmethyl)ethane-1,2-diamine). The ligands Na(2)L1 and L2 are built on the same backbone, L2 only contains nitrogen donors, while two carboxylate arms have been introduced in Na(2)L1. The two complexes have been characterized by single-crystal X-ray diffraction, magnetic susceptibility, EPR spectroscopy, and electrochemistry. X-Ray crystallography revealed that 1 is a manganese(II) hexamer and 2 is a manganese(II) dimer featuring an unprecedented mono-?-acetato, mono-?-chlorido bridging motif. The ability of the complexes to catalyse H(2)O(2) disproportionation, thereby acting as models for manganese catalases, has been investigated and compared to the activity of two other related manganese complexes. The introduction of carboxylate donors in the ligands, leading to increased denticity, resulted in a drop in H(2)O(2) disproportionation activity. PMID:20957239

Berggren, Gustav; Huang, Ping; Eriksson, Lars; Styring, Stenbjörn; Anderlund, Magnus F; Thapper, Anders

2010-12-01

435

Application of different molecular techniques for characterization of catalase-positive cocci isolated from sucuk.  

PubMed

This study was carried out for the characterization and discrimination of the indigenous Gram positive, catalase-positive cocci (GCC) population in sucuk, a traditional Turkish dry-fermented sausage. Sucuk samples, produced by the traditional method without starter culture were collected from 8 local producers in Kayseri/Turkey and a total of 116 GCC isolates were identified by using different molecular techniques. Two different molecular fingerprinting methods; namely, randomly amplified polymorphic DNA-PCR (RAPD-PCR) and repetitive extragenic palindrome-PCR (rep-PCR), were used for the clustering of isolates and identification at species level was carried out by full length sequencing of 16S rDNA. Combining the results obtained from molecular fingerprinting and 16S rDNA sequencing showed that the dominant GCC species isolated from the sucuk samples was Staphylococcus saprophyticus followed by Staphylococcus succinus and Staphylococcus equorum belonging to the Staphylococcus genus. Real-time PCR DNA melting curve analysis and high-resolution melting (HRM) analysis targeting the V1 + V3 regions of 16S rDNA were also applied for the discrimination of isolates belonging to different species. It was observed statistically different Tm values and species-specific HRM profiles for all except 2 species (S. saprophyticus and Staphylococcus xylosus) that have high 16S rDNA sequence similarity. The combination of rep-PCR and/or PCR-RAPD with 16S rRNA gene sequencing was an efficient approach for the characterization and identification of the GCC population in spontaneously fermented sucuk. On the other hand, intercalating dye assays were found to be a simple and very promising technique for the differentiation of the GCC population at species level. PMID:24410408

Kesmen, Zülal; Yarimcam, Burcu; Aslan, Hakiye; Ozbekar, Esra; Yetim, Hasan

2014-02-01

436

Biological variability of superoxide dismutase, glutathione peroxidase, and catalase in blood.  

PubMed

We studied the biological variability of blood superoxide dismutase (SOD; EC 1.15.1.1), glutathione peroxidase (GPX; EC 1.11.1.9), and catalase (CAT; EC 1.11.1.6) in a sample of 1836 apparently health subjects, ages 4-97 years. SOD and GPX activities were assayed in plasma (P) and erythrocytes (E) by automated methods, and CAT was measured in erythrocytes by a manual technique. No statistically significant variation of these antioxidant enzyme activities according to gender was demonstrated, except for E-GPX, which was slightly but significantly higher in women than in men (P less than 0.001). Activities appear rather stable in adults less than 65 years old, but decrease for most enzymes in the elderly. There is no evidence that weight, blood pressure, or menopause influences the antioxidant enzymes' activities. In girls ages 10-14 years, E-SOD activity is reduced by 16% (P less than 0.05) after menarche. Variations related to smoking and alcohol consumption are slight and concern only P-SOD and P-GPX, respectively. Conversely, intake of some drugs (e.g., anti-inflammatory agents, antidepressants, and thyroid hormones) modifies activity of some of the three enzymes. E-SOD positively correlates with P-SOD (r = 0.216, P less than 0.001) and E-CAT (r = 0.123, P less than 0.001), and E-GPX with P-GPX (r = 0.218, P less than 0.001). Finally, we propose reference intervals for activities of the three antioxidant enzymes in blood in individuals less than 65 years old. PMID:1934468

