Showing papers on "Catalase published in 1970"
1,088 citations
TL;DR: The existence of a microsomal ethanol-oxidizing system, especially its capacity to increase in activity adaptively after ethanol feeding, may explain various effects of ethanol, including proliferation of hepatic smooth endoplasmic reticulum, induction of other hepaticmicrosomal drug-detoxifying enzymes, and the metabolic tolerance to ethanol which develops in alcoholics.
800 citations
TL;DR: Results indicate that Compound I of chloroperoxidase may contain a reactive oxygen atom, and by analogy with organic mechanisms for the decomposition of peracids, these results indicate that the enzyme also oxidizes ethanol to form acetaldehyde.
194 citations
TL;DR: Inhibitor production paralleled H2O2 formation in Lactobacillus cultures, further indicating that the observed inhibition resulted from H2 O2 produced by lactobacilli.
Abstract: Eighty-one microbial species isolated from seafoods and other marine sources were examined to determine the extent of interactions among these species. Spot-plates, cross-plates, and concurrent growth experiments at 7, 15, 20, and 30 C indicated that Lactobacillus species were capable of inhibiting other microorganisms. Lactobacillus species isolated from oysters and identified as Lactobacillus plantarum produced a substance inhibitory to Pseudomonas, Bacillus, and Proteus species, the most sensitive being Pseudomonas. The inhibitory substance accumulated in Lactobacillus culture media, reaching maximum concentrations in 4 to 5 days at 30 C. The active substance was dialyzable, heat labile, and inactivated by catalase. Inhibitor production paralleled H2O2 formation in Lactobacillus cultures, further indicating that the observed inhibition resulted from H2O2 produced by lactobacilli. These findings may explain the abnormal shifts in microbial flora observed in foods where Lactobacillus species have overgro...
153 citations
TL;DR: The spectral changes caused by the addition of hydrogen peroxide and halide salts to chloroperoxidase have been investigated and discussed in relation to the halogenation activity of the enzyme.
127 citations
TL;DR: It is suggested that γ-butyrobetaine is hydroxylated to carnitine simultaneously with the oxidative decarboxylation of 2-ketoglutarate in a reaction sequence which involves the intermediate formation of a peroxide of the two substrates.
118 citations
TL;DR: It is concluded that, while catalase-dependent H( 2)O(2) metabolism is not essential for particle entry, this pathway represents one of the metabolic pathways stimulated by particle entry in the AM.
Abstract: EVIDENCE FOR THE PRESENCE OF PEROXIDATIVE METABOLISM IN RABBIT ALVEOLAR MACROPHAGES (AM) HAS BEEN OBTAINED FROM THE FOLLOWING OBSERVATIONS: (a) catalase is present in high concentrations; (b) peroxidase activity could not be detected employing guaiacol as substrate; (c) the irreversible inhibition of AM catalase by aminotriazole served as a detection system for H(2)O(2) and demonstrated increased intracellular H(2)O(2) after phagocytosis; (d) formate oxidation, a marker of catalase-dependent peroxidations, occurs in resting AM and is increased by phagocytosis; (c) measurements of H(2)O(2) accumulation in a dialysate of AM demonstrated twofold increase during phagocytosis; and (f) aminotriazole diminishes O(2) utilization and (14)CO(2) production from labelled glucose and pyruvate. It is concluded that, while catalase-dependent H(2)O(2) metabolism is not essential for particle entry, this pathway represents one of the metabolic pathways stimulated by particle entry in the AM.
108 citations
TL;DR: Prolonged consumption of ethanol enhances the activities of the hepatic microsomal ethanol oxidizing system and of reduced nicotinamide-adenine dinucleotide phosphate oxidase, but not of catalase.
Abstract: Prolonged consumption of ethanol enhances the activities of the hepatic microsomal ethanol oxidizing system and of reduced nicotinamide-adenine dinucleotide phosphate oxidase, but not of catalase. The oxidase-catalase system is not part of the microsomal ethanol oxidizing system since catalase inhibitors dissociate ethanol oxidation by the two pathways. Enhanced reduced nicotinamide-adenine dinucleotide phosphate oxidase activity may contribute to liver injury, possibly by favoring lipoperoxidation.
100 citations
TL;DR: Tests showed the uterine fluid-iodide-hydrogen peroxide system suspended spermatozoa was inhibited by catalase and by such low-molecular-weight compounds as azide reduced glutathione cysterine ergothioneine and ascorbic acid, which suggests that its sperm inhibitory effect is due to its perioxidase content.
