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At least 1,423 records · Page 79Linked to original sources
PubMed1989

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

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 H2O2 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 (H2O2). Since both catalase and the glutathione pathway are dependent on NADPH for function, this finding raises the possibility that both mechanisms destroy H2O2 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 H2O2 when H2O2 is generated at a rate comparable to that which leads to hemolysis in G6PD- deficient erythrocytes.

Carbon Dioxide↗
PubMed1988

Superoxide dismutase and catalase conjugated to polyethylene glycol increases endothelial enzyme activity and oxidant resistance.

Covalent conjugation of superoxide dismutase and catalase with polyethylene glycol (PEG) increases the circulatory half-lives of these enzymes from less than 10 min to 40 h, reduces immunogenicity, and decreases sensitivity to proteolysis. Because PEG has surface active properties and can induce cell fusion, we hypothesized that PEG conjugation could enhance cell binding and association of normally membrane-impermeable enzymes. Incubation of cultured porcine aortic endothelial cells with 125I-PEG-catalase or 125I-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. Endothelial cell cultures incubated with PEG-superoxide dismutase and PEG-catalase for 24 h and then extensively washed were protected from the damaging effects of reactive oxygen species derived from exogenous xanthine oxidase as judged by two criteria: decreased release of intracellular 51Cr-labeled proteins and free radical-induced changes in membrane fluidity, measured by electron paramagnetic resonance spectroscopy of endothelial membrane proteins covalently labeled with 4-maleimido-2,2,6,6-tetramethylpiperidinooxyl. 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.

Animals↗
PubMed1987

Ethanol metabolism in alcohol dehydrogenase deficient deermice is mediated by the microsomal ethanol oxidizing system, not by catalase.

The participation of the microsomal ethanol oxidizing system (MEOS) and catalase in total ethanol metabolism is reviewed. Non-alcohol dehydrogenase (ADH) dependent pathways contribute to in vivo ethanol metabolism, but the respective role of each has long been debated. The principal data supporting a role for catalase is an occasionally reported moderate depression of ethanol metabolism after aminotriazole. In deermice lacking ADH, we observed a slight (though not statistically significant) decrease in basal ethanol metabolism of hepatocytes after aminotriazole. However, this decrease was found to parallel a similar inhibition of MEOS by aminotriazole, and thus may not reflect catalase mediated peroxidation in this animal. 1-butanol, a competitive inhibitor of ethanol oxidation by MEOS and not a substrate for catalase, decreased ethanol metabolism by hepatocytes in a concentration dependent manner. These results, as well as those from other investigators, indicate that MEOS mediates virtually all of non-ADH ethanol metabolism in vivo.

1-Butanol↗
PubMed1987

Purification and characterization of a catalase-peroxidase from the photosynthetic bacterium Rhodopseudomonas capsulata.

Catalase-peroxidase was isolated from aerobically grown Rhodopseudomonas capsulata. The enzyme resembles typical catalases in some of its physicochemical properties. It has an apparent molecular weight of 236,000 and is composed of four identical subunits. It shows a typical high spin ferric heme spectrum with absorption maxima at 403 and 635 nm and shoulders at 503 and 535 nm. Upon binding of cyanide, the enzyme is converted to the low spin state, as shown by the shift of the Soret maximum to 418 nm and the band at 532 nm. It has an isoelectric point at pH 4.5. The enzyme differs from typical catalases in also having a strong peroxidatic activity with dianisidine, pyrogallol, and diaminobenzidine as electron donors. Both the catalatic and the peroxidatic activities are similarly inactivated by treatment with 1 mM H2O2, heating to 50 degrees C, exposure to ethanol/chloroform, and photooxidative conditions. In contrast to typical catalases, but similarly to peroxidases, the enzyme is reduced by sodium dithionite. The pH optimum of the peroxidatic activity is 5-5.3 (in contrast to 6-6.5 of the catalatic activity). 50% of the apparent maximal activities are reached at 0.3 and 4.2 mM H2O2 for the peroxidatic and catalatic activities, respectively. Both enzymic activities are equally inhibited by cyanide, 50% inhibition being achieved with 2.2 X 10(-5) M KCN. Contrarily, the two activities differ in their response to hydroxylamine and azide. 50% inhibition of the catalatic activity is obtained with 1.5 X 10(-4) M azide or 2.15 X 10(-6) M hydroxylamine; 50% inhibition of the peroxidatic activity requires 7.3 X 10(-4) M azide or 7.8 X 10(-5) M hydroxylamine. The activation energies of the catalatic and the peroxidatic activities are 1.9 and 1.7 kcal/mol, respectively.

Azides↗
PubMed1986

Effect of superoxide dismutase and catalase on myocardial energy metabolism during ischemia and reperfusion.

