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

Catalase was purified to an apparent homogeneity from dog erythrocytes and its properties were compared with those of human erythrocyte catalase. Purification was unsuccessful without the use of glycerol as the stabilizing agent. Molecular weight of the purified dog catalase was estimated to be about 63,000 Da in monomer and about 230,000 Da in native tetramer form. The ratio of A405/A280, the index of hematin content relative to protein, was 1.15. The isoelectric point was in the range of 5.8 to 6.4. These properties of dog catalase were very similar to those of human catalase. Dog catalase also possessed the same partial amino acid sequence as human catalase. However, the specific activity of dog enzyme was about threefold less than that of human enzyme. The amount of catalase protein in dog erythrocytes determined by immunoblotting analysis was about tenfold less than that of human erythrocytes. This was consistent with the fact that the catalase activity in dog hemolysate was about 1/30 of that in human hemolysate.
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PMID:A low catalase activity in dog erythrocytes is due to a very low content of catalase protein despite having a normal specific activity. 972 87

Histoplasma capsulatum produces an extracellular catalase termed M antigen, which is similar to catalase B of Aspergillus and Emericella species. Evidence is presented here for two additional catalase isozymes in H. capsulatum. Catalase A is highly similar to a large-subunit catalase in Aspergillus and Emericella species, while catalase P is a small-subunit catalase protein with greatest similarity to known peroxisomal catalases of animals and Saccharomycotina yeasts. Complete cDNAs for the CATA and CATP genes (encoding catalases A and P, respectively) were isolated. The transcriptional expression of the H. capsulatum CATA, CATB (M antigen) and CATP genes was assessed by Northern blot hybridizations on total RNA. Results at the transcript levels for these genes are shown for three conditions: cell morphology (mycelial versus yeast phase cells), oxidative stress (in response to a challenge with H(2)O(2)) and carbon source (glucose vs glycerol). Collectively, these results demonstrated regulation of CATA by both cell morphology and oxidative stress, but not by carbon source, and regulation of CATB and CATP by carbon source but not cell morphology or oxidative stress. A phylogenetic analysis of presently available catalase sequences and intron residences was done. The results support a model for evolution of eukaryotic monofunctional catalase genes from prokaryotic genes.
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PMID:Redundancy, phylogeny and differential expression of Histoplasma capsulatum catalases. 1193 57

We examined the combined effects of gamma-radiation (24 degrees C) on spores of Clostridium botulinum-type Eklund strain suspended in different gas-saturated Na-phosphate buffer in absence or presence of protectors or sensitizers. Response surface methodology (RSM) was also used to ascertain the effects of radiation on the recovery of spores using a medium containing various levels of NaCl or Na-thioglycollate. The former (< 0.5%) decreased viable spore counts, but the latter (0.15%) did not. Irradiation inactivation of Eklund spores was most effective in air-saturated buffers compared to N2O and N2 gas. The Na2-EDTA (0.01 M) was the most efficient radioprotector of spores due to its reactivity toward hydroxy radicals, followed by t-butanol (0.1 M) in NO2 or N(2)-saturated buffers, respectively. Catalase (10.0 mg ml(-1)) and DL-cysteine (0.1 mM) sensitized the spores during irradiated N2O or N(2)-saturated buffers, and NaCl (0.01 M) only sensitized spores in N2 environment. Spores frozen at -75 degrees C for 30 days and thawed prior to use were more sensitive to radiation damage compared to freshly prepared spores. Glycerol (15%), in Na-phosphate buffer (pH 7.0, 0.06 M), protected Eklund spores and increased the number of spores from 10(6) to 10(11) colony forming unit (CFU) ml(-1), and enhanced their radiosensitivities. Seven strains of C. botulinum type E were screened for plasmids and strain BL764 had two plasmids (15.8 and 46.8 mDa), BL4028 also had two (4.4 and 13.2 mDa), BL4850 contained only one (4.9 mDa), whereas EQA, BL211, Eklund, and Beluga had none. Gamma-Radiation (10 kGy, absorbed dose) cured the 15.8-mDa plasmid in strain BL764, but its absence yielded no changes in toxigenicity.
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PMID:Combined effects of ionizing-irradiation and different environments on Clostridium botulinum type E spores. 1462 91

