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PubMedDate not supplied

[Search for micromycetes--producers extracellular catalase and study of conditions of its synthesis].

Production of extracellular catalase by microscopic mycelial fungi (255 strains) belonging to different taxonomic groups was studied. Producers of extracellular catalase were found among fungi of the genera Penicillium, Talaromyces and Aspergillus. Strains of the genus Penicillium were the most active producers. The formation of catalase depended on the initial pH, carbon and nitrogen sources and their ratio, and the content of microelements in the medium. The yield of extracellular catalase produced by the strains selected (P. chrysogenum, P. funiculosum, P. pinophilum, and P. minioluteum) was not less than 400-1400 U per ml culture liquid.

Carbon↗
PubMedDate not supplied

[Antifibrosis effect of modified forms of catalase and superoxide dismutase in experimental silicosis].

The forms of catalase modified by treatment with dextran aldehyde were obtained and studied. Efficacy of the preparations containing native and modified forms of catalase and superoxide dismutase as well as their covalent bienzyme conjugate containing catalase-dextran aldehyde-superoxide dismutase was studied in rats with simulated silicosis. The preparations were administered into rats by means of inhalation and intraperitoneal injection. Positive protective effect exhibited a mixture of native enzymes and their covalent conjugate. The most pronounced additional effect was caused by the mixture of native catalase and superoxide dismutase as compared with modified preparation of superoxide dismutase. The preparation of bienzyme containing conjugate was less effective.

Animals↗
PubMed2003

[Effect of N-acetyl-L-cysteine and catalase on apoptosis of lens epithelial cell and the activity of caspase-3].

OBJECTIVE: To investigate the effect of antioxidants N-acetyl-L-cysteine and catalase on H(2)O(2)-induced apoptosis of lens epithelial cells and the activity of caspase-3. METHODS: Rat lenses were incubated in MEM with 2 mmol/L H(2)O(2) (H(2)O(2) groups) or without H(2)O(2) (control groups), antioxidants 100 micromol/L N-acetyl-L-cysteine and 900 U/ml catalase were used to block the oxidative injury of lens epithelial cells respectively. Lens opacification and apoptosis of lens epithelial cells were detected using transmission electron microscope and AnnexinV-PI staining after 24 hours incubation. The activity of caspase-3 was analyzed by Western blot at the same time. RESULTS: The observations revealed that 2 mmol/L H(2)O(2) could apparently induce lens opacification and lens epithelial cell apoptosis in vitro, the apoptosis rate increased to (31.20 +/- 3.31)% after 24 hours incubation, which is also the time caspase-3 was activated. Treatment with N-acetyl-L-cysteine and catalase could inhibit lens opacification, apoptosis and caspase-3 activation induced by H(2)O(2). The apoptosis rate decreased to (20.90 +/- 3.16)% and (15.02 +/- 2.41)% respectively (P < 0.01). CONCLUSION: These data indicate that antioxidants N-acetyl-L-cysteine and catalase, possibly through regulation of the activity of caspase-3, can prevent lens opacification and apoptosis of lens epithelial cells.

Acetylcysteine↗
PubMed2004

[Effects of catalase on the mitochondria and apoptosis of SW480 cells].

OBJECTIVE: To investigate the effects of catalase on the mitochondria and apoptotic behavior of SW480 cells treated by lipopolysaccharide (LPS), and the changes in intracellular expression of nuclear factor kappaB (NF-kappaB). METHODS: LPS-stimulated SW480 cells were treated with catalase and the changes in their mitochondria and apoptotic behavior were observed by transmission electron microscopy. The expression of NF-kappaB was detected by immunohistochemical method. RESULTS: Mitochondria damages and apoptosis were slightly diminished in the LPS-stimulated cells with catalase pretreatment, and the NF-kappaB expression was also decreased. CONCLUSION: Catalase protect the mitochondria of SW480 cells from damages by LPS and inhibit the cell apoptosis, possibly due to the activation of NF-kappaB.

Apoptosis↗
PubMed1992

Effects of hemorrhagic shock and retransfusion on catalase and superoxide dismutase activities in rabbits.

