Showing papers on "Catalase published in 1974"
TL;DR: The results point to a reaction between H2O2 and O2- (Haber-Weiss reaction) as a major source of the ·OH radicals and to a combined action of blocking ·OH formation as well as accelerating its removal.
896 citations
TL;DR: It is demonstrated that the superoxide radical, at least under some conditions, is a precursor of H202 generated by submitochondrial particles (SMP), however, some observations revealed an alternative pathway of mitochondrial H20, formation apparently involving an oxygen species distinct from 0,.
614 citations
TL;DR: Heterozygote erythrocyte catalase exerts properties intermediate to those of the normal enzyme and of the variant found in homozygotes for Swiss-type acatalasemia, this enzyme species is considered to represent a molecular hybrid.
Abstract: 1
Dissociation of the erythrocyte catalase tetramer into its dimer form proceeds readily in urea: the rate depends on urea concentration, time of inactivation and temperature, but is not influenced by enzyme concentration. This process is accompanied by loss of catalase activity, generation of peroxidase activity and an alteration of antigenic properties.
2
Recombination of dimer subunits to the tetramer molecule can be accomplished by removing urea by dialysis. Under optimal conditions up to 80% of the original catalase activity can be recovered. The reconstituted material is identical with the native catalase regarding enzymatic and antigenic properties, but differs with respect to electrophoretic mobility and heat stability.
3
Normal human erythrocyte catalase and the enzyme species present in blood of individuals heterozygous for Swiss-type acatalasemia differ with regard to electrophoretic mobility and heat stability. Moreover, dissociation of the heterozygote catalase tetramer into dimer subunits occurs at lower urea concentrations when compared to the normal enzyme. Since heterozygote erythrocyte catalase exerts properties intermediate to those of the normal enzyme and of the variant found in homozygotes for Acatalasemia, this enzyme species is considered to represent a molecular hybrid.
4
Hybridization of catalases can be accomplished in vitro by dissociating a mixture of normal and heterozygote catalase preparations in 8 M urea and subsequent dialysis. The resulting enzyme species reveals intermediate electrophoretic mobility and heat stability when compared with its native constituents.
241 citations
TL;DR: It is suggested that H2O2 is a normal metabolite in both plants and animals and is not particularly cytotoxic, and Catalase may function by preventing the formation of excessive concentrations of H 2O2 and by using H2 O2 in the peroxidatic oxidation of compounds such as methanol and formic acid.
Abstract: SUMMARY
Recent research suggests that H2O2 is a normal metabolite in both plants and animals and is not particularly cytotoxic. The impact of H2O2 on cell metabolism is discussed with particular reference to photorespiration. Catalase may function by preventing the formation of excessive concentrations of H2O2 and by using H2O2 in the peroxidatic oxidation of compounds such as methanol and formic acid. Radicals (such as OH and O2-) and ‘excited’ oxygen are far more damaging to living organisms. The formation of these radicals in biological systems is described. Superoxide dismutase plays a key role in protection against such radicals, but glutathione peroxidase is also involved.
226 citations
TL;DR: It is deduced that oxyleghemoglobin and other oxygenbinding proteins exert their effects by facilitating the diffusion of oxygen through a thin layer of solution, the "unstirred layer," surrounding the bacteroids, which results in the "effective" oxygen uptake which supports nitrogenase activity.
209 citations
TL;DR: Cytochemical studies using 3,3′-diaminobenzidine (DAB) revealed that theCatalase activity was located in microbodies, suggesting that the catalase activities would be related to the hydrocarbon metabolism in the yeasts.
