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

Catalase, peroxidase and superoxide dismutase were found to inhibit significantly carrageenin edema and the primary phase of adjuvant arthritis in rats after i.v. injection. Heat-inactivated enzymes were as effective as the native enzymes. None of 10 scavengers of oxygen radicals inhibited the adjuvant arthritis at any time. Accordingly, no evidence for a participation of oxygen radicals in the secondary arthritis phase could be found, whereas a role of oxygen radicals in the primary arthritis phase and in carrageenin edema cannot be ruled out.
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PMID:Effects of catalase, peroxidase, superoxide dismutase and 10 scavengers of oxygen radicals in carrageenin edema and in adjuvant arthritis of rats. 732 41

A reliable method for the determination of uric acid in plasma or serum is described. The hydrogen peroxidase developed in the uricase reaction is used, together with peroxidase, for the coupling of sulphonated dichlorophenol and 4-aminoantipyine to a red dye. The difference in absorbance at 515 nm before and after addition of uricase is measured. Of the components tested for interference some gave rise to falsely lowered values. Reagents are cheap and the high molecular absorption coefficient of the red dye permits the use of small sample volumes.
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PMID:Determination of uric acid with uricase and peroxidase. 735 49

Peroxidase from Leptospira biflexa strain B-16 ad catalase from Leptospira interrogans canicola Hond Utrecht were characterized and compared and both appeared to be heme enzymes as judged by their inhibition profiles and rapid inactivation during catalysis. Neither enzyme exhibited monovalent or divalent cation requirements. Dialysis of cell-free extracts resulted in loss of peroxidase activity but catalase was unaffected by this procedure. Peroxidase had a Km for H2O2 of 12.5 microM while catalase had a Km of 70 mM for H2O2. Catalase and peroxidase were physically separated by sedimentation in linear sucrose gradients. The specific activities of each enzyme seemed to be a function of the state of growth at which the cells were harvested and both enzymes were found associated with membranes, peroxidase by hydrophobic and catalase by ionic interactions. Speculative deductions are presented concerning the phylogenetic interrelationships of both enzymes as well as their significance in the biology and pathogenicity of leptospires.
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PMID:Characterization of leptospiral catalase and peroxidase. 740 1

1. Mitochondrial H2O2 formation is not in equilibrium with defence mechanisms that counteract an accumulation of H2O2 in rat-heart cells. 2. A model for the accumulation kinetics is proposed which is consistent with the data presented. 3. Four different pathways of H2O2 metabolism are described in rat-heart mitochondria. The major site for metabolic branching of H2O2 via different routes was found to be the mitochondrial catalase. 4. Glutathione (GSH) peroxidase accounts for only 15% of intramitochondrial H2O2 metabolism, while catalase-mediated destruction is four times more rapid. 5. Catalase activity is limited by its structural compartmentation in the matrix, while GSH peroxidase activity was found to be dependent on the availability of free GSH. 6. Catalase was shown to protect rat-heart mitochondria from upsetting redox states of GSH and pyridine nucleotides following H2O2 decomposition by GSH peroxidase. 7. Computer simulations of experimental data suggest the existence of a third sink for mitochondrial H2O2, possibly due to mitochondrial formation of OH . radicals; another fraction of the H2O2 matrix pool may cross the mitochondrial membrane and accumulate in the cytosol.
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PMID:The metabolic fate of mitochondrial hydrogen peroxide. 743 85

On incubation with catalase diperoxovanadate was found to be degraded, showing a decrease in its absorbance at 356 nm and a loss of its peak with a chemical shift at -706 ppm in its 51V NMR spectrum. The products of the reaction had an absorption peak at 266 nm and chemical shifts at -569 and -578 ppm in NMR spectra assigned to dimer and tetramer of vanadate, respectively. Catalase released half the molecular equivalent of oxygen during this degradation of diperoxovanadate with a rate two orders of magnitude lower than that seen with H2O2. By substituting for and not releasing H2O2, diperoxovanadate supported scopoletin oxidation by horseradish peroxidase, as indicated by the reaction being not sensitive to catalase, unlike that seen with H2O2. Catalase-dependent oxygen release was sensitive to azide with both H2O2 and diperoxovanadate as substrates, whereas EDTA selectively inhibited this reaction with diperoxovanadate. The results bring out the potential of catalase in degrading diperoxovanadate and suggest caution in the use of this enzyme to destroy excess H2O2 during preparation of this compound.
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PMID:Catalase degrades diperoxovanadate and releases oxygen. 764 74