The effects of hemorrhagic shock and retransfusion on the activities of two endogenous antioxidant enzymes, catalase and superoxide dismutase, were studied in male New Zealand white rabbits. Following instrumentation and stabilization, blood was withdrawn to reduce mean arterial pressure to 35 mmHg (SHOCK). After 60 min of shock, the warmed autologous blood was infused and the animals were allowed to recover for an additional 30 min (RETRANS). CONTROL animals were instrumented but not bled or transfused. A 60 min period of hemorrhagic shock had no significant effect on tissue or plasma activities of catalase or superoxide dismutase. However, transfusion following hemorrhagic shock resulted in an increase in catalase activity of nearly two-fold in the liver and five-fold in the small intestine. In contrast, superoxide dismutase activity remained unchanged after retransfusion in other tissues and in plasma. These results indicate that superoxide dismutase and catalase activities may be preserved or even induced following transfusion for hemorrhagic shock.

Animals↗
PubMedDate not supplied

[Catalase activity as affected by carnosine and sodium nitrite in vitro].

It was shown in vitro that the activity of catalase Penicillium vitale decreases when treated by sodium nitrite to the greater extent than when affected by dipeptide carnosine (beta-alanyl-L-histidine). At alternating introduction of carnosine and NaNO2 that component affected the catalase activity which was the first to be introduced. The entering of the next metabolite into the medium did not change the enzyme activity. It is shown that carnosine binds with a molecule of catalase. Carnosine may be considered one of natural regulators of catalase activity.

Carnosine↗
PubMed2005

Differential expression of three catalase genes in hot pepper (Capsicum annuum L.).

Three different catalase cDNA clones (CaCat1, CaCat2, and CaCat3) were isolated from hot pepper (Capsicum annuum L.), and their expression patterns were analyzed at the levels of mRNA and enzyme activity. Northern hybridization showed that the three catalase genes were differentially expressed in various organs, and that expression of CaCat1 and CaCat2 was regulated differently by the circadian rhythm. In situ hybridization revealed different spatial distributions of CaCat1 and CaCat2 transcripts in leaf and stem. In response to wounding and paraquat treatment, CaCat1 mRNA increased at 4-12 h in both paraquat-treated and systemic leaves. In contrast, wounding had no significant effect on expression of the catalase genes. The increase of catalase activity in the paraquat-treated and systemic leaves paralleled that of CaCat1 mRNA, but did not match that of CaCat1 mRNA in paraquat-treated stems. Our results suggest that CaCat1 may play a role in responses to environmental stresses.

Amino Acid Sequence↗
PubMed1990

[Catalytic properties and stability of catalase in reversed micelles of aerosol OT in octane].

The catalytic function of catalase and its peroxidatic activity during tetramethylbenzidine (TMB) oxidation by cumene hydroperoxide were studied in reversed micelles of Aerosol OT (AOT) in octane relative to the [H2O]/[AOT] ratio and the initial catalase concentration. The optimum conditions permitting to retain the catalytic activity of the enzyme and its ability to induce peroxidation of TMB, were found. The catalytic function of the enzyme was shown to be dependent on its concentration in AOT micelles. The catalase stability monitored by the catalytic reaction and the decrease of the Soret band were analyzed. Both processes have two phases differing by the rate constants of the pseudo-first order. The catalase inserted into AOT micelles is characterized by the high stability as compared to other hemoproteins (cytochrome P-450, myoglobin, hemoglobin, peroxidase) under identical conditions.

Animals↗
PubMedDate not supplied

[Role of catalase and superoxide dismutase in the yeast Saccharomyces cerevisiae response to hydrogen peroxide in exponential phase of growth].

The role of catalase and superoxide dismutase (SOD) in response of the yeast Saccharomyces cerevisiae to oxidative stress induced by hydrogen peroxide in the middle-exponential phase has been investigated. It was shown that cell survival is significantly decreased after yeast exposure to hydrogen peroxide in the strains defective in cytosolic or peroxisomal catalases. Treatment of the wild-type cells with 0.5 mM H2O2 for 30 min causes an increase in the activity of catalase and superoxide dismutase, but the effect was not observed in all strains investigated. It was also shown that hydrogen peroxide leads to an increase in the activities of both catalases and Cu,Zn-containing SOD. The effect was cancelled by cycloheximide, an inhibitor of protein synthesis.

Catalase↗
PubMed1991

Macrophages produce nitrite, nitrate and nitrosamines after addition of catalase.

Mouse macrophages produced nitrite and N-nitrosomorpholine after incubation with catalase. A macrophage cell line, J774.1 (1 x 10(6) cells/ml), was incubated with catalase (500 U/ml) and morpholine (5 mM); after 48 h incubation at 37 degrees C, macrophages produced nitrite (100 microM) and N-nitrosomorpholine (1 microM). Stimulation of J774.1 cells with catalase enhanced interleukin-1 production and tumour-killing activity against mastocytoma P815 cells. Flow cytometric analysis showed that catalase was bound to the surface of the macrophages.