Survival of cardiac patients undergoing heart surgery depends critically upon the recovery of myocardial energy metabolism during reperfusion of ischemic myocardium. The present study compares various parameters of myocardial energy metabolism using an isolated in situ pig heart. The left anterior descending (LAD) coronary artery was occluded for 60 min, followed by 60 min of global hypothermic cardioplegic arrest and 60 min of reperfusion. Free radical scavengers [superoxide dismutase SOD and catalase] were used to protect the ischemic heart from reperfusion injury. In both control and SOD plus catalase-treated groups, ATP, creatine phosphate (CP), ATP/ADP ratio, energy charge and phosphorylation potential dropped significantly during ischemic insult. After reperfusion, CP, ATP/ADP ratio and phosphorylation potential improved significantly, but they were restored to control level only in treated animals. In either case, free energy of ATP hydrolysis (delta G) lowered only by 5% during ischemia, but recovered promptly upon reperfusion. SOD and catalase also improved coronary blood flow and reduced creatine kinase release compared to those of untreated animals, suggesting improved myocardial recovery upon reperfusion. Our results suggest that SOD and catalase significantly improve the myocardial recovery during reperfusion by enhancing rephosphorylation steps, and the value of delta G is more critical compared to those of ATP and CP for myocardial recovery.

Adenosine Triphosphate↗
PubMed1979

[Regulation of catalase synthesis in Proteus mirabilis].

During the log-phase growth of Proteus mirabilis the specific activity of catalase decreases, while at the beginning of or during the stationary phase an increase takes place which is abolished by inhibitors of nucleic acid or protein synthesis. Glucose in the culture medium has no appreciable effect on the level of enzyme synthesis nor does the passage of bacteria to anaerobiosis bring any noticeable change. Successive additions of hydrogen peroxide up to weak final concentrations (0.2--0.5 mM) stimulate catalase synthesis. Determination of the enzyme in vivo reveals but a weak proportion of the total catalase which can only be titrated after the breakdown of cells. The titrable enzyme in vivo represents, as an order of magnitude, the activity found associated with the cell wall, in an easily released form after the mechanical separation of the inner and outer membranes. Thus, bacteria can act upon exogenous peroxide only through a peripheral catalase while they possess in a masked form an important reserve of cytoplasmic enzyme.

Anaerobiosis↗
PubMed1979

Oxidation of tryptophan-P-1 and P-2 by beef liver catalase-H2O2 intermediate: comparison with horseradish peroxidase.

Tryptophan-p-1 (trp-p-1) and p-2, which have high mutagenic and carcinogenic potential, are oxidized by catalase- and horseradish peroxidase (HRP)-H2O2 intermediates with optimum pH 5.9 (0.2 M-acetate) in catalase and pH 5.0 (0.2 M-acetate), 8.0 (0.01 M-phosphate) in HRP. The rate constants (k4) of the oxidation in the catalase at pH 5.9 (0.2 M-acetate) were 2965 M-1 x sec-1 for trp-p-1 and 576 M-1 x sec-1 for trp-p-2. In the case of HRP, 1894 M-1 x sec-1, (pH 5.0, 0.2 M-acetate) for trp-p-1 and 705 M-1 x sec-1 (pH 8.0, 0.001 M-phosphate) for trp-p-2 under each optimum condition. The oxidation products of trp-p-1 and p-2 by catalase or HRP lost completely their mutagenic potential in the mutation assay.

Animals↗
PubMed1979

Properties of erythrocyte catalase from heterozygotes for Japanese type acatalasemia.

The level of blood catalase activity in heterozygotes for Japanese type acatalasemia was demonstrated to be about half of normal levels by means of titration and spectrophotometric methods. A distribution plot of catalase activities in heterozygous blood was completely separate from that of normal blood. Comparative analysis of the partially purified erythrocyte catalase preparations obtained from normal and heterozygous individuals revealed no distinct differences between them regarding stability to heat, sodium dodecyl sulfate and some enzyme inhibitors or pH dependency. The erythrocyte catalase in heterozygotes for Japanese type acatalasemia contains about half the normal specific activity and as stable as that in normal individuals.

Acatalasia↗
PubMed1985

Discrepancy between the different subcellular activities of rat liver catalase and superoxide dismutases in response to acute ethanol administration.

After acute ethanol administration (2.3 g/kg) peroxisomal and extra-peroxisomal catalase activities were affected in opposite directions. As long as ethanol was present, peroxisomal catalase activity was enhanced, but unaffected by amino-triazole (AT) injection. Extra-peroxisomal catalase activity was decreased during the 24hr following ethanol administration and was also inhibited after AT injection. Whereas mitochondrial manganese-dependent superoxide dismutase (Mn-SOD) was unaffected, the cytosolic Cu,Zn-SOD activity was decreased. The time-course of this decrease suggests that acute ethanol administration affects primarily extra-peroxisomal catalase activity, thus rendering cytosolic superoxide dismutase more exposed to oxygen derivatives.