Guemouri, L; Artur, Y; Herbeth, B; Jeandel, C; Cuny, G; Siest, G

1991-11-01

437

386 ON THE FAILURE OF TUMOUR HOMOGENATE INJECTIONS TO SIMULATE QUANTITATIVELY THE CHANGES IN CATALASE ACTIVITY IN THE TUMOUR-BEARING HOST  

E-print Network

IN recent years much work has been done on the catalase depressing action of fractions derived from tumour tissues. However the effects on liver catalase produced by these fractions, or by the injection of whole homogenates of tumour tissues, have seldom been compared quantitatively with those observed in the tumour-bearing animal. In fact there now seems considerable doubt whether injections of tumour homogenates or fractions are capable of quantitatively simulating the action of the tumour on its host. In the tumour-bearing mouse most investigators seem to agree that catalase activity falls progressively during tumour growth, Recently, however, Kampschmidt, and remains low until the death of the animal. M. E. Adams and McCoy (1959) found that when daily injections of tumour fractions were given to mice, their catalase activity fell sharply, but after a few days rose again while the injections were still being given.

D. H. Adams

1961-01-01

438

232 1\\'1. POLONOVSKI. -L'AMMONIAQUE catalase n'est pas forte et s'exprime volumtrique ment par 0,5-1,0.  

E-print Network

232 1\\'1. POLONOVSKI. - L'AMMONIAQUE catalase n'est pas forte et s'exprime volumétrique ment par 0,5-1,0. 3. La catalase ne peut pas servir à la définition -de la qualité du levainlactique. BIBLIOGRAPHIE : l'absence d'ammoniolactie accentuée devenant un test de conservation aseptique dû lait. TILLMANS

Boyer, Edmond

439

Cloning, characterization and phenotypic expression in Escherichia coli of catF , which encodes the catalytic subunit of catalase isozyme CatF of Pseudomonas syringae  

Microsoft Academic Search

The phytopathogenic, gram-negative bacterium Pseudomonas syringae pv. syringae 61 contains three isozymes of catalase (EC 1.11.1.6), which have been proposed to play a role in the bacterium's responses to various environmental stresses. To study the role of individual isozymes, the gene coding for the catalytic subunit of one catalase isozyme was cloned from a cosmid library hosted in Escherichia coli

M. G. Klotz; Y. C. Kim; J. Katsuwon; A. J. Anderson

1995-01-01

440

Catalase-based thin-layer enzyme cell used in organic-phase FIA system for determination of moisture in oily foods  

Microsoft Academic Search

The aim of our present work was to study the possibility of constructing a biosensor based on immobilized catalase enzyme (EC 1.11.1.6.) in organic-phase solutions. The catalase enzyme was immobilized by glutaraldehyde on a natural protein membrane in a thin-layer enzyme cell, connected to a stopped-flow injection analyser (SFIA) system with an amperometric detector. Adding FMCA to acetonitrile, the optimal concentration

Nóra Adányi; Mária Váradi

2004-01-01

441

High-Level Expression of Heme-Dependent Catalase Gene katA from Lactobacillus Sakei Protects Lactobacillus Rhamnosus from Oxidative Stress  

Microsoft Academic Search

Lactic acid bacteria (LAB) are generally sensitive to hydrogen peroxide (H2O2), Lactobacillus sakei YSI8 is one of the very few LAB strains able to degrade H2O2 through the action of a heme-dependent catalase. Lactobacillus rhamnosus strains are very important probiotic starter cultures in meat product fermentation, but they are deficient in catalase. In\\u000a this study, the effect of heterologous expression

Haoran An; Hui Zhou; Ying Huang; Guohong Wang; Chunguang Luan; Jing Mou; Yunbo Luo; Yanling Hao

2010-01-01

442

A prenatal test for the cerebro-hepato-renal (Zellweger) syndrome by demonstration of the absence of catalase-containing particles (peroxisomes) in cultured amniotic fluid cells  

Microsoft Academic Search

In this paper we show that whereas acyl-CoA: dihydroxyacetone phosphate acyltransferase, a membranebound peroxisomal enzyme, is deficient in homogenates of cultured amniotic fluid cells of fetuses with Zellweger syndrome, catalase a soluble peroxisomal matrix enzyme is present in normal amounts. Digitonin titration exper