Animals↗
PubMed1991

Tumor necrosis factor/cachectin decreases catalase activity of rat liver.

Tumor bearing hosts and animals treated with endotoxin commonly show a decrease in the catalase activity of the liver and kidney. Since tumor necrosis factor (TNF)/cachectin may play a significant role in these conditions, we investigated its effects on the catalatic and peroxidatic activity of catalase in the liver and kidney of the rat. The activities of glucose-6-phosphate dehydrogenase and lactate dehydrogenase were measured simultaneously to monitor the pentose phosphate and glycolytic pathways, respectively. Injection i.p. of 100 micrograms/kg/day human recombinant TNF-alpha for 5 days resulted in a significant (P less than 0.01) decrease in the catalatic activity of the liver when compared to rats fed ad libitum. The decrease in four experiments ranged from 21 to 56%. A significant decrease (18%; P = 0.01) in liver catalatic and peroxidatic activity was also observed in another experiment using pair fed rats as controls. The peroxidatic activity of catalase with ethanol as hydrogen donor closely paralleled the catalatic activity. TNF treatment had no detectable effect on the catalatic or peroxidatic activity of catalase in the kidney. The activity of glucose-6-phosphate dehydrogenase increased (31-80%) significantly (P less than or equal to 0.02) in the liver and, to a lesser extent, in the kidney (5-27%, P = 0.05). Lactate dehydrogenase activity decreased (14-19%) significantly (P less than or equal to 0.05) in the liver and kidney but mainly in rats treated with TNF and additionally fasted for 24 h. Electron microscopic examination of liver sections showed that the hepatocytes of TNF-treated rats were undamaged but contained fewer and smaller peroxisomes than those of the control rats.

Animals↗
PubMed1978

Cytochemical distinction between azurophils and catalase-containing granules in leukocytes. I. Studies in developing neutrophils and monocytes from patients with myeloperoxidase deficiency: comparison with peroxidase-deficient chicken heterophils.

The neutrophils and monocytes of two patients with hereditary myeloperoxidase (MPO) deficiency lacked MPO activity as determined by light and electron microscopic cytochemical staining. With a technique employing neutral 3,3'-diaminobenzidine, azurophils of precursor and mature neutrophils were devoid of MPO whereas eosinophil, basophil, and platelet peroxidases exhibited normal activity. After incubation in alkaline DAB medium, which stains catalase, some small granules were strongly reactive in both immature and mature neutrophils and monocytes. These catalase-containing granules were distinct from all other categories of granules. Their number decreased with maturation. In the presence of cyanide or aminotriazole, peroxidatic activity could also be detected in ellipsoid azurophils, although large spherical granules remained unreactive. This peroxidatic activity is apparently not due to MPO inasmuch as it has been demonstrated that this protein is not synthesized in these patients. Thus, the significance of the last finding is unclear but suggests a heterogeneity of azurophil content. In contrast to human MPO-deficient cells, chicken heterophils naturally devoid of peroxidase are unable to produce hydrogen peroxide upon phagocytosis and were also devoid of catalase-containing particles. This observation suggests that catalase is involved in the control of the intracellular level of hydrogen peroxide in human cells.

Animals↗
PubMed1990

Enzymatic properties of immobilized catalase on protein coated supports.

Sephadex-100, DEAE-Sephadex and polyvinyl alcohol supports used for immobilization of catalase were prepared by modifications initially with 2-amino-4,6-dichloro-s-triazine and then with diaminohexane and glutaraldehyde prior to coating with gelatine, whereas the Fe2O3 support was coated directly. Optimum support/enzyme ratios were determined for these protein coated supports in a series of immobilization reactions with varying amounts of catalase in the presence of the crosslinking agent glutaraldehyde. Activity variations with respect to pH, temperature, stability behaviour and the inhibition effect of hydroxylamine were investigated for the immobilized catalase preparations. The time-dependent decomposition rate of H2O2 and the deactivation rate constants for catalase were investigated in a discontinuous batch-type reactor system.

Catalase↗
PubMed1977

Effects of dietary vitamin B-2 and vitamin E on the delta9-desaturase and catalase activities in the rat liver microsomes.

