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[Study of catalase and proteolytic activities of different variants of Bacillus mesentericus].

Catalase and proteolytic activity of the culures and morphological variants of Bacillus mesentericus fuscus, Bac. mesentericus vulgatus were studied. The variants were obtained as a result of prolonged cultivation of the stock strains in the potato mash under the layer of vaseline oil. The level of catalase activity varies in different morphological variants of the same culture, changes with age and depends on the storage conditions. The catalase activity in the rough, smooth and papillar variants that were freshly isolated from the potato mash was 1.5=2.5 times lower than that in the variants long kept on the agar medium. The quantitative indexes of the proteolytic activity of different variants also varied.

Bacillus↗

[Catalase activity in Paramecium aurelia].

The catalase activity of Paramecium aurelia was determined by the procedure of Sinha after bacteria elimination from culture medium. A significant level of catalase activity was shown, higher than in other cell kinds. The role of catalase activity in Paramecium sensitivity to low doses of ionizing radiations is discuted.

Animals↗

The role of cationized catalase and cationized glucose oxidase in mucosal oxidative damage induced in the rat jejunum.

The successful prevention of hydrogen peroxide-induced damage to the rat jejunal mucosa by cationized catalase is described in this study. Biological damage was induced in a closed circulating intestinal loop of the rat by hydrogen peroxide and by hydroxyl radicals induced in situ via the metal-mediated Haber-Wiess reaction. The mucosal activity of lactate dehydrogenase and the amount of potassium ions were used to quantitatively characterize the tissue damage. Catalase was cationized by reacting it with N,N'-dimethyl-1,3-propanediamine to give a soluble product or with polyhistidine to give an insoluble product. The activity of the modified enzymes was assessed, and their ability to protect the rat jejunal mucosa against oxidative stress was studied. It was found that in all cases the cationized enzymes were superior to the native catalase in their shield capability. A significant protection against Fe(II)/H2O2 and ascorbic acid/copper ion-mediated damage was obtained when the cationized enzymes were used. In the presence of glucose, native glucose oxidase failed to cause damage in the rat jejunal mucosa; however, the cationized enzyme caused profound tissue injury. These findings indicate the potential therapeutic merit of cationized enzymes for the treatment of pathological processes in the intestine, whenever oxidative stress is involved.

Animals↗

Serum catalase as the protective agent against inactivation of alpha 1-proteinase inhibitor by hydrogen peroxide; comparison between normal and rheumatoid sera.

Human serum contains catalase activity, which can protect alpha 1-proteinase inhibitor from inactivation by H2O2. The primary source of serum catalase is probably erythrocytic. The enzyme activity correlates with haemoglobin concentration in sera from control subjects but not in sera from patients with rheumatoid arthritis. Catalase is inactivated by oxidants, such as H2O2 and hