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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

As a first step in an analysis of the DNA regions involved in the control of the catalase A gene of Saccharomyces cerevisiae by glucose, heme, and oxygen this gene has been cloned. Catalase A-deficient mutants were obtained by UV mutagenesis of a ctt1 mutant strain specifically lacking catalase T. All the catalase A-deficient mutants obtained fall into one complementation group. The single recessive mutation causing specific lack of catalase A was designated cta1. Several overlapping DNA fragments complementing the cta1 mutation were obtained by transforming ctt1 cta1 double mutants with a yeast gene library in vector YEp13. Hybrid selection of RNA with the help of one of the cloned DNAs followed by in vitro translation of this RNA and identification of the protein synthesized with catalase A-specific antibodies showed that the catalase A structural gene has been cloned. A single copy of this gene is present in the yeast genome. Transcription of the catalase A gene cloned into vector YEp13 is repressed by glucose. The DNA isolated hybridizes to a 1.6 kb polyA+-RNA virtually absent from heme-deficient cells, presumably catalase A mRNA.
Mol Gen Genet 1985
PMID:Isolation of the catalase A gene of Saccharomyces cerevisiae by complementation of the cta1 mutation. 389 93

The catalase T structural gene of Saccharomyces cerevisiae was cloned by functional complementation of a mutation causing specific lack of the enzyme (cttl). Catalase T-deficient mutants were obtained by UV mutagenesis of an S. cerevisiae strain bearing the cas1 mutation, which causes insensitivity of catalase T to glucose repression. Since the second catalase protein of S. cerevisiae, catalase A, is completely repressed on 10% glucose, catalase T-deficient mutant colonies could be detected under such conditions. A cttl mutant was transformed with an S. cerevisiae gene library in plasmid YEp13. Among the catalase T-positive clones, four contained overlapping DNA fragments according to restriction analysis. Hybridization selection of yeast mRNA binding specifically to one of the cloned DNAs, translation of this mRNA in cell-free protein synthesis systems, and demonstration of catalase T protein formation by specific immunoadsorption showed that the catalase T structural gene had been cloned. By subcloning, the gene was located within a 3.5-kilobase S. cerevisiae DNA fragment. As in wild-type cells, catalase T synthesis in cttl mutant cells transformed with plasmids containing this fragment is sensitive to glucose repression. By DNA-RNA hybridization, catalase T transcripts were shown to be present in oxygen-adapting cells but absent from heme-deficient cells.
Mol Cell Biol 1983 Sep
PMID:Isolation of the catalase T structural gene of Saccharomyces cerevisiae by functional complementation. 635 26

The substructural organization of completely crystalline peroxisomes present in Hansenula polymorpha cells grown under methanol limitation in a chemostat was investigated by different cytochemical and ultrastructural techniques. Time-dependent cytochemical staining experiments indicated that activities of the two main constituents of these organelles, namely, alcohol oxidase and catalase, were present throughout the crystalline matrix. Catalase was completely removed from isolated peroxisomes by osmotic shock treatment. After such treatment, the ultrastructure of the crystalline matrix of the organelles remained virtually intact. Because alcohol oxidase activity was still present in this matrix, it was concluded that alcohol oxidase protein is the only structural element of the peroxisomal crystalloids. The molecular architecture of the crystalloids was investigated in ultrathin cryosections which permitted recognition of individual molecules in the crystalline matrix. Depending on the plane of sectioning, different crystalline patterns were observed. Tilting experiments indicated that these images were caused by superposition of octameric alcohol oxidase molecules arranged in a tetragonal lattice. A three-dimensional model of the crystalloid is presented. The repeating unit of this structure is composed of four alcohol oxidase molecules. The crystalloid represents an open structure, which may explain the observed free mobility of catalase molecules.
Mol Cell Biol 1981 Oct
PMID:Substructure of crystalline peroxisomes in methanol-grown Hansenula polymorpha: evidence for an in vivo crystal of alcohol oxidase. 705 Jun 59