The effects of dietary vitamin B-2 and vitamin E on delta9-desaturation of stearoyl-CoA, catalase, glutathione peroxidase, superoxide dismutase and electron transport components in rat liver microsomes have been investigated. delta9-desaturase activities were decreased on diets deficient of vitamin B-2, E and supplemented with E. Among the peroxide-scavenging enzymes, only the catalase activity in microsomes correlates significantly with delta9-desaturase activity. In vitro addition of bovine catalase had no effect on microsomal delta9-desaturase activity on control diet. However, it enhanced the delta9-desaturation in microsomes on vitamin B-2-deficient diet which contained low catalase and high superoxide dismutase activities, compared to those in microsomes of control diet. It is suggested that the hydrogen peroxide-generating and -decomposing systems may play an important role on the delta9-desaturase activity in microsomes.

Animals↗
PubMed1990

Redox interactions between catalase and alcohol dehydrogenase pathways of ethanol metabolism in the perfused rat liver.

Alcohol metabolism via alcohol dehydrogenase (ADH) and catalase was studied in perfused rat livers by measuring the oxidation of methanol and butanol, selective substrates for catalase and ADH, respectively. In livers from fasted rats, basal rates of methanol uptake of 15 +/- 1 mumol/g/h were decreased significantly to 8 +/- 2 mumol/g/h by addition of butanol. Concomitantly, pyridine nucleotide fluorescence detected from the liver surface was increased by butanol but not methanol. Both effects of butanol were blocked by an inhibitor of ADH, 4-methylpyrazole, consistent with the hypothesis that elevation of the NADH redox state by butanol inhibited H2O2 production via NAD+-requiring peroxisomal beta-oxidation, leading indirectly to diminished rates of catalase-dependent methanol uptake. In support of this idea, both butanol and butyraldehyde inhibited H2O2 generation. The NADH redox state was also elevated by xylitol, causing a 75% decrease in rates of methanol uptake by livers from fasted rats. This effect was not observed in livers from fed rats unless malate-aspartate shuttle activity was reduced by infusion of the transaminase inhibitor aminooxyacetate. Taken together, these data indicate that generation of reducing equivalents from ADH in the cytosol inhibits H2O2 generation leading to significantly diminished rates of peroxidation of alcohols via catalase. This phenomenon may represent an important physiological mechanism of regulation of ethanol oxidation in intact cells.

Alcohol Dehydrogenase↗
PubMed1990

Coupled-enzyme determination of catalase activity in erythrocytes.

This coupled-enzyme method for determining the activity of catalase (EC 1.11.1.6) in erythrocyte lysates is based on measuring the absorbance at 340 nm of NADH produced from the peroxidic reaction between ethanol, hydrogen peroxide, and catalase. Hydrogen peroxide is produced as a substrate in situ from the oxidation of glucose catalyzed by glucose oxidase (EC 1.1.3.4). Catalase oxidizes ethanol to acetaldehyde in the presence of hydrogen peroxide. Acetaldehyde is then oxidized by aldehyde dehydrogenase (EC 1.2.1.5) to produce acetate with concomitant conversion of NAD+ to NADH. The reaction did not follow strict zero-order kinetics; enzyme activity was quantified by using initial rates and standards prepared from purified catalase. The method demonstrated within-run and between-run CVs of 1.0% to 2.9% and 2.4% to 3.3%, respectively. This semiautomated method correlated well (r = 0.92) with the more tedious manual method involving measurement at 240 nm.

Catalase↗
PubMed1989

[A method of determining the catalase activity of bacteria].

An iodine-starch method has been developed for the detection of catalase in bacteria and for measuring this enzyme's activity. The method is based on potassium iodide reduction with hydrogen peroxide to form free iodine. The bacteria are layered on starch gel, treated with hydrogen peroxide, and then with potassium iodide. The starch gel stains blue, and light areas emerge round catalase-positive bacteria; the size of these light sites helps assess the enzyme's activity. The method permits estimating the populational heterogeneity of the cultures judging from catalase activities and helps detect the mutants by catalase; it is convenient, simple, and provides reliable information on the taxonomic status of the bacteria.

Bacteria↗
PubMed1989

Effect of age, sex, and smoking on serum catalase activity.

In selected hospitalized patients (9294) with normal serum catalase activity, 7.58 per cent higher (p less than 0.001) serum catalase activity was detected in males than in females. With age, serum catalase activity decreased (slope-0.0683) in males, increased (slope 0.101) in females and did not change in all patients (slope 0.049). Cigarette smoking did not influence serum catalase activity (p greater than 0.05).

Adolescent↗