Showing papers on "Catalase published in 1971"
TL;DR: Aerotolerant anaerobes, which survive exposure to air and metabolize oxygen to a limited extent but do not contain cytochrome systems, were found to be devoid of catalase activity but did exhibit superoxide dismutase activity.
Abstract: The distribution of catalase and superoxide dismutase has been examined in various micro-organisms. Strict anaerobes exhibited no superoxide dismutase and, generally, no catalase activity. All aerobic organisms containing cytochrome systems were found to contain both superoxide dismutase and catalase. Aerotolerant anaerobes, which survive exposure to air and metabolize oxygen to a limited extent but do not contain cytochrome systems, were found to be devoid of catalase activity but did exhibit superoxide dismutase activity. This distribution is consistent with the proposal that the prime physiological function of superoxide dismutase is protection of oxygen-metabolizing organisms against the potentially detrimental effects of the superoxide free radical, a biologically produced intermediate resulting from the univalent reduction of molecular oxygen.
974 citations
TL;DR: Lack of reproducibility, a feature of previous methods of measuring the susceptibility of red cells to exogenous peroxide, could be overcome by (i) catalase inhibition, (ii) attention to the non‐linear relation between packed‐cell volume and MDA formation, and (iii) elimination of potentially misleading coloured complexes on spectroscopy.
Abstract: Summary.
Malonyldialdehyde (MDA) formation, a measure of polyunsaturated fat autoxidation, was estimated in normal human red cells incubated in vitro. Exposure to oxygen under a variety of conditions did not induce autoxidation. Exposure to hydrogen peroxide was either by the addition of a hydrogen peroxide solution or by incubation in an atmosphere saturated with hydrogen peroxide vapour. A pattern of MDA formation was established with both methods. Lack of reproducibility, a feature of previous methods of measuring the susceptibility of red cells to exogenous peroxide, could be overcome by (i) catalase inhibition, (ii) attention to the non-linear relation between packed-cell volume and MDA formation, and (iii) elimination of potentially misleading coloured complexes on spectroscopy. A number of recognized antioxidants inhibited peroxide-induced MDA formation. Inhibition was proportional to the logarithm of the antioxidant concentration. Under certain conditions pre-incubation with nucleosides and with lecithin protected the cells against autoxidation on subsequent exposure to peroxide. Peroxide-induced cell autoxidation was also influenced by plasma, bovine albumin, and ascorbic acid. Haemolysis was an invariable consequence of autoxidation. Similarities and dissimilarities between autoxidation and antioxidation in free lipid emulsions and in organized biological structures were examined and discussed in the light of the experimental findings.
950 citations
TL;DR: It is concluded that the previous reports that tyrosine hydroxylase is stimulated by Fe2+ can be explained by the known ability ofFe2+ to decompose H2O2.
381 citations
TL;DR: The data show that 6-hydroxydopamine generates Hydrogen peroxide and that hydrogen peroxide can damage the biogenic amine uptake systems, and that part of the damage caused by the 6-Hydroxyopamine that accumulates in the catecholamine nerve terminals in vivo may be attributed to the hydrogenPeroxide.
Abstract: Hydrogen peroxide, dialuric acid, or 6-hydroxydopamine inhibited the uptake of dopamine, norepinephrine, and serotonin into rat brain synaptosomal preparations. The addition of catalase protected all systems, but catalase was only partially protective for 6-hydroxydopamine acting upon catecholamine uptake. The data show that 6-hydroxydopamine generates hydrogen peroxide and that hydrogen peroxide can damage the biogenic amine uptake systems. Part of the damage caused by the 6-hydroxydopamine that accumulates in the catecholamine nerve terminals in vivo may be attributed to the hydrogen peroxide.
202 citations
TL;DR: It is shown that in general, when the specific radioactivity of proteins is measured between 1 and 10 days after the injection of labeled leucine, all proteins with half-lives between 0.1 and 2 days will show apparent half-lived between 3 and 4 days, and some suggestions are made for optimizing the design of such experiments.
149 citations
TL;DR: Phagocytosis-induced formate and glucose C-1 oxidation by the polymorphonuclear leukocytes of a patient with hereditary myeloperoxidase deficiency was considerably greater than normal and the addition of catalase to the leukocyte suspension was required for optimum formate oxidation.