Diaphorase was studied as a possible oxidoreductase participating in NO production from some vasorelaxants. In the presence of NADH or NADPH, diaphorase can convert selected NO donors, glycerol trinitrate (GTN) and formaldoxime (FAL) to nitrites and nitrates with NO as an intermediate. This activity of diaphorase was inhibited by diphenyleneiodonium (DPI) (inhibitor of some NADPH-dependent flavoprotein oxidoreductases), while it remained uninhibited by NG-nitro-L-arginine methyl ester (inhibitor of NO synthase) 7-Ethoxyresorufin (inhibitor of cytochrome P-450 1A1 and cytochrome P-450 NADPH-dependent reductase) inhibited the conversion of GTN only. Existence of NO as an intermediate of the reaction was supported by results of electron paramagnetic resonance spectroscopy. In addition to its ability to affect the above mentioned NO donors, diaphorase was able to reduce 2-phenyl-4,4,5,5,-tetramethylimidazoline-1-oxyl-3-oxide (PTIO) and thus to eliminate its NO scavenging effect. This activity of diaphorase could also be inhibited by DPI. The reaction of diaphorase with GTN and PTIO was not affected by superoxide dismutase (SOD) or catalase. Reaction of FAL with diaphorase was lowered with SOD by 38 % indicating the partial participation of superoxide anion probably generated by the reaction of diaphorase with NADH or NADPH. Catalase had no effect. Diaphorase could apparently be one of the enzymes participating in the metabolism of studied NO donors to NO. The easy reduction and consequent elimination of PTIO by diaphorase could affect its use as an NO scavenger in biological tissues.
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PMID:Diaphorase can metabolize some vasorelaxants to NO and eliminate NO scavenging effect of 2-phenyl-4,4,5,5,-tetramethylimidazoline-1-oxyl-3-oxide (PTIO). 1558 29

Effect of six organic solvents-methanol, ethanol, propanol, dimethyl sulphoxide (DMSO), N,N-dimethyl formamide (DMF), and glycerol on the conformation and interaction of catalase and anticatalase antibodies were studied with the aim of identifying the solvents in which antigen-antibody interactions are strong. The antigen binding activity of the antibodies in the various organic solvents increased in the following order: ethanol<methanol<no organic solvent<propanol<DMSO<DMF<glycerol. The structure of both the antibody and the antigen molecule was affected significantly in 40% concentration of the organic solvents used in this study. Catalase activity was inhibited in DMSO. However, the enzyme was activated in DMF upto about 50% of its concentration.
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PMID:Effect of organic solvents on the conformation and interaction of catalase and anticatalase antibodies. 1667 2

1. Hyperbaric (HBO(2)) and topical oxygen represent two accepted options to oxygenate tissues. The aim of the present study was to investigate the effect of HBO(2) on energy metabolism and anti-oxidant enzymes in a rat model of ischaemia-reperfusion (IR) skeletal muscle injury. 2. In the first study, 16 rats were randomized to a HBO(2)-treated group (Group 1; n = 8) and an untreated group (Group 2; n = 8). Under general anaesthesia, right hind limb ischaemia was produced by application of a rubber-band tourniquet for 3 h. After 2 h ischaemia, Group 1 rats received HBO(2) during the last hour of ischaemia. The HBO(2) consisted of 100% oxygen delivered at 282.8 kPa absolute pressure. Group 2 rats were not treated. Following the ischaemic period, the tourniquet was released for 1 h. A microdialysis probe was used to sample lactate, glucose and glycerol concentrations in the muscle extracellular tissue every 15 min throughout each experiment. 3. In the second study, 24 rats were randomized into four groups (n = 6 each). The first two groups were subjected to the IR injury protocol outlined above and either treated (Group 1) or untreated (Group 2) with HBO(2). Group 3 rats were anaesthetized, did not undergo IR injury, but underwent HBO(2) treatment. Group 4 rats were anaesthetized but did not undergo either IR injury or HBO(2) treatment. At end of each experiment, the biceps femoris muscle was removed and assayed for superoxide dismutase (SOD) and catalase (CAT) activity. Malondialdehyde (MDA) was measured to estimate the extent of membrane lipid peroxidation. 4. Three hours of skeletal muscle ischaemia resulted in a gradual decrease in the glucose concentration and a gradual increase in the lactate concentration within the extracellular fluid of the affected skeletal muscle tissue. Treatment with HBO(2) had no effect on the glucose concentration; however, HBO(2) significantly attenuated the ischaemia-induced increase in lactate and glycerol. In both groups, glucose concentration increased rapidly during reperfusion; glucose concentration returned to pre-ischaemic levels 15 min after reperfusion both with and without HBO(2). 5. Catalase activity and MDA increased significantly after 1 h of reperfusion. The HBO(2) attenuated the reperfusion-induced increase in CAT activity and MDA. 6. The results of the study suggest that HBO(2) may have some beneficial effect by decreasing lactate and glycerol levels and modulating anti-oxidant enzyme activity in postischaemic skeletal muscle in our rat model of tourniquet-induced IR skeletal muscle injury.
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PMID:Effects of hyperbaric oxygen on glucose, lactate, glycerol and anti-oxidant enzymes in the skeletal muscle of rats during ischaemia and reperfusion. 1720 38

