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

M. luteus catalase dissociates upon treatment with urea, dodecylsulfate and anhydrides into monomers, the molecular weight of which appears to be 1/4 of that of the native enzyme. The urea-induced dissociation depends upon the incubation time, the urea concentration and the pH of the incubation mixture. Reassociation of the subunits proved to be unsuccessful. Native M. luteus catalase only contains 30% alpha-helix. When fully dissociated in presence of urea, it still retains 15% alpha-helix. Catalase from M. luteus was found to lack cysteine residues.
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PMID:Subunit structure of Micrococcus luteus catalase. Dissociation of M. luteus catalase induced by dodecylsulfate, citraconic and 2,3-dimethylmaleic anhydrides and urea. 68 Jun 45

The effect of atmospheric oxygen on the viability of 13 strains of anaerobic bacteria, two strains of facultative bacteria, and one aerobic organism was examined. There were great variations in oxygen tolerance among the bacteria. All facultative bacteria survived more than 72 h of exposure to atmospheric oxygen. The survival time for anaerobes ranged from less than 45 min for Peptostreptococcus anaerobius to more than 72 h for two Clostridium perfringens strains. An effort was made to relate the degree of oxygen tolerance to the activities of superoxide dismutase, catalase, and peroxidases in cell-free extracts of the bacteria. All facultative bacteria and a number of anaerobic bacteria possessed superoxide dismutase. There was a correlation between superoxide dismutase activity and oxygen tolerance, but there were notable exceptions. Polyacrylamide gel electropherograms stained for superoxide dismutase indicated that many of the anaerobic bacteria contained at least two electrophoretically distinct enzymes with superoxide dismutase activity. All facultative bacteria contained peroxidase, whereas none of the anaerobic bacteria possessed measurable amounts of this enzyme. Catalase activity was variable among the bacteria and showed no relationship to oxygen tolerance. The ability of the bacteria to reduce oxygen was also examined and related to enzyme content and oxygen tolerance. In general, organisms that survived for relatively long periods of time in the presence of oxygen but demonstrated little superoxide dismutase activity reduced little oxygen. The effects of medium composition and conditions of growth were examined for their influence on the level of the three enzymes. Bacteria grown on the surface of an enriched blood agar medium generally had more enzyme activity than bacteria grown in a liquid medium. The data indicate that superoxide dismutase activity and oxygen reduction rates are important determinants related to the tolerance of anaerobic bacteria to oxygen.
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PMID:Factors related to the oxygen tolerance of anaerobic bacteria. 69 63

Catalase A from Saccharomyces cerevisiae and its biosynthetic precursors can specifically be immunoprecipitated from extracts obtained from yeast cells grown in the presence of L-[3H]leucine or 59FeCl3. The enzyme and its precursors recognized by a specific antiserum are absent from anaerobic cells. During oxygen adaptation of yeast pre-grown on 0.3% glucose under anaerobic conditions catalase A is formed via a heme-less precursor, probably the apomonomer of the protein, and a heme-containing intermediate. When cells are grown in the presence of Tween 80 the amount of catalase A, but not of catalase T, increases 4-fold. Comparison of the mode of synthesis of catalase T and A shows that no precursor-product relationship exists between the two proteins.
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PMID:Catalase biosynthesis in yeast: formation of catalase A and catalase T during oxygen adaptation of Saccharomyces cerevisiae. 79 66

Catalase (EC 1.11.1.6) activity levels were found to decrease in the fruit fly, Drosophila melanogaster, from 1 to 5 days of age and to increase from 5 to 8 days of age, followed by a second decline in old age. Feeding the hypolipidemic compounds, beta-diethylaminoethyl-alpha-p-chlorophenoxyisobutyrate hydrochloride, Nafenopin and Clofenapate did not significantly alter catalase levels. Median survival time was decreased 8.3% by feeding Clofenapate and increased up to 5.5% by beta-diethylamino-ethyl-alpha-p-chlorophenoxyisobutyrate hydrochloride.
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PMID:Catalase levels in Drosophila and the lack of induction by hypolipidemic compounds. A brief note. 81 92

The addition of catalase to the surface of selective medium plates permitted increased enumeration of physically or chemically injured (stressed) microorganisms. Catalase acted by preventing the accumulation of hydrogen peroxide in, or around, injured cells. Heat-injured Staphylococcus aureus cells had decreased catalase activity, and heat-inactivated catalase had no effect on enumeration.
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PMID:Catalase: its effect on microbial enumeration. 82 45