Abstract: Phagocytosis-induced formate and glucose C-1 oxidation by the polymorphonuclear leukocytes of a patient with hereditary myeloperoxidase deficiency was considerably greater than normal. The addition of catalase to the leukocyte suspension was required for optimum formate oxidation. Azide and cyanide increased glucose C-1 oxidation by normal leukocytes but had little or no effect on myeloperoxidase-deficient leukocytes suggesting that these agents normally stimulate glucose C-1 oxidation, in part, by inhibition of myeloperoxidase. It is suggested that the inhibition or absence of myeloperoxidase results in an increased utilization of H2O2 in nonmyeloperoxidase-mediated H2O2-dependent reactions such as formate oxidation and hexose monophosphate pathway activation. The possibility of a microbicidal control mechanism in which a decrease in the microbicidal activity of myeloperoxidase is offset, in part, by an increase in the nonenzymatic microbicidal activity of H2O2 is considered.
135 citations
TL;DR: The primary intermediate of catalase and hydrogen peroxide was identified and investigated in peroxisome-rich mitochondrial fractions of rat liver and its significant peroxidatic activity towards its endogenous hydrogen donor was suggested.
Abstract: 1. The primary intermediate of catalase and hydrogen peroxide was identified and investigated in peroxisome-rich mitochondrial fractions of rat liver. On the basis of kinetic constants determined in vitro, it is possible to calculate with reasonable precision the molecular statistics of catalase action in the peroxisomes. 2. The endogenous hydrogen peroxide generation is adequate to sustain a concentration of the catalase intermediate (p(m)/e) of 60-70% of the hydrogen peroxide saturation value. Total amount of catalase corresponds to 0.12-0.15nmol of haem iron/mg of protein. In State 1 the rate of hydrogen peroxide generation corresponds to 0.9nmol/min per mg of protein or 5% of the mitochondrial respiratory rate in State 4. 3. Partial saturation of the catalase intermediate with hydrogen peroxide (p(m)/e) in the mitochondrial fraction suggests its significant peroxidatic activity towards its endogenous hydrogen donor. A variation of this value (p(m)/e) from 0.3 in State 4 to 0 under anaerobic conditions is observed. 4. For a particular preparation the hydrogen peroxide generation rate in the substrate-supplemented State 4 corresponds to 0.17s(-1) (eqn. 6), the hydrogen peroxide concentration to 2.5nm and the hydrogen-donor concentration (in terms of ethanol) to 0.12mm. The reaction is 70% peroxidatic and 30% catalatic. 5. A co-ordinated production of both oxidizing and reducing substrates for catalase in the mitochondrial fraction is suggested by a 2.2-fold increase of hydrogen peroxide generation and a threefold increase in hydrogen-donor generation in the State 1 to State 4 transition. 6. Additional hydrogen peroxide generation provided by the urate oxidase system of peroxisomes (8-12nmol of uric acid oxidized/min per mg of protein) permits saturation of the catalase with hydrogen peroxide to haem occupancy of 40% compared with values of 36% for a purified rat liver catalase ofk(1)=1.7x10(7)m(-1).s(-1) and k'(4)=2.6x10(7)m(-1). s(-1)(Chance, Greenstein & Roughton, 1952). 7. The turnover of the catalase ethyl hydrogen peroxide intermediate (k'(3)) in the peroxisomes is initially very rapid since endogenous hydrogen peroxide acts as a hydrogen donor. k'(3) decreases fivefold in the uncoupled state of the mitochondria.
123 citations
TL;DR: Results support the view that catalase exists in the matrix of the peroxisomes and urate oxidase in the core of rat liver homogenate and find that tightness of binding of the four enzymes studied to heavy sedimentable material increased in the order.
72 citations
TL;DR: In this paper, a method for the determination of the activity of catalase in soils is described, which envolves the gasvolumetric determination of oxygen released by decomposition of a H2O2-solution by soils, suspended in buffers in the presence and absence of the Catalase inhibitor NaN3.
Abstract: The determination of Catalase Activity in Soils by Dr. Beck
1. The elaboration of a method for the determination of the activity of catalase in soils is described. The method envolves the gasvolumetric determination of oxygen released by decomposition of a H2O2-solution by soils, suspended in buffers in the presence and absence of the catalase inhibitor NaN3.
2. The influences of the following factors on catalase activity were studied: Methods for the determination of developed oxygen, enzyme- and substrate concentration, inhibition of catalase by NaN3, pH- and temperature-optima of catalase and the presence of plant residues in soils.