A strictly anaerobic, mesophilic, sulfate-reducing bacterial strain (MSL86(T)) isolated from an estuarine sediment in the Sea of Japan (around the Japanese islands) was characterized phenotypically and phylogenetically. The cells were found to be Gram-negative, motile, non-spore-forming rods. Catalase was not detected. The optimum NaCl concentration for growth was 1.0 % (w/v) and the optimum temperature was 35 degrees C. Strain MSL86(T) was slightly alkaliphilic, with optimum growth at pH 7.5-7.6. Organic electron donors were incompletely oxidized to (mainly) acetate. Strain MSL86(T) utilized formate, pyruvate, lactate, fumarate, ethanol, propanol, butanol and glycerol as electron donors for sulfate reduction and did not use acetate, propionate, butyrate, succinate, malate, methanol, glycine, alanine, serine, aspartate, glutamate or H(2). Sulfite, thiosulfate and fumarate were used as electron acceptors with lactate as an electron donor. Without electron acceptors, the strain fermented pyruvate and fumarate. The genomic DNA G+C content was 54.4 mol%. Menaquinone MK-8(H(4)) was the major respiratory quinone. The major cellular fatty acids were C(16 : 0), C(16 : 1)omega7, C(16 : 1)omega5 and C(17 : 1)omega6. A phylogenetic analysis based on the 16S rRNA gene sequence placed the strain in the class Deltaproteobacteria. The recognized bacterium most closely related to strain MSL86(T) was [Desulfobacterium] catecholicum DSM 3882(T) (sequence similarity 94.4 %), and the next most closely related recognized species were Desulfotalea psychrophila (94.2 % sequence similarity with the type strain) and Desulfotalea arctica (93.7 %). As the physiological and chemotaxonomic characteristics of MSL86(T) were distinctly different from those of any related species, a novel genus and species Desulfopila aestuarii gen. nov., sp. nov. are proposed to accommodate the strain. The type strain of Desulfopila aestuarii is MSL86(T) (=JCM 14042(T)=DSM 18488(T)).
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PMID:Desulfopila aestuarii gen. nov., sp. nov., a Gram-negative, rod-like, sulfate-reducing bacterium isolated from an estuarine sediment in Japan. 1732 77

Two strictly anaerobic, mesophilic, sulfate-reducing bacterial strains, Pro1(T) and Pro16, were isolated from an estuarine sediment in the Sea of Japan of the Japanese islands and were characterized by phenotypic and phylogenetic methods. Strains Pro1(T) and Pro16 had almost the same physiological and chemotaxonomic characteristics. Cells of both strains were Gram-negative, motile, non-spore-forming rods. Catalase activity was not detected. The optimum NaCl concentration for growth was 3.0 % (w/v). The optimum temperature for growth was 35 degrees C and the optimum pH was 6.7. Both strains used formate, propionate, pyruvate, lactate, fumarate, malate, ethanol, propanol, butanol, glycerol, alanine, glucose, fructose and H(2) as electron donors for sulfate reduction and did not use acetate, butyrate, succinate, methanol, glycine, serine, aspartate, glutamate, cellobiose or sucrose. Organic electron donors were incompletely oxidized mainly to acetate. Both strains also used thiosulfate as an electron acceptor. Without electron acceptors, both strains fermented pyruvate and lactate. The genomic DNA G+C contents of strains Pro1(T) and Pro16 were 48.6 and 46.0 mol%, respectively. The major respiratory quinone of both strains was menaquinone MK-5(H(2)). Major cellular fatty acids of both strains were C(15 : 0), C(16 : 0), C(17 : 1)omega6 and C(18 : 1)omega7. Phylogenetic analysis based on 16S rRNA gene sequences placed both strains in the class Deltaproteobacteria. The closest recognized relative of strains Pro1(T) and Pro16 was Desulfobulbus mediterraneus with sequence similarities of 95.2 and 94.8 %, respectively. Based on phylogenetic, physiological and chemotaxonomic characteristics, strains Pro1(T) and Pro16 represent a novel species of the genus Desulfobulbus, for which the name Desulfobulbus japonicus is proposed. The type strain is Pro1(T)(=JCM 14043(T)=DSM 18378(T)) and strain Pro16 (=JCM 14044=DSM 18379) is a reference strain.
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PMID:Desulfobulbus japonicus sp. nov., a novel Gram-negative propionate-oxidizing, sulfate-reducing bacterium isolated from an estuarine sediment in Japan. 1739 18