Abstract: The report suggests that uterine fluid under certain conditions exerts a sperm inhibitory effect. The addition of rat uterine fluid iodide and hydrogen peroxide to washed spermatozoa suspended in a calcium ion-free Krebs-Ringer phosphate fructose medium pH 6.5 resulted in an inhibition of motility which was complete in 10 min. When the spermatozoa were incubated in medium alone they remained fully motile for 2 hr. Deletion of hydrogen peroxide from the system abolished the sperm-inhibitory effect. Some inhibition of motility was evident on prolonged incubation when either uterine fluid or iodide was deleted. Thiocyanate could substitute for iodide and glucose and glucose oxidase could substitute for hydrogen peroxide giving 94% and 95% inhibition respectively. The uterine fluid could be replaced by a preparation of LPO (lactoperoxidase) or less effectively by MPO (myeoperoxidase). This suggests that its sperm inhibitory effect is due to its perioxidase content. The uterine fluid-iodide-hydrogen peroxide system suspended spermatozoa resulted in a decrease in pyruvate oxidation. Unwashed spermatozoa were unaffected by the system suggesting inhibitors in seminal plasma. This was born out by tests which showed the system was inhibited by catalase and by such low-molecular-weight compounds as azide reduced glutathione cysterine ergothioneine and ascorbic acid. Heat-stable low-molecular-weight inhibitors are found in seminal plasma and to a lesser degree in uterine fluid.
54 citations
TL;DR: Catalase was crosslinked to a water-insoluble network by treatment with a bifunctional reagent, glutardialdehyde, and the insoluble enzyme was stable for several months at 4 °C.
52 citations
TL;DR: The comparative efficiency of a number of solubilization procedures was studied, and blending with 0.05 per cent Triton X-100 was demonstrated as the most efficient means of releasing paniculate catalase activity.
TL;DR: In a suspension culture of peanut cotyledons the rate of protein synthesis decreased as the cell mass increased in diameter, with a decrease in free amino acids except in a cell mass of 0.15–0.5 mm.
Abstract: In a suspension culture of peanut cotyledons (Arachis hypogaea L.) the rate of protein synthesis decreased as the cell mass increased in diameter, with a decrease in free amino acids except in a cell mass of 0.15–0.5 mm. A high level of catalase and low level of peroxidase activity was related to a higher rate of protein synthesis in single cell ( 0.5 mm in diameter. Another peroxidase isozyme appeared in a cell mass of 2–4 mm in diameter. Quantitatively there was a significant increase in peroxidase with a decrease in catalase activity between cell clumps of increasing sizes.
TL;DR: The results suggest strongly that microbody proliferation is dependent not on catalase synthesis but on synthesis of non-enzymatic protein.
Abstract: The relationship between the formation of microbodies and catalase synthesis in the hepatic cells of male rats was examined with conventional electron microscopy and with the peroxidase staining technic for demonstrating catalase. Daily intraperitoneal injections of ethyl-α-p-chlorophenoxyisobutyrate (CPIB) for 5 days caused a profound increase in microbody numbers without markedly affecting the appearance of the matrix material and all microbodies retained peroxidase activity. A single injection 5 days before sacrifice of 3-amino-1,2,4-triazole (AT), an inhibitor of catalase activity but not catalase synthesis, did not affect their numbers, appearance of matrix material or peroxidase staining. Twice daily injection for 5 days of allylisopropylacetamide (AIA), an inhibitor of catalase synthesis, also did not affect microbody numbers but lowered the electron-density of the microbody matrix and abolished peroxidase staining. After combined administration of these drugs, the number of hepatic microbodies increased but they did not contain peroxidase activity. The results suggest strongly that microbody proliferation is dependent not on catalase synthesis but on synthesis of non-enzymatic protein.
TL;DR: An enzyme activity acting at neutral pH's capable of degrading native cytoplasmic protein to peptide and amino acids has been demonstrated in the peroxisome fraction of rat liver.
TL;DR: This chapter describes the procedure for the preparation and assay of catalase and a mechanism involving the inactivation ofCatalase (due to disintegration of the protein) by free radicals generated during the auto-oxidation of ascorbate.
Abstract: Publisher Summary This chapter describes the procedure for the preparation and assay of catalase. The inhibition of catalase by ascorbate is described in the chapter. A mechanism involving the inactivation of catalase (due to disintegration of the protein) by free radicals generated during the auto-oxidation of ascorbate is discussed in the chapter. The presence of divalent cations (particularly Cu2+ and Fe2+) and Fe3+ during the auto-oxidation greatly increases this inhibition. Catalytic activity is determined by measuring the decrease in absorbance at 240mμ when catalase is incubated with H2O2. The measurements can be made manually or, more simply, by a recording spectrophotometer. Assay procedure involves the detection of inhibition of catalase by ascorbate and factors affecting the inhibition.