Abstract: The catalase activities of the Candida cells grown on hydrocarbons were generally much higher than those of the cells grown on Iauryl alcohol, glucose or ethanol. Km values for hydrogen peroxide of the enzymes from the glucose- and the hydrocarbon-grown cells of Candida tropicalis were the same level. The enzyme activities of the yeasts were higher at the exponential growth phase, especially of the hydrocarbon-grown cells, than at the stationary phase. Profuse appearance of microbodies having homogeneous matrix surrounded by a single-layer membrane has also been observed electronmicroscopically in the hydrocarbon- grown cells of several Candida yeasts. Cytochemical studies using 3,3′-diaminobenzidine (DAB) revealed that the catalase activity was located in microbodies. These facts suggest that the catalase activities would be related to the hydrocarbon metabolism in the yeasts.
199 citations
TL;DR: Data indicate that, in both prokaryotes and in eukaryotes, superoxide dismutase is an important component of the defenses against oxygen toxicity.
Abstract: Saccharomyces cerevisiae var. ellipsoideus contained 6.5 times more superoxide dismutase and 2.3 times more catalase when grown under 100% O2 than when grown anaerobically. Growth under oxygen caused equal increases in both the cyanide-sensitive and the cyanide-insensitive superoxide dismutases of this organism. Experience with other eukaryotes has shown that cyanide sensitivity is a property of the cupro-zinc superoxide dismutase of the cytosol, whereas cyanide insensitivity is a property of the corresponding mangani-enzyme found in mitochondria. Cu2+, which has been shown to increase the radioresistance of yeast, also caused an increase of both of the superoxide dismutases of S. cerevisiae. Yeast which had been grown under 1 atm of O2 were more resistant toward the lethal effects of 20 atm of O2 than were yeast which had been grown in the absence of O2. Escherichia coli K-12 his− responded to growth under 1 atm of O2 by increasing its content of catalase and of peroxidase, but not of superoxide dismutase. This contrasts with E. coli B, which was previously shown to respond to O2 by a striking increase in superoxide dismutase. E. coli K-12 his− did not gain resistance toward 20 atm of O2 because of having been grown under 1 atm of O2. Once again, this contrasts with the behavior of E. coli B. These data indicate that, in both prokaryotes and in eukaryotes, superoxide dismutase is an important component of the defenses against oxygen toxicity.
169 citations
TL;DR: The solubilization and subsequent separation of the hepatic microsomal ethanol-oxidizing system from alcohol dehydrogenase and catalase activities by DEAE-cellulose column chromatography is described.
138 citations
TL;DR: Lactobacillus plantarum, although able to grow in the presence of oxygen, was found to retain a completely anaerobic metabolism, indicating that it did not reduce oxygen even when exposed to high concentrations of this gas.
Abstract: Lactobacillus plantarum, although able to grow in the presence of oxygen, was found to retain a completely anaerobic metabolism. Thus, L. plantarum did not consume detectable amounts of oxygen and did not contain measureable amounts of those enzyme activities which serve to protect anaerobic cells against the lethality of O2− and of H2O2. Superoxide dismutase, catalase, and peroxidase appeared to be absent from these cells. L. plantarum was unusually resistant towards hyperbaric oxygen, indicating that it did not reduce oxygen even when exposed to high concentrations of this gas. A photochemical reaction mixture, known to generate O2−, did kill L. plantarum. The lethality was diminished by superoxide dismutase, catalase, or mannitol and was augmented by H2O2. This suggests that the lethal agent generated in the photochemical system was primarily OH., generated from the reaction of O2− with H2O2.
111 citations
TL;DR: In this article, a comparative study was made of three important plant peroxide metabolism enzymes, namely peroxidase (EC 1.11.1.7), catalase ( EC 1.15.2.6) and superoxide dismutase, in Phaseolus vulgaris.
110 citations
TL;DR: The absence of sex difference in microbody proliferative response in nafenopin-treated rats and wild type mice is of particular significance, since ethyl-α-p-chlorophenoxyisobutyrate (CPIB)-induced microbody proliferation and increase in catalase activity occurred only in males.
Abstract: Nafenopin (2-methyl-2[p-(1,2,3,4-tetrahydro-1-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% produced a significant and sustained increase in the number of peroxisomes. The hepatic microbody proliferation in both male and female rats and wild type Csa strain mice treated with nafenopin was of the same magnitude and was associated with a two-fold increase in catalase activity and in the concentration of catalase protein. The increase in microbody population in acatalasemic mice, although not accompanied by increase in catalase activity, was associated with a twofold increase in the amount of catalase protein. The absence of sex difference in microbody proliferative response in nafenopin-treated rats and wild type mice is of particular significance, since ethyl-α-p-chlorophenoxyisobutyrate (CPIB)-induced microbody proliferation and increase in catalase activity occurred only in males. Nafenopin can, therefore, be used as an inducer of microbody proliferation and of catalase synthesis in both sexes of rats and mice. The serum glycerol-glycerides were markedly lowered in all the animals given nafenopin, which paralleled the increase in liver catalase. All the above effects of nafenopin were fully reversed when the drug was withdrawn from the diet of male rats. During reversal, several microbody nucleoids were seen free in the hyaloplasm or in the dilated endoplasmic reticulum channels resulting from a rapid reduction in microbody matrix proteins after the withdrawal of nafenopin from the diet. Because of microbody proliferation and catalase induction with increasing number of hypolipidemic compounds, additional studies are necessary to determine the interrelationships of microbody proliferation, catalase induction, and hypolipidemia.
TL;DR: In this article, a bio-electrochemical sensor for hydrogen peroxide is described, which consists of two membranes, a catalase-collagen membrane and a teflon membrane.
TL;DR: The immobilization of glucose oxidase and catalase by adsorption within the pores of controlled‐pore titania has yielded a remarkably stable enzyme system.
Abstract: The immobilization of glucose oxidase and catalase by adsorption within the pores of controlled-pore titania has yielded a remarkably stable enzyme system. Catalase apparently acts as both a stabilizer and an activator for glucose oxidase within the pores of this material. Hydrogen peroxide concentrations and flow rates have a marked effect upon the apparent activity of the immobilized enzyme system. The carrier parameters were varied to obtain optimum loading and stability information.
TL;DR: It can be concluded that a large part of the enhanced resistance toward phagocytic kill exhibited by iron-replete E. coli B was due to their increased content of the periplasmic ferrisuperoxide dismutase.
TL;DR: Spinach (Spinacia oleracea L.) leaf extracts catalyse the oxidation of formate to CO(2) and the peroxidatic action of catalase and NAD-dependent formate dehydrogenase, which is mainly, if not exclusively, located in the mitochondria.
Abstract: 1. Spinach (Spinacia oleracea L.) leaf extracts catalyse the oxidation of formate to CO2. 2. Two enzymic systems are responsible for this oxidation, the peroxidatic action of catalase (EC 1.11.1.6) and NAD-dependent formate dehydrogenase (EC 1.2.1.2). 3. Formate dehydrogenase is mainly, if not exclusively, located in the mitochondria. This enzyme has a pH optimum of 6–6.5 and a Km for formate of 1.7mm in the presence of 1 mm-NAD+. 4. Peroxidatic action of catalase is presumed to take place in peroxisomes, since these seem to be the subcellular site of catalase. Formate oxidation at pH5 by chloroplast and mitochondrial fractions is due to their ability to generate H2O2 and the presence of contaminating catalase. 5. During photorespiration, peroxidatic oxidation of formate by catalase can occur over a wide range of pH values, but the rate of this reaction is probably controlled by the concentration of formate present, to an extent dependent on the pH.
TL;DR: The results are consistent with a mechanism requiring the enzymatic decomposition of H 2 O 2 to a radical, possibly ·OH, in the biosynthesis of prostaglandins.
TL;DR: Crystalline beef liver catalase, used as an enzyme tracer, and the peroxisomal catalases have been visualized cytochemically by a modification of the 3,3'diaminobenzidine tetrahydrochloride technique, and it has been suggested that thePeroxidatic activity of catal enzyme is responsible for this reaction.
Abstract: Peroxidatic activity of catalase (E .C .1 .11 .1 .6) was discovered by Keilin and Hartree (1), and it has been firmly established that, catalase oxidizes various substrates such as ethanol, methanol, nitrite, and formate (2-4) . Crystalline beef liver catalase, used as an enzyme tracer (5), and the peroxisomal catalase (6, 7) have been visualized cytochemically by a modification of the 3,3'diaminobenzidine tetrahydrochloride (DAB)' technique of Graham and Karnovsky (8), and it has been suggested that the peroxidatic activity of catalase is responsible for this reaction (9) . The
TL;DR: New electrodes based on chemically bound enzymes are described for glucose and L-amino acids that are more sensitive than the hydrogen peroxide-based electrodes described previously, because the unstable peroxide can be consumed in several ways such as catalase decomposition or reaction with other products.
TL;DR: These in vivo studies show that microencapsulated catalase is as effective as the same assayed amount of catalases in free solution in reducing total body substrates in the form of exogenous perborates.
TL;DR: A model has been developed which predicts the rate of decomposition of peroxide and inactivation of catalase in a flow reactor and first order dependence on peroxide concentration is assumed.
Abstract: Immobilized beef liver catalase has been used in a flow reactor to decompose hydrogen peroxide; at the same time the catalase is inactivated by its substrate. A model has been developed which predicts this rate of decomposition of peroxide and inactivation of catalase. First order dependence on peroxide concentration is assumed. The model was verified by experiment for a range of operating conditions and then used to predict the effects of a change in operating variables.
TL;DR: Phenylalanine hydroxylase was prepared from rat liver and purified 200-fold to about 90% purity; it is postulated that catalase (or other peroxidase) plays a part in the hydroxolation reaction independent of the protection by catal enzyme of enzyme and cofactor from inactivation by a hydroperoxide.
Abstract: Phenylalanine hydroxylase was prepared from rat liver and purified 200-fold to about 90% purity. All the enzymic activity of the liver appeared in a single protein of mol.wt. approx. 110000, but omission of dithiothreitol and of a preliminary filtration step to remove lipids resulted in partial conversion into a second enzymically active protein of mol.wt. approx. 250000. The Km and Vmax. values of the enzyme for phenylalanine, p-fluorophenylalanine and dimethyltetrahydropterin were measured; p-chlorophenylalanine inhibited the enzyme by competing with phenylalanine. Disc gel electrophoresis at pH7.2 showed a single protein band containing all the enzymic activity, but at pH8.7 the enzyme dissociated into two inactive fragments of similar but not identical molecular weight. The molecule of phenylalanine hydroxylase contained two atoms of iron, one atom of copper and one molecule of FAD; molybdenum was absent. Treatment with chelating agents showed that both non-haem iron and copper were necessary for enzymic activity. The molecule contained five thiol groups, and thiol-binding reagents inhibited the enzyme. Catalase or peroxidase enhanced enzymic activity fivefold; it is postulated that catalase (or other peroxidase) plays a part in the hydroxylation reaction independent of the protection by catalase of enzyme and cofactor from inactivation by a hydroperoxide.
TL;DR: Organ photometry on intact hemoglobin-free perfused rat liver in order to measure Compound I selectively provides a direct insight into the dynamics of the H2O2 metabolism which takes place in the range of nanomolar concentrations.
Abstract: The marker enzyme of the peroxisome—a phylogenetically old yet only recently discovered cell organelle—is catalase, a hemoprotein which decomposes hydrogen peroxide catalatically as well as peroxidatically. In the peroxisomes, catalase is associated with H2O2-producing oxidases and other enzymes. Also in parenchymal cells such as liver and kidney cells part of the reduction of oxygen occurs via formation of H2O2. A central role in peroxisomal H2O2-metabolism is played by the active intermediate, catalase-Fe3+-H2O2, (Compound I), which is distinguished from free catalase by specific absorption bands. Organ photometry on intact hemoglobin-free perfused rat liver in order to measure Compound I selectively provides a direct insight into the dynamics of the H2O2 metabolism which takes place in the range of nanomolar concentrations. Endogenously, 1g of liver forms approximately 50 nmol of H2O2 per min. The turnover number, which in the steady state is 108 min−1 for the isolated enzyme with an excess of substrate, can be increased to approximately 102 min−1 by intracellular stimulation of the H2O2 production (e.g. by glycolate or urate). The peroxidatic oxidation of hydrogen donors (e.g. methanol and ethanol), favored relative to the catalase pathway at low turnover numbers, is of importance in normal metabolism and in pathological conditions.
TL;DR: The most straightforward interpretation of the present results is that metal ion-catalyzed oxidation of dithiothreitol produces hydrogen peroxide which oxidizes one or more critical residues in the glutamine binding site of the light subunit.
TL;DR: Catalase derived from M. tuberculosis was purified by ammonium sulfate precipitation, ion exchange chromatography, and gel filtration, and 3-Amino-1,2,4-triazole stimulates M.culosis catalase activity, in contrast to its inhibitory effect on catal enzyme from some other sources.
Abstract: Catalase derived from M. tuberculosis was purified by ammonium sulfate precipitation, ion exchange chromatography, and gel filtration. This product has a molecular weight of about 160,000, exhibits a peak absorption in the Soret band, and gives a positive reaction with benzidine. It has peroxidase-like activity at pH 7.5 but not at 4.0. Inactivation of the catalase by isoniazid or its isomer, nicotinic acid hydrazide, is intensified by cupric ion. Phosphate can protect the pure enzyme from the deleterious effect of isoniazid, and dialysis of isoniazid-inactivated catalase results in partial restoration of its activity. 3-Amino-1,2,4-triazole stimulates M. tuberculosis catalase activity, in contrast to its inhibitory effect on catalase from some other sources.
TL;DR: It is concluded that the development of peroxisomes in the cotyledons is specifically controlled by phytochrome and that this subcellular differentiation also involves the control of catalase, a marker enzyme for both glyoxysomes and peroxISomes.
Abstract: In contrast to an earlier publication (Drumm et al., Cytobiol. 2, 335, 1970), a definite enhancement by phytochrome of the catalase level in mustard (Sinapis alba L.) cotyledons can be demonstrated. This response can be obtained either with continuous far-red light or with short red pulses, the effect of which is reversible by short far-red pulses. From the comparison of the time courses of catalase activity with the time courses of glyoxysomal (isocitrate lyase) and peroxisomal (glycolate oxidase, glyoxylate reductase) marker enzymes in dark grown and far-red irradiated cotyledons, there appears to be a close relationship between the catalase present in darkness and glyoxysomes and between the phytochrome-stimulated portion of total catalase and peroxisomes, respectively. The isoenzyme pattern of catalase shows 3 strong and several weaker bands in dark grown cotyledons. Irradiation with white or far-red light leads to a more complex pattern with at least 12 detectable bands. The isoenzymes increased by light supplement rather than replace the isoenzymes present in darkness. This is true also in cotyledons and true leaves of white light grown plants which do not possess glyoxysomes. In the hypocotyl of the seedling, catalase formation is depressed by far-red light and no change in the isoenzyme pattern is observed. It is concluded that the development of peroxisomes in the cotyledons is specifically controlled by phytochrome and that this subcellular differentiation also involves the control of catalase, a marker enzyme for both glyoxysomes and peroxisomes. The implications of these results with respect to the developmental origin of peroxisomes in cotyledons of fat-storing, potentially photosynthetically active cotyledons is discussed.
Journal Article•
TL;DR: The demonstration of microbody proliferation and catalase induction with hypolipidemic compounds, CPIB, nafenopin and, in these studies, with methyl clofenapate suggests a possible but as yet unclarified relationship between microbodies and hypolIPidemia.
Abstract: The effects of the administration of methyl clofenapate (methyl-2-[4-(p-chlorophenyl)phenoxy]2-methylpropionate) on the inducibility of hepatic microbody (peroxisome) proliferation and catalase synthesis were studied in male rats and in both sexes of wild type (Csa strain) and acatalasemic (Csb strain) mice. These investigations included electron microscopic examination of livers, assay of liver catalase activity, quantitation of catalase protein by immunotitration procedure, and measurements of serum cholesterol and glyceride-glycerol levels. In all groups of animals administration of methyl clofenapate at dietary concentrations of 0.015, 0.05 and 0.125% produced a significant and sustained increase in number of hepatic microbody (peroxisome) profiles. There was no appreciable increase in mitochondrial population, but several mitochondria were markedly enlarged and possessed numerous cristae. The hepatic microbody proliferation in male rats and in both sexes of wild type mice following methyl clofenapate administration was associated with a twofold increase in catalase activity and in the concentration of catalase protein. The increase in microbody population in acatalasemic mice, however, was not accompanied by a significant elevation of the catalase activity, which is due to the unusual heat lability of the mutant catalase enzyme. A marked decrease in serum cholesterol and glyceride-glycerol levels was observed in male rats following methyl clofenapate administration which paralleled the increase in liver catalase activity. In both strains of mice there was a significant reduction in serum glyceride-glycerol concentrations. All the above effects of methyl clofenapate were fully reversed when the drug was withdrawn from the diet of male wild type mice. The demonstration of microbody proliferation and catalase induction with hypolipidemic compounds, CPIB, nafenopin and, in these studies, with methyl clofenapate suggests a possible but as yet unclarified relationship between microbodies and hypolipidemia.
TL;DR: It is concluded that glucose is the most important single culture factor determining the morphological status of M. genevensis; mitochondrial development and the functional oxidative capacities of the cell appear to be less important factors in the differentiation process.
Abstract: Mucor genevensis was grown in both glucose-limited and glucose-excess continuous cultures over a range of dissolved oxygen concentrations (<01 to 25 μM) to determine the effects of glucose and the influence of metabolic mode (fermentative versus oxidative) on dimorphic transformations in this organism The extent of differentiation between yeast and mycelial phases has been correlated with physiological and biochemical parameters of the cultures Under glucose limitation, oxidative metabolism increased as the dissolved oxygen concentration increased, and this paralleled the increase in the proportion of the mycelial phase in the cultures Filamentous growth and oxidative metabolism were both inhibited by glucose even though mitochondrial development was only slightly repressed However, the presence of chloramphenicol in glucose-limited aerobic cultures inhibited mitochondrial respiratory development but did not induce yeast-like growth, indicating that oxidative metabolism is not essential for mycelial development Once mycelial cultures had been established under aerobic, glucose-limited conditions, subsequent reversal to anaerobic conditions or treatment with chloramphenicol caused only a limited reversal (<35%) to the yeast-like form Glucose, however, induced a complete reversion to yeast-like form It is concluded that glucose is the most important single culture factor determining the morphological status of M genevensis; mitochondrial development and the functional oxidative capacities of the cell appear to be less important factors in the differentiation process
TL;DR: The catalase activity of Candida tropicalis pK 233 was induced by hydrocarbons but not by glucose, galactose, ethanol, acetate or lauryl alcohol as mentioned in this paper.
Abstract: The catalase activity of Candida tropicalis pK 233 was induced by hydrocarbons but not by glucose, galactose, ethanol, acetate or lauryl alcohol.The induction of the catalase activity depending upon hydrocarbons was sensitive to cycloheximide but not to chloramphenicol.Glucose repressed strongly the induction of the catalase activity by hydrocarbons but galactose did not affect seriously.When C. tropicalis was incubated with hydrocarbons, the appearance of microbodies was observed electronmicroscopicaliy.