Serum concentrations of triiodothyronine (T3), thyroxine (T4) and thyroid-stimulating hormone (TSH) were measured in 127 patients with chronic heart failure (CHF) (left ventricular ejection fraction; 40% < or = and NYHA; III-IV), and 1,079 patients without CHF (non-CHF) (left ventricular ejection fraction; 40% < or = and NYHA; I-II). Serum-T3, T4 and free-T4 were significantly decreased in patients with CHF. The prevalence of slight increase of serum TSH (5 < or = TSH < 15 microU/ml) were 20.5% in CHF and 4.08% in non-CHF. There was a statistically significant difference in the prevalence of slight increase of TSH (p < 0.01). In the patients with slight increase of serum TSH, the 123I-thyroid scintigraphy and perchlorate test were performed 12 patients with CHF and 19 patients with non-CHF. The incidences of iodine organification defect were 33.3% in CHF and 5.26% in non-CHF. There was a statistically significant difference in the incidence of iodine organification defect (p < 0.05). The histologic examination of thyroid biopsy specimen obtained 12 patients with CHF and primary hypothyroidism, these revealed only non-specific mild atrophic changes. Follicular damage and lymphocyte-infiltration were not evident. These findings suggest that the primary hypothyroidism were frequently complicated in CHF and associated with iodine organification defect by reduction of thyroid-peroxidase activity or decrease of hydrogen peroxidase. We conclude that the primary hypothyroidism with iodine organification defect was probably developed as a result of CHF.
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PMID:[Thyroid hormones and thyroid-stimulating hormone in patients with chronic heart failure--relationship between primary hypothyroidism with iodine organification defect and chronic heart failure]. 773 54

Catalase-peroxidase was purified to near homogeneity from Streptomyces sp. The enzyme was composed of two subunits with a molecular mass of 78 kDa and contained 1.05 mol of protoporphyrin IX/mol of dimeric protein. The absorption and resonance Raman spectra of the native and its cyano-enzyme were closely similar to those of other heme proteins with a histidine as the fifth ligand. However, the peak from tyrosine ring at approximately 1612 cm-1, which is unique in catalases, was not found in resonance Raman spectra of catalase-peroxidase. The electron paramagnetic resonance spectrum of the native enzyme revealed uniquely two sets of rhombic signals, which were converted to a single high spin, hexacoordinate species after the addition of sodium formate. Cyanide bound to the sixth coordination position of the heme iron, thereby converting the enzyme to a low spin, hexacoordinate species. The time-dependent inactivation of the enzyme with diethyl pyrocarbonate and its kinetic analysis strongly suggested the occurrence of histidine residue. From the above-mentioned spectroscopic results and chemical modification, it was deduced that the native enzyme is predominantly in the high spin, ferric form and has a histidine as the fifth ligand.
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PMID:Spectral characterization and chemical modification of catalase-peroxidase from Streptomyces sp. 777 29

5,8,11,14-eicosatetraynoic acid (ETYA), an isomorphic competitive analogue of arachidonic acid, spontaneously generates a chemiluminescence signal detected with a liquid scintillation spectrometer operated at ambient temperature in the out-of-coincidence mode. The intensity of the signal was 10- or more-fold above background, required oxygen for its generation, was inhibited by antioxidants, and approximately doubled in D2O. Arachidonic acid, which contains 4-alkene rather than alkyne bonds did no more than double the chemiluminescent signal above background. When examined at 37 degrees C in a Berthold AutoLumat 958 luminometer, DBA (lucigenin) was required to detect a signal above background. Catalase or peroxidase, and to a lesser extent mannitol or histidine but not superoxide dismutase, strongly diminished the signal intensity. These observations provide a baseline for interpreting the functional and electron microscopic changes produced by ETYA in PC3 prostate and A172 glioblastoma cell lines, consistent with a contribution from oxidative stress associated with free radicals, and the absence of these morphological changes in U937 monoblastoid cells.
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PMID:Spontaneous chemiluminescence of ETYA (5,8,11,14-eicosatetraynoic acid) is inhibited by catalase or peroxidase. 784 95