Because alveolar macrophages generate and release reactive oxygen metabolites but also contain antioxidative enzymes, they have the potential of either damaging or protecting tissues. We investigated the relative role of the hydrogen peroxide (H2O2)-scavenging antioxidative enzymes in H2O2 disposal and cell protection using freshly isolated (5 h ex vivo) and overnight (24 h ex vivo) cultured human alveolar macrophages. Cell protection was assessed on the basis of maintenance of cellular high-energy phosphates, leakage of intact nucleotides into the extracellular medium, and appearance of the nucleotide catabolic products xanthine, hypoxanthine, and uric acid. To investigate the relative importance of catalase and the glutathione redox cycle, the experiments were conducted in cells pretreated with amino-triazole (ATZ) to inactivate catalase or with 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) to inactivate glutathione reductase. Catalase, glutathione peroxidase, and glutathione reductase activities did not change significantly during overnight culture of the cells. Both freshly isolated and cultured cells consumed exogenous H2O2 mainly by the catalase-dependent pathway. When the cells were exposed to H2O2 (100 microM), catalase and the glutathione redox cycle equally participated in maintaining cellular high-energy nucleotides. However, when cultured cells were exposed to formylated peptide (FMLP) (10(-7) M), the glutathione redox cycle was responsible for the maintenance of high-energy nucleotides. Furthermore, in both exposures, the glutathione redox cycle was more important in maintaining cell membrane integrity and preventing nucleotide leakage from the cells. Immunocytochemical labeling showed that catalase was primarily localized in the peroxisomal compartment of these cells.(ABSTRACT TRUNCATED AT 250 WORDS)
Am J Respir Cell Mol Biol 1995 Oct
PMID:Catalase and glutathione reductase protection of human alveolar macrophages during oxidant exposure in vitro. 754 73

In aerated water solutions Fe(II)Cytochrome c is slowly oxidized to Fe(III)Cytochrome c by molecular oxygen, from which superoxide anion radicals are produced (kobs = 2.7 x 10(-4) min-1 at 37 degrees C and pH = 7.3). The biological importance of this reaction has been evidenced by kinetic investigations in the presence of scavengers. In the presence of Superoxide dismutase the oxidation rate is strongly enhanced (kobs = 3 x 10(-3) min-1 at 37 degrees C). Catalase and mannitol reduce the rate constant values by 50% and 25% respectively either in the presence or in the absence of Superoxide dismutase: differences between rate constants correspond to the differences in stoichiometric redox ratios indicating that hydrogen peroxide and hydroxyl radicals are formed subsequently to the production of superoxide anion radicals.
Biochem Mol Biol Int 1995 Apr
PMID:Production of reactive oxygen-derived species by redox reactions between Fe(II)cytochrome c and oxygen. A kinetic study. 762 18

ESR spin trapping was utilized to study the singlet oxygen (1O2) generation in the reaction of superoxide (O2) with H2O2. The spin trap used was 2,2,6,6-tetramethyl-4-piperdone. Incubation of xanthine, xanthine oxidase and H2O2 generated 1O2 spin adduct signal. Omission of xanthine, xanthine oxidase or H2O2 caused a sharp decrease in 1O2 generation. 1O2 scavenger, sodium azide, inhibited 1O2 generation while .OH scavenger, ethanol, only slightly decreased the signal intensity. Potassium superoxide (KO2) decomposition generated 1O2. Catalase and sodium azide inhibited 1O2 generation and H2O2 enhanced it. The results demonstrate that O2 is capable of generating 1O2 upon reaction with H2O2.
Biochem Mol Biol Int 1995 May
PMID:Singlet oxygen generation in the superoxide reaction. 766 19

Effects of hypoxia-reoxygenation (H-R) on myocytes isolated from 10 week hypertrophied and sham control rat hearts were studied. Myocyte hypertrophy was indicated by an increase in cell size. Superoxide dismutase (SOD) and glutathione peroxidase (GSHPx) enzyme activities were significantly higher and lipid peroxidation (TBARS) was lower in hypertrophied myocytes prior to any H-R. Hypertrophied myocyte population showed significantly less damage to cell morphology due to H-R. In sham as well as hypertrophied myocytes, Na+ and Ca2+ contents were increased by H-R, but Ca2+ accumulation was significantly less in the hypertrophied myocytes. Both SOD and GSHPx activities were depressed by the oxidative stress in the sham myocytes whereas these activities were not significantly changed in the hypertrophied myocytes. Catalase activity in the prehypoxic sham and hypertrophied myocytes was comparable and this activity did not change during H-R. There was a significant increase in lipid peroxidation due to H-R but this change was less in hypertrophied myocytes. This study shows less vulnerability of hypertrophied myocytes to oxidative stress and an increase in endogenous antioxidant reserve may have an important role in mediating this protection.
J Mol Cell Cardiol 1995 Jan
PMID:Endogenous antioxidants in isolated hypertrophied cardiac myocytes and hypoxia-reoxygenation injury. 776 Mar 50