3. It was found, that there was only a little decrease in catalase activity when fresh or dried samples of soils were stored over a periode of 4 months under laboratory conditions. The catalase activity of different soils showed very good correspondence to the dehydrogenase activity of the soils and less correspondence to the amount of soil respiration and the amylase activity. No relation could be found to the number of microorganisms in soil.
71 citations
TL;DR: Evidence is presented that the rate of synthesis of Z(4) exceeds that of V(4), which suggests that this may be a major factor in the differential expression of the two catalase genes.
Abstract: The turnover of two homotetramers of catalase, V4 and Z4, specified by genes at two separate loci, has been studied during germination of maize seed by the techniques of density labeling and starch-gel electrophoresis. Both isozymes were shown to be turning over during this time. However, Z4 accumulates because the rate of synthesis exceeds the rate of degradation, whereas V4 slowly disappears because the rate of degradation exceeds the rate of synthesis. Evidence is also presented that the rate of synthesis of Z4 exceeds that of V4, which suggests that this may be a major factor in the differential expression of the two catalase genes.
54 citations
TL;DR: It was shown that CPIB enhances the rate of synthesis of hepatic catalase by more than 80% in three days and maintains this enhanced synthesis throughout the duration of its administration.
TL;DR: Urea-denatured hemoprotein possessed increased nonenzymatic activity due to increased exposure of the protein-bound heme, however, peroxidase increased less than catalase which is consistent with the fact that per oxidase is the more heat stable enzyme.
Abstract: Purified catalase and peroxidase were denatured by heat, acid and urea. Denaturation resulted in up to 22-fold increase in nonenzymatic lipid oxidation activity concomitant with loss of enzymatic activity. It is proposed that the increased nonenzymatic activity is due to increased exposure of the heme group. Acid-splitting of the hemoproteins into apoprotein and hemin had the greatest influence on both of the catalytic activities and recombination reversed the effect. Urea-denatured hemoprotein possessed increased nonenzymatic activity due to increased exposure of the protein-bound heme, however, peroxidase increased less than catalase which is consistent with the fact that peroxidase is the more heat stable enzyme. Nonenzymatic activity of the heat denatured hemoproteins was maximum when catalase was treated at 90 C for 2 min and peroxidase at 100 to 125 C for 5 to 30 min.
Journal Article•
TL;DR: Antisera prepared by immunizing rabbits to the blood of normal mice stabilize the mutant catalases against the effect of heat and alkaline pH, and the antigen-antibody complex exhibits a greater catalatic activity than was originally added, i.e., an apparent activation.
Abstract: This study concerns a mouse strain which is mutant with respect to blood and tissue catalase. The mutant catalase is abnormally sensitive to heat and extraordinarily sensitive to mild alkalinity. Antisera prepared by immunizing rabbits to the blood of normal mice stabilize the mutant catalases against the effect of heat and alkaline pH. As a result of this stabilization, the antigen-antibody complex exhibits a greater catalatic activity than was originally added, i.e., an apparent activation.
TL;DR: Shortly after intraportal administration of 3H-leucine to rats, label is found in the liver in a material that is precipitated by anti-catalase, but does not accompany catalase through purification.
TL;DR: Based on the mechanism postulated for the Mehler reaction in isolated chloroplasts, it was deduced that the differences in the kinetics of the O2 exchange catalyzed by methyl viologen reflect Differences in the endogenous catalase activity in these algae.
TL;DR: In this article, the hypothesis that an in situ cataloperoxidase would affect serum lipids was tested in these mutants and serum triglycerides and cholesterol were found to be significantly lower than in the wild strain.
Abstract: Mutant "acatalasemicm" mice have an unstable catalase in hepatic and renal peroxisomnes that is readily degraded, apparently into peroxidase subunits. The hypothesis that an in situ cataloperoxidase would affect serum lipids was tested in these mutants and serum triglycerides and cholesterol were found to be significantly lower than in the wild strain. This finding is in accordance with reports that a hypolipidemic response to the injection of peroxidase subunits of hepatic catalase occurs in humans and rabbits.
TL;DR: The renewal of catalase activity in C57BL/6J male mice of different ages was followed for 24 h after the removal of activity with 3-amino-1,2,4,-triazole (AT) and the return of activity after injection of AT.