Streptomyces coelicolor ATCC 10147 produced catalases whose electrophoretic mobility varied depending on the growth phase in liquid culture. Polyacrylamide gel electrophoresis of cell extracts resulted in six catalase activity bands, which were designated Cat1 to Ca6. Of these, Cat4 appeared during all growth phases, whereas Cat1 appeared only during the stationary phase. Catalase-deficient mutants were screened by the H2O2 bubbling test following NTG mutagenesis. In all the non-bubbling mutants tested, the Cat4 activity band significantly decreased or disappeared, suggesting that Cat4 is the major catalase. Cat4 was purified to electrophoretic homogeneity and some of its properties analysed. The enzyme has a native molecular mass of 225 kDa, as determined by gel permeation column chromatography, and consists of four identical subunits of 57 kDa, as determined by SDS-PAGE. The enzyme contains 2.6 molecules of protohaem IX per tetramer, as indicated by the absorption spectrum. It was not reducible by sodium dithionite and exhibited no peroxidase activity with o-dianisidine as the substrate. All these characteristics, as well as inhibitor studies, indicate that the major vegetative catalase in S. coelicolor, unlike E. coli vegetative catalase, is a member of the typical monofunctional catalases found in eukaryotes and some bacteria.
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PMID:Characterization of the major catalase from Streptomyces coelicolor ATCC 10147. 788 56

The production of H2O2 by cells in cold paraformaldehyde-fixed frozen sections of inflammatory lesions was histochemically demonstrated by incubating them with diaminobenzidine (DAB) for 2 to 6 h. Catalase (150 micrograms/ml, about 1400 U/ml) inhibited the reaction, indicating that H2O2 was required to produce the chromogenic DAB product. Granulocytes (PMNs and eosinophils) were the main types of cells stained by the DAB reaction. Positive staining of macrophages was less frequent. The H2O2 was produced by metabolic enzymes that were still active after cell death and mild fixation. An atmosphere of 95 to 100% oxygen enhanced the specific DAB reaction, and an atmosphere of 100% nitrogen eliminated it. The DAB histochemical reaction to detect H2O2 requires the presence of peroxidases to produce the colored reaction product. Within our tissue sections, such peroxidases were evidently present in excess, because addition of low concentrations of H2O2 significantly increased the reaction product. Although some of the H2O2 produced by the granulocytes may have been derived from the dismutation of superoxide (O2-), the NADPH oxidase pathway for O2- formation did not seem to be involved: NADPH oxidase, a rather labile enzyme, should not be active after mild fixation, and diphenyleneiodonium (100 microM), an inhibitor of flavine-requiring NADPH oxidase, did not inhibit the reaction. Reactive nitrogen intermediates were also not involved, because NG-monomethyl-L-arginine and NG-nitro-L-arginine methyl ester, inhibitors of nitric oxide synthetase, did not appreciably inhibit the reaction. We conclude that stable, non-flavine-requiring oxidases, possibly cyclooxygenases or lipoxygenases, produced the H2O2 measured histochemically by our DAB reaction. These studies were made on tissue sections of acute dermal inflammatory lesions produced in rabbits by the topical application of 1% sulfur mustard [bis(2-chloroethyl) sulfide] in methylene chloride. Both intact PMNs and disintegrating PMNs in the base of the crust produced H2O2. Despite the production of H2O2 and the presence of peroxidase activity, no tissue damage was seen microscopically near the H2O2-producing cells, which indicates that the tissues are well protected by the antioxidants present in this self-limiting inflammatory reaction.
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PMID:Histochemical demonstration of hydrogen peroxide production by leukocytes in fixed-frozen tissue sections of inflammatory lesions. 793 Sep 39


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