TL;DR: The hemoproteins catalase and peroxidase, after heat treatment which decreased their enzyme activities, became more efficient as heme catalysts of linoleic acid oxidation.
Abstract: The hemoproteins catalase and peroxidase, after heat treatment which decreased their enzyme activities, became more efficient as heme catalysts of linoleic acid oxidation. These effects might be of importance for preservation and storage of food.
TL;DR: The results indicate that the inactivated catalase of the acatalasemic mutant is an active peroxidase that oxidizes both diaminobenzidine and benzidine at neutral and alkaline pH and at 15 and 37°C and is resistant to theCatalase inhibitor, 3 amino-1,2,4-triazole.
Abstract: Peroxisomes (microbodies) of a strain of acatalasemic mice (Csb) are, paradoxically, more rapidly and intensely stained than those of the wild type (Csa) when incubated in a diaminobenzidine medium that demonstrates the peroxidatic activity of catalase. Biochemical studies have shown that the mutant catalase is unstable and is rapidly inactivated by heat with loss of catalatic activity. Our results indicate that the inactivated catalase of the acatalasemic mutant is an active peroxidase that oxidizes both diaminobenzidine and benzidine at neutral and alkaline pH and at 15 and 37°C and is resistant to the catalase inhibitor, 3 amino-1,2,4-triazole.
TL;DR: An amine oxidase was purified from bovine aorta approximately 150-fold and actively catalyzed the oxidation of benzylamine, simple alkylamines, but not tryptamine, histamine, or tyramine.
TL;DR: The conversion of fraction A of both species to fraction C is characterized by a decrease in the number of sulfhydryl groups titratable in 8 M urea, and the resulting difference between fraction A and C is larger in the horse enzyme than in human catalase.
Abstract: Publisher Summary This chapter discusses a study to examine molecular variations in erythrocyte catalase. Residual catalase activity in reticulocyte enriched fractions of acatalasemic blood was plotted against the reticulocyte count in the assayed samples. The linear relationship obtained points to a direct correlation between these two parameters. Erythrocytes of normal and acatalasemic blood were fractionated according to density and cell age and subsequently were treated with fluorescent anticatalase. In samples of normal blood all cells, independent of cell age showed an intense fluorescence. In acatalasemic blood, however, a distinct pseudomosaicism was observed. The fraction with the highest percentage of reticulocytes also contained the largest number of catalase positive cells. The conversion of fraction A of both species to fraction C is characterized by a decrease in the number of sulfhydryl groups titratable in 8 M urea. The resulting difference between fraction A and C is larger in the horse enzyme than in human catalase. Possible oxidation products of sulfhydryl groups are disulfide bridges and sulfinic or sulfonic acids
TL;DR: It is particularly significant that the genetic factor affecting the amount of liver catalase does so by altering the rate ofCatalase degradation rather than the rates of synthesis, confirming the previously published report of Rechcigl and Heston (1967).
Abstract: An examination of three inbred strains of mice differing with respect to liver and kidney catalase activity reveals two distinct genetic factors controlling the level of liver catalase activity. The first genetic factor controls the catalytic activity of the enzyme. Specific activity of purified enzyme from C57BL/6 and C57BL/Ha strains is 60% of that of the DBA/2 strain. The second factor controls the content of liver catalase. Liver catalase of C57BL/Ha is degraded in vivo at a rate one half that of liver catalase of DBA/2 and C57BL/6, resulting in the accumulation of twice as many catalase molecules in C57BL/Ha. The factor affecting turnover of catalase is apparently specific for catalase of liver since no differences exist in kidney catalase levels between C57BL/Ha and C57BL/6. Furthermore, this factor does not appear to alter the metabolism of total liver protein since no substantial difference in the turnover rate of liver protein is observed among the strains. It is particularly significant that the genetic factor affecting the amount of liver catalase does so by altering the rate of catalase degradation rather than the rate of synthesis, confirming the previously published report of Rechcigl and Heston (1967). Thus, these studies emphasize that the quantity of an enzyme in animal cells is a balance between the rate of synthesis and the rate of degradation of the enzyme.
TL;DR: Suspensions of Vicia faba chloroplasts exhibit a light-dependent O2 uptake instead of an evolution, and it is suggested that some endogenous components become reduced during illumination and then act as hydrogen donors for a peroxidase reaction mediated by the chloroplast catalase system.
TL;DR: The use of sulphur-35 labelled thiocyanate demonstrated the production of sulphite and sulphate reaction products in the peroxidative system, however, these products were not demonstrable in the non-peroxidatives inhibitory system.