Abstract: The renewal of catalase activity in C57BL/6J male mice of different ages was followed for 24 h after the removal of activity with 3-amino-1,2,4,-triazole (AT). The return of activity after injection o
TL;DR: Chronic granulomatous disease PMN, which lack a respiratory burst and fail to generate H( 2)O(2) during phagocytosis and do not kill catalase positive bacteria, had peroxide-generating amino acid oxidase activity equal to that found in PMN homogenates from patients with bacterial infections.
Abstract: D-Amino acid oxidase and L-amino acid oxidase have been measured in sucrose homogenates of polymorphonuclear leukocytes (PMN) obtained from guinea pigs and humans. Subcellular distribution patterns and studies on latency indicate that these oxidases are soluble enzymes. Their hydrogen peroxide-generating capacity was verified. Chronic granulomatous disease PMN, which lack a respiratory burst and fail to generate H2O2 during phagocytosis and do not kill catalase positive bacteria, had peroxide-generating amino acid oxidase activity equal to that found in PMN homogenates from patients with bacterial infections. The precise metabolic and bactericidal role of amino acid oxidases in PMN remains uncertain.
TL;DR: The results indicate that bursts of peroxisomal synthesis occur during the development of the mouse liver, particularly in the early postnatal stages and during maturation.
Abstract: PEROXISOMES are cytoplasmic organelles which occur in liver and kidney cells of higher animals and in lower forms of life. They have a unique enzyme composition and function in the oxidation of specific substrates by oxidases1. Catalase (hydrogen peroxide: hydrogen peroxide oxidoreductase E.C. 1.11.1.6) is an essential component of this oxidizing system which facilitates the catalytic or peroxidatic destruction of hydrogen peroxide. Large granular catalase activity serves as a marker for the organelle and has been used here to describe the ontogeny of peroxisomes in mouse liver. The results indicate that bursts of peroxisomal synthesis occur during the development of the mouse liver, particularly in the early postnatal stages and during maturation.
TL;DR: The assay described in the chapter is based on the oxygen consumption obtained with tyramine as the substrate in the presence of added catalase, and discusses purification procedure and properties.
Abstract: Publisher Summary This chapter focuses on tyramine oxidase (Sarcina lutea). Tyramine oxidase catalyzes the oxidation of tyramine and dopamine with the consumption of 1 mole of oxygen, and the production of 1 mole of aldehyde, 1 mole of ammonia, and 1 mole of hydrogen peroxide. In the presence of the catalase, hydrogen peroxide is converted to water and 0.5 mole of oxygen. The assay described in the chapter is based on the oxygen consumption obtained with tyramine as the substrate in the presence of added catalase. The chapter also discusses purification procedure and properties.
Patent•
19 Nov 1971
TL;DR: In this article, a process for quantitively determining uric acid in blood with uricase characterized by making microbe-originated URICase act on uric acids in blood in the presence of a catalase inhibitor and a buffer effective to maintain the pH at 5.5 to 7.0 was proposed.
Abstract: A process for quantitively determining uric acid in blood with uricase characterized by making microbe-originated uricase act on uric acid in blood in the presence of a catalase inhibitor and a buffer effective to maintain the pH at 5.5 to 7.0 and measuring the quantity of the generated hydrogen peroxide under a condition of a pH of 4.0 to 7.0 in the presence of an anionic surface active agent, a chromogen developing a color with hydrogen peroxide and a substance having a function of separating free oxygen from hydrogen peroxide and catalysing the oxidation of the chromogen.
TL;DR: It is suggested that either hydrogen peroxide or an organic peroxide formed by oxidation in air of the cofactor is the substance attacking phenylalanine hydroxylase, dithiothreitol and cofactor.
Abstract: 1. Phenylalanine hydroxylase is inhibited by its cofactor, 6,7-dimethyltetrahydropterin. The rate of inactivation, which is irreversible, increases with the concentration of cofactor. 2. Catalase, in sufficient amount relative to cofactor, prevents this inactivation. More tyrosine is formed in the presence of added catalase. 3. Dithiothreitol in the presence of liver extract also prevents inactivation of the enzyme by the cofactor and stimulates hydroxylation of phenylalanine, probably by protecting the cofactor from oxidation and regenerating it from a dihydropterin reaction product. Dithiothreitol restores linearity of rate at very low enzyme concentrations. 4. Dimethyltetrahydropterin is unstable when the solution is exposed to air but is stabilized by dithiothreitol the aerobic oxidation of which is greatly accelerated by dimethyltetrahydropterin. 5. NADH together with liver extract stabilizes the cofactor but not phenylalanine hydroxylase. 6. It is suggested that either hydrogen peroxide or an organic peroxide formed by oxidation in air of the cofactor is the substance attacking phenylalanine hydroxylase, dithiothreitol and cofactor.