Alcoholic Intoxication↗
PubMed1983

The effect of catalase on the inactivation of tyrosinase by ascorbic acid and by cysteine or glutathione.

When tyrosine was incubated with tyrosinase in the presence of ascorbic acid, dopa and 5-hydroxydopa were formed and the enzyme was inactivated. In the presence of catalase, more dopa and 5-hydroxydopa were formed because enzyme inactivation was prevented. Incubation of dopa and cysteine with small amounts of mushroom tyrosinase led to rapid inactivation of the enzyme. This inactivation was accelerated in the presence of catalase. New systems developed have been useful in demonstrating the role of hydrogen peroxide in tyrosinase inactivation by several compounds of importance in melanin biochemistry. Cysteine and glutathione inactivated tyrosinase. Addition of catalase increased the inactivation at high thiol concentrations, but decreased the inactivation at low concentrations. Ascorbic acid and 5-hydroxydopamine also inactivated tyrosinase, but with these compounds inactivation was completely prevented by addition of catalase. The inactivation by dopamine was negligible under the experimental conditions. Inactivation of tyrosinase by ascorbic acid and by 5-OH-dopamine was found dependent on oxygen, whereas inactivation by cysteine and glutathione was independent of oxygen. Large amounts of serum albumin protected tyrosinase from inactivation by ascorbic acid and 5-OH-dopamine, but did not prevent inactivation by cysteine and glutathione. The presence of substrate had a protective effect on the inactivation of tyrosinase by cysteine.

Ascorbic Acid↗
PubMed1981

Intracellular inhibition of catalase by alpha-methyldopa.

The effect of preincubation with alpha-methyldopa on catalase-dependent decomposition of H2O2 was studied in isolated rat hepatocytes. A direct assay of catalase function was obtained by measurement of O2 production under anaerobic conditions following additions of H2O2. Both the total O2 produced and the maximal O2 concentration attained were decreased by preincubation with alpha-methyldopa. The results demonstrate that alpha-methyldopa-induced formation of Compound II is associated with loss of intracellular catalase activity. These results indicate that the hepatotoxicity of alpha-methyldopa may be related to an increased sensitivity to oxidative injury due to inhibited catalase function.

Animals↗
PubMed1982

Superoxide radical inhibits catalase.

Catalase was inhibited by a flux of O2- generated in situ by the aerobic xanthine oxidase reaction. Two distinct types of inhibition could be distinguished. One of these was rapidly established and could be as rapidly reversed by the addition of superoxide dismutase. The second developed slowly and was reversed by ethanol, but not by superoxide dismutase. The rapid inhibition was probably due to conversion of catalase to the ferrooxy state (compound III), while the slow inhibition was due to conversion to the ferryl state (compound II). Since neither compound III nor compound II occurs in the catalatic reaction pathway, they are inactive. This inhibition of catalase by O2- provides the basis for a synergism between superoxide dismutase and catalase. Such synergisms have been observed in vitro and may be significant in vivo.

Acetaldehyde↗
PubMed1984

An immunological investigation of catalase in three mammalian species.

An immunological comparison of catalase has been conducted in the mouse, rat and guinea pig. In each of these species, enzyme activity from the peroxisomal compartment was indicated as immunologically distinct from the cytosolic activity, with catalase in the small granule compartment displaying intermediate characteristics. When related to the established data on the biogenetic and degradative changes of catalase in the mouse, the present results support the proposal that peroxisomal alterations, epigenetic modifications and degradative persistence are general characteristics of catalase biology in mammalian species.

Animals↗
PubMed1983

Effects of superoxide dismutase and catalase on disseminated intravascular coagulation in rats.

The effects of superoxide dismutase (SOD) and catalase on endotoxin-induced experimental disseminated intravascular coagulation (DIC) were studied in rats. Experimental DIC was induced by a 4 hr sustained infusion of endotoxin at a dose of 100 mg/kg. The rats were subcutaneously injected with SOD at 0.5, 5.0 or 50.0 mg/kg, or catalase at 0.01, 0.1 or 1.0 mg/kg, followed by the continuously infusion of 100 mg/kg/4hr of endotoxin. A preventive effect against DIC was noted in all the parameters, such as fibrinogen and fibrin degradation products, fibrinogen level, prothrombin time, partial thromboplastin time, platelet count and the number of renal glomeruli with fibrin thrombi, in the rats treated with 50.0 mg/kg of SOD or 1.0 mg/kg of catalase. When 50.0 mg/kg of SOD or 1.0 mg/kg of catalase was injected subcutaneously at 1, 2 or 3 hr after the initiation of the endotoxin-infusion, the protective effect against DIC was noted in all the parameters.