A strictly anaerobic, mesophilic, sulfate-reducing bacterial strain, designated MSL71T, was isolated from an estuarine sediment from the Sea of Japan bordering the Japanese islands and was characterized phenotypically and phylogenetically. The cells were found to be Gram-negative, motile, non-spore-forming, slightly curved rods. Catalase and oxidase activities were not detected. The optimum NaCl concentration for growth was 2.0 % (w/v), the optimum temperature was 30 degrees C and the optimum pH was 6.3. Strain MSL71T utilized formate, butyrate, pyruvate, lactate, malate, ethanol, propanol, butanol, glycerol and H2 as electron donors for sulfate reduction. The organic electron donors used were incompletely oxidized, mainly to acetate. The strain did not use acetate, propionate, fumarate, succinate, methanol, glycine, alanine, serine, aspartate or glutamate. Sulfite and thiosulfate were used as electron acceptors with lactate as an electron donor, but fumarate was not utilized. Without electron acceptors, pyruvate and malate, but not lactate or fumarate, were fermented. The genomic DNA G+C content was 62.0 mol%. Menaquinone MK-8(H4) was the major respiratory quinone. The major cellular fatty acids were C14 : 0, C16 : 0, C16 : 1 omega 7, C18 : 1 omega 9, C18 : 1 omega 7 and C14 : 0 3-OH. A phylogenetic analysis based on the 16S rRNA gene sequence placed the strain in the class Deltaproteobacteria. The closest recognized relative of strain MSL71T was Desulfofrigus fragile (93.9 % sequence similarity) and the next closest recognized species was Desulfofrigus oceanense (93.5 %). On the basis of the significant differences in the 16S rRNA gene sequence and phenotypic characteristics between strain MSL71T and each of the related species, a novel genus and species, Desulfoluna butyratoxydans gen. nov., sp. nov., are proposed to accommodate strain MSL71T. The type strain is MSL71T (=JCM 14721T=DSM 19427T).
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PMID:Desulfoluna butyratoxydans gen. nov., sp. nov., a novel Gram-negative, butyrate-oxidizing, sulfate-reducing bacterium isolated from an estuarine sediment in Japan. 1839 77

In this study we evaluated the effect of diphenyl diselenide (PhSe)(2) on glycerol-induced acute renal failure in rats. Rats were pre-treated by gavage every day with (PhSe)(2 )(7.14 mg kg(-1)) for 7 days. On the eighth day, rats received an intramuscular injection of glycerol (8 mL kg(-1)). Twenty-four hours afterwards, rats were euthanized and the levels of urea and creatinine were measured in plasma. Catalase (CAT), glutathione peroxidase (GPx), glutathione S-transferase (GST), delta-aminolevulinate dehydratase (delta-ALA-D) and Na(+), K(+)-ATPase activities and ascorbic acid levels were evaluated in renal homogenates. Histopathological evaluations were also performed. The results demonstrated that (PhSe)(2) was able to protect against the increase in urea and creatinine levels and histological alterations in kidney induced by glycerol. (PhSe)(2) protected against the inhibition in delta-ALA-D, CAT and GPx activities and the reduction in ascorbic acid levels induced by glycerol in kidneys of rats. In conclusion, the present results indicate that (PhSe)(2) was effective in protecting against acute renal failure induced by glycerol.
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PMID:Diphenyl diselenide protects against glycerol-induced renal damage in rats. 1948 1


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