TL;DR: Normale und anomale Katalase-Varianten mit identischer elektrophoretischer Wanderungsgeschwindigkeit konnten durch unterschiedliche Harnstoff- und Temperatur-Wirkung voneinander untersichert werden.
Abstract: Normale und anomale Katalase-Varianten mit identischer elektrophoretischer Wanderungsgeschwindigkeit konnten durch unterschiedliche Harnstoff- und Temperatur-Wirkung voneinander unterschieden werden.
TL;DR: It was observed that two reactive chemical species (peroxide and permanganate) can coexist in stream form within a tube and similar behaviour between blood catalase and infused peroxide may also be possible.
Abstract: SummaryTo ascribe the therapeutic benefits following simultaneous peroxide infusion and radiotherapy to the oxygen effect is to assume that the infused peroxide breaks down very rapidly. The literature gives disparate values for the rate of decomposition of peroxide, one supporting the oxygen effect, the other consonant with a ‘peroxide effect’.In vitro experiments with model systems simulating in vivo flow conditions have been used to examine the mixing of infusate in a stream of flowing fluid. Mixing has been shown to be imperfect even after one second has elapsed. The effect of imperfect mixing on the decomposition rate has been discussed.Infusion through an epidural cannula produces little or no turbulence to assist mixing.It was observed that two reactive chemical species (peroxide and permanganate) can coexist in stream form within a tube. Similar behaviour between blood catalase and infused peroxide may also be possible.The decomposition of peroxide infused into flowing blood is examined directly i...
TL;DR: If potato peroxidase or catalase activity differed in various parts of the tuber, if these activities could be associated with resistance or susceptibility of the tissue to blackspot, and if certain relationships could be established to predict the response of potato tissue to bruising were determined.
Abstract: Peroxidase and catalase activities in selected potato tuber tissue were studied for differences and possible association with resistance or susceptibility to blackspot. Unbruised stem-end tissue had significantly greater peroxidase activity than did unbruised bud-end tissue. However, there was no significant difference between catalase activity at either end of the tuber; between blackspot susceptibility and peroxidase or catalase activity; and between blackspot susceptible or resistant tissue and the ratio of either catalase or peroxidase to phenolase activity. Bruising did not cause significant changes in either peroxidase or catalase activity or in ratios between these enzymes and phenolase that could be associated with susceptibility or resistance of tissue to blackspot.
TL;DR: Proteinase has been isolated from pig liver, puriSed and crystallized from ammonium sulfate solutions and nucleases are used in the purification procedure and enhance the yields in both quantity and purity.
Abstract: Catalase has been isolated from pig liver, puriSed and crystallized from ammonium sulfate solutions. Nucleases are used in the purification procedure and enhance the yields in both quantity and purity. The enzyme has a molecular weight of 241,000 and contains 4 hemes per molecule. The enzyme has a wide pH range of activit,r with 8.0 being the optimum value. Maximum activity is achieved at an ionic strength of 0.1 M.
Journal Article•
TL;DR: It is hypothesized that the unstable catalase protein with genetical change in structure easily decomposes during acatalasemic reticulocyte maturation.
Abstract: The concentration of catalase protein in anemic blood with enhanced population of reticulocytes and in non-anemic blood was determined immunologically by double diffusion test with anti-mome-liver catalase rabbit serum. The change in catalase protein concentration in anemic blood during incubation at 37°C for 24 hours was also studied. It was indicated that the diminished catalase activity in acatalasemic blood was due to the depletion of the protein and that catalase protein in acatalasemic reticulocytes decreased markedly by in vitro maturation. Furthermore, the possible presence of inactive catalase protein in acatalasemic blood was also suggested. Catalase protein concentration of acatalasemic anemic blood
decreased by the incubation at 37°C for 24 hours in parallel with the decrease in reticulocyte count and catalase activity, and the decrease in catalase protein concentration of hemolysate by the same incubation parallel with the decrease in catalase activity. It is hypothesized that the unstable catalase protein with genetical change in structure easily decomposes during acatalasemic reticulocyte maturation is presented.