Animals↗
PubMed1984

[Physico-chemical characteristics of catalases from Micrococcus sp. n].

The physico-chemical properties of heme-containing and non-heme catalases isolated from the cell culture of Micrococcus sp. n. grown under intensive aeration were studied. The enzyme preparations were homogenous during polyacrylamide disc electrophoresis. The spectral and functional properties of the enzymes (e. g. specific activity, subunit molecular weight, quaternary structure, amino acid composition, immunoprecipitability, N-terminal amino acid sequences) were investigated. Monocrystals of non-heme catalase applicable for an X-ray analysis were grown and examined by X-ray spectroscopy. Both enzymes were stable upon storage in 40% ammonium sulfate for 2 months and resistant to lyophylization without any significant loss of their activity. Non-heme catalase is apparently an independent enzyme which is not derived from heme-containing catalase via dissociation, limited proteolysis or heme cleavage.

Amino Acids↗
PubMed1984

Correlation between induction of duodenal tumor by hydrogen peroxide and catalase activity in mice.

Incidences of duodenal tumor induced by oral administration of hydrogen peroxide (HPO) and catalase activities in the duodenal mucosa, blood and liver were correlated in C3H/HeN, C57BL/6N, (C57BL X C3H)F1 (B6C3F1) and hypocatalasemic C3H/Cbs mice. A solution of 0.4% HPO was given to the mice as drinking water for about 6 months. Incidences of duodenal tumor were 11.1% in C3H, 31.8% in B6C3F1, 100% in C57BL and 91.7% in C3H/Cbs mice. Catalase activities (10(-4) k/mg protein) in the duodenal mucosa, blood and liver were 5.3, 7.8 and 75.3 in C3H, 1.7, 7.7 and 62.8 in B6C3F1, 0.7, 5.1 and 40.7 in C57BL, and 0.4, 0.4 and 33.3 in C3H/Cbs mice, respectively. The coefficients of correlation (r) of catalase activities with the incidences of duodenal tumor in C3H, B6C3F1 and C57BL mice are -0.83 in duodenal mucosa, -0.98 in blood and -0.99 in liver. The results indicate that the incidence of duodenal tumor induction by HPO is dependent on the individual mouse strain and may be determined by the genes controlling the catalase activities.

Animals↗
PubMedDate not supplied

[Effect of oxygen and substrates for growth on the superoxide dismutase and catalase activity of microorganisms].

The activity of superoxide dismutase (SOD) and catalase in Azotobacter vinelandii, Citrobacter freundii, Rhodopseudomonas capsulata, Thiocapsa roseopersicina and Spirulina platensis is far higher when the cultures are grown under the aerobic conditions. The activities of SOD and catalase are higher in R. capsulata cells cultivated in a medium with glucose in the dark under the aerobic conditions than in cells grown under the same conditions but in the light. R. capsulata grown in a medium with glucose and T. roseopersicina cultivated in a medium with formate or pyruvate had higher activities of SOD and catalase than R. capsulata grown in a medium with acetate and T. roseopersicina cultivated in a medium with glucose. Irrespective of the growth conditions, the highest activity of SOD was manifested by C. freundii while that of catalase by A. vinelandii 1. C. freundii and T. roseopersicina contained both Mn-SOD and Fe-SOD whereas A. vinelandii and Rh. capsulata contained only Mn-SOD. The SOD from R. capsulata was purified to a homogeneous state. Its molecular weight is about 40,000 and it contains 1 Mn mole per mole of the enzyme.

Aerobiosis↗
PubMed1980

The relation of heme to catalase apoprotein synthesis in yeast.

The synthesis of two hemoproteins, catalase A and catalase T, was studied in mutants of Saccharomyces cerevisiae deficient in heme formation. These mutants can be grown on the end-product heme or on a heme precursor, or on ergosterol and Tween 80 (a source of oleic acid). It was found by immunoprecipitation that, in the presence of heme, catalases A and T were present in the mutants, but that in its absence (growth on ergosterol and Tween 80) the apoproteins of these enzymes were not detectable. In contrast, cytochrome c peroxidase, and some of the subunits of cytochrome c oxidase are present in cells grown without heme (Saltzgaber-Müller, J., and Schatz, G. (1978) J. Biol. Chem. 253, 305-310). Other evidence suggests that absence of catalase T apoprotein under heme-less conditions may be due to control by heme of apoprotein synthesis (G. Ammerer and H. Ruis, unpublished results), rather than increased proteolytic degradation.

Apoenzymes↗