Late ovarian chambers of Drosophila melanogaster have been examined by ultrastructural cytochemistry in an attempt to characterize some of the transformations which precede the completion of oogenesis. From stage 11 onward peroxidase activity is present in the endoplasmic reticulum of both nurse cells and oocyte, as well as in the egg-covering precursors of the columnar follicle cells. Catalase activity is restricted to the very last stages of oogenesis (stage 13-14) and appears to be located in membrane-bound organelles of the ooplasm which are continuous with the endoplasmic reticulum. Because of the presence of catalase as well as by their structural appearance, these organelles are to be identified as microperoxisomes. Catalase activity becomes cytochemically detectable in the ooplasm somehow in coincidence with the formation of glycogen. Furthermore, glycogen is first formed in intimate association with alpha-1 yolk platelets. On the basis of these findings it is suggested that glycogen synthesis occurs by a process of gluconeogenesis.
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PMID:Cytochemistry of late ovarian chambers of Drosophila melanogaster. 82 30

Catalase formation by Bacteroides fragilis was immediately stopped upon addition of glucose to a culture growing in peptone medium. Each of eight other carbohydrates fermented by the organism also repressed catalase formation. Without added carbohydrate, the strains produced relatively large amounts of catalase (25 to 50 U/mg of protein).
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PMID:Carbohydrate repression of catalase synthesis in Bacteroides fragilis. 83 Jun 47

The catalase level of Bacteroides distasonis (ATCC 8503, type strain) varied with the amount of hemin supplied to the medium when the cells were grown in either a prereduced medium containing 0.5% peptone, 0.5% yeast extract, and 1% glucose or in a prereduced, defined heme-deficient medium. The effect of hemin on catalase production could not be duplicated by ferrous sulfate or ferrous ammonium citrate. Catalase activity reached peak values in late log phase, whereas superoxide dismutase specific activity remained constant throughout the culture growth cycle. The catalase was a nondialyzable, cyanide and azide-sensitive, heat-labile protein that coeluted with bovine erythrocyte catalase from Sepharose 6 B. Analysis of polyacrylamide gels stained for catalase activity and for heme showed a correspondence between the single catalytic activity band and one of three heme-protein bands. These data suggest a heme-protein of approximately 250,000 molecular weight. The superoxide dismutase was a cyanide-insensitive protein of approximately 40,000 molecular weight that migrated electrophoretically on acrylamide gels as a single band of activity.
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PMID:Production and some properties of catalase and superoxide dismutase from the anaerobe Bacteroides distasonis. 84 16

To investigate the possibility that human polymorphonuclear leukocytes (PMN) elaborate sufficient amounts of hydrogen peroxide (H2O2) and other radicals of reduced oxygen to be autotoxic and retard directed cell movement and phagocytosis, the rate of ingestion of opsonized lipopolysaccharide-paraffin oil particles and movement through Nuclepore filters were studied. Ingestion rates were increased under anaerobic conditions and in normal aerobic conditions in the presence of extracellular catalase but not superoxide dismutase (SOD) or scavengers of singlet oxygen or hydroxyl radicals. Conversely, ingestion rates were decreased when cells were exposed to H2O2 or a superoxide anion (O2-)-H2O2 generating system of xanthine-xanthine oxidase. Catalase, but not SOD, prevented the effect and also enhanced the directed movement of PMN in normal aerobic conditions. PMN from volunteers administered 1600 U/day of the membrane lipid antioxidant alpha-tocopherol were hyperphagocytic but killed Staphylococcus aureus 502A less effectively than controls, suggesting that less H2O2 was available to damage PMN or kill bacteria. H2O2-dependent stimulation of the hexose monophosphate shunt, H2O2 release from phaogytizing PMN, and fluoresceinated concanavalin A cap formation promoted by H2O2 damage to microtubules were all diminished, but the release of O2- from phagocytizing PMN was not diminished in the vitamin E group. These results support the hypothesis that directed movement and phagocytosis by PMN are attenuated by autooxidative damage to the cell membrane by endogenously derived H2O2 and that the administration in vivo of vitamin E may prevent this damage by scavenging H2O2.
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PMID:Autooxidation as a basis for altered function by polymorphonuclear leukocytes. 87 28

An early-reading blank-corrected end-point determination of uric acid in serum has been developed for use with a centrifugal analyzer. The method is based on a modification of the uricase (urate:oxygen oxidoreductase, EC 1.7.3.3)/catalase (hydrogen peroxide:hydrogen peroxide oxidoreductase EC 1.11.1.6)/aldehyde dehydrogenase (aldehyde:NAD(P)+ oxidoreductase, EC 1.2.1.5)-coupled analytical scheme reported by Haeckel [Z. Klin. Chem. Klin. Biochem. 14, 101 (1976)]. Sensitivity and precision of the method are excellent, and results compare well with those obtained by the Kageyama procedure [Clin. Chim. Acta 31, 421 (1971)].
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PMID:Enzyme-coupled measurement of uric acid in serum with a centrifugal analyzer. 89 Aug 96


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