The mechanisms by which two quinone-forming compounds, hydroquinone (HQ) and tert-butyl-hydroquinone (tBHQ), induce chromosomal loss and breakage in a prostaglandin H synthase-containing V79 cell line have been investigated using the cytokinesis-block micronucleus assay with CREST antibody staining. Increased frequencies of CREST-positive micronuclei (indicating chromosome loss) and CREST-negative micronuclei (indicating chromosome breakage) were observed following exposure of cells to HQ and tBHQ. The formation of micronuclei by HQ, but not tBHQ, was dependent on arachidonic acid supplementation, indicating activation by prostaglandin H synthase. Since the oxidation of hydroquinones can result in the generation of oxygen radicals, the contribution of oxygen radicals to the formation of chromosomal alterations induced by HQ and tBHQ was investigated. In the presence of a superoxide-generating system consisting of hypoxanthine and xanthine oxidase, a significant increase in micronucleated cells was observed. These induced micronuclei consisted exclusively of CREST-negative micronuclei and their formation was completely inhibited by pretreatment with catalase. Catalase also significantly inhibited the CREST-negative micronuclei induced by HQ and tBHQ. In addition, glutathione treatment inhibited both CREST-positive and negative micronuclei induced by these phenolic compounds. These results indicate that both chromosome loss and breakage are induced by these two quinone-forming agents. Reactive oxygen species contribute to the chromosomal breakage induced by HQ and tBHQ but the observed chromosomal loss appears to result from other mechanisms such as an interference of quinone metabolites with spindle formation.
Environ Mol Mutagen 1994
PMID:Role of oxygen radicals in the chromosomal loss and breakage induced by the quinone-forming compounds, hydroquinone and tert-butylhydroquinone. 785 41

EDTA-chelated ferrous chloride (Fe(2+)-EDTA) mixed with ascorbic acid (VC) was shown in vitro to produce 2,3-dihydroxybenzoic acid (2,3-DHBA), one of the hydroxyl radical (.OH) derivatives formed from reaction with 1 mM salicylic acid. The .OH generating system of Fe(2+)-EDTA (5, 25 and 50 microM) mixed with VC (50, 250 and 500 microM) was perfused for 15 min to the isolated rat hearts to characterize the effect of exogenous .OH on cardiac function, metabolism, and structure. A dose-effect relationship was observed between .OH dosage and ventricular dysfunction, increase in coronary flow, structural damage, decrease in ATP and increase in lipid peroxidation. Catalase (CAT, 500 U/ml) and deferoxamine (DFX, 10 mM) significantly (P < 0.05) reduced .OH formation in vitro, but superoxide dismutase (SOD, 100 U/ml) did not. When these agents were given to the heart perfused with 50 microM Fe(2+)-EDTA plus 500 microM VC, SOD failed to modify any myocardial alterations whereas CAT and DFX completely reversed them. Addition of 500 microM hydrogen peroxide (H2O2) to the 50 microM Fe(2+)-EDTA plus 500 microM VC further caused a 14-fold increase in .OH generation. Addition of H2O2 (500 microM) to the .OH generating mixture induced more conspicuous myocardial changes compared with the mixture without H2O2 addition, but the extent of those changes other than increase in coronary flow was less than that caused by perfusion with 500 microM H2O2 alone. These results further suggest that the cardiac changes induced by the .OH generating system are due to the combined effects of .OH and H2O2 which is formed as an intermediate product.
J Mol Cell Cardiol 1994 Apr
PMID:Characterization of exogenous hydroxyl radical effects on myocardial function, metabolism and ultrastructure. 807 2

The present study was carried out to determine the localization of peroxidase activity in bull spermatozoa. 3,3'-Diaminobenzidine (DAB) was used as a substrate for revealing peroxidase activity, and light and electron microscopic analysis of the results obtained was performed. Peroxidase activity was detected in the mitochondria of the middle piece and the outer acrosomal membrane. Catalase was excluded as an enzyme, catalyzing the detected peroxidase activity. Concerning the biochemical properties of bull sperm peroxidases, peroxidase activity was found to be manifested in a large pH range, 4-10.5. Bull sperm peroxidase activity appeared to be temperature sensitive and azide sensitive and could be readily inhibited by phenylhydrazine. Electrophoretic analysis of the proteins from bull sperm extracts separated in a Davis-Ornstein system of 7% polyacrylamide gel, followed by the determination of peroxidase activity on the polyacrylamide gels, revealed that all 14 sperm protein fractions available on the gel possessed peroxidase when benzidine was used as a substrate. The possible reasons for the electrophoretic heterogeneity of bull sperm peroxidases are discussed.
Mol Reprod Dev 1994 Feb
PMID:Peroxidase activities in bull spermatozoa. 817 3


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