TL;DR: The significant improvement in in vitro livability at 37°C by the addition of amylase in the absence of catalase was minor compared to the improvement in livability obtained by the additions of catAlase and Caprogen.
Abstract: Four ejaculates from each of three bulls were diluted in four ambient temperature extenders: (1) Caprogen; (2) Caprogen containing 8 fl-gfml ",·amylase; (3) Caprogen containing 4·5 fl-gfml catalase; and (4) Caprogen containing amylase and catalase. The conception rate (49·day % non-return rate) for each extender was 64·63; 63·37; 64·58; and 66·09% respectively. Whereas the addition of catalase significantly increased conception rates (P = 0·025), the addition of amylase did not (P > 0·25). There was a significant enzyme interaction, suggesting that any beneficial effect attributable to the amylolytic preparation was only exerted in the presence of catalase (P < 0·025). The significant improvement in in vitro livability at 37°C by the addition of amylase in the absence of catalase was minor compared to the improvement in livability obtained by the addition of catalase
TL;DR: In this paper, the rate of oxidation of tyrosine, p-cresol and catechol by potato enzyme diminished as H2O2 concentration increased, and increased with the presence of catalase.
Abstract: The rate of oxidation of tyrosine, p-cresol and catechol by potato enzyme diminished as H2O2 concentration increased. By contrast, the rate of oxidation of chlorogenic acid in the presence of H2O2 increased. Bovine catalase destroyed H2O2 and thus effectively prevented either H2O2-induced inhibition or acceleration of oxidation of the four substrates by potato enzyme. Horseradish peroxidase in the presence of H2O2 did not oxidize either monophenol, but oxidized both polyphenols. Possible association of H2O2, peroxidase and catalase with blackspot susceptibility is discussed.
Patent•
26 Oct 1970TL;DR: For the production of POSITIVE PHOTOGRAPHIC images, Laysers are used LAYERS CONTAINing CATALASE ACTIVE and/or PEROXIDAS ACTIVE ENZYMES, WHICH are inactivated on EXPOSURE TO LIGHT, thus becoming unable of DECOMPOSING PEROXIDE COMPOUNDS as mentioned in this paper.
Abstract: FOR THE PRODUCTION OF POSITIVE PHOTOGRAPHIC IMAGES ARE USED LAYERS CONTAINING CATALASE ACTIVE AND/OR PEROXIDASE ACTIVE ENZYMES, WHICH ARE INACTIVATED ON EXPOSURE TO LIGHT, THUS BECOMING INCAPABLE OF DECOMPOSING PEROXIDE COMPOUNDS. THE PEROXIDE COMPOUNDS ARE USED EITHER TO FORM AN IMAGE OF GAS BUBBLES IN THE LAYER OR TO PRODUCE A DYE IMAGE BY A COLOR-FORMING OXIDATION REACTION. THE SENSITIVITY CAN LARGELY BE INCREASED BY SUBSTANCES WHICH ON EXPOSURE TO LIGHT LIBERATE HALOGEN OR CYANIDE, WHICH LATTER PRODUCTS ACTS AS POISONS FOR THE ENZYMES.
Patent•
28 Sep 1970TL;DR: An InERT, WETTABLE (By An AQUEOUS System) BIBULOUS (Interconnected PORE System) MATERIAL with a Stable, SOLID SUBSTance ABLE TO RELEASE HYDROGEN PEROXIDE UPON DISSOLUTION THEREOF in an AQUEous System is SPECIFICALLY DESCRIBED for IMPROVED RESPonCE in the QUANTITATIVE and QUALITative DETERMINATION OF CATalase by DISC FLOTATION.
Abstract: AN INERT, WETTABLE (BY AN AQUEOUS SYSTEM) BIBULOUS (INTERCONNECTED PORE SYSTEM) MATERIAL IMPREGNATED WITH A STABLE, SOLID SUBSTANCE ABLE TO RELEASE HYDROGEN PEROXIDE UPON DISSOLUTION THEREOF IN AN AQUEOUS SYSTEM IS SPECIFICALLY DESCRIBED FOR IMPROVED RESPONCE IN THE QUANTITATIVE AND QUALITATIVE DETERMINATION OF CATALASE BY DISC FLOTATION. THE SPECIFIC CONSTRUCTION DESCRIBED IS PARTICULARLY ADAPTED TO QUICK-SCREENING TESTS FOR THE DETECTION OF BACTERIURA AND/OR RENAL PATHOLOGY.
TL;DR: An inverse correlation between morphological, immunochemical characteristics (reflecting the extent of malignancy) of the hepatomas studied and the activity of the two forms of catalase was found and one infers that experimental data available do not favour the view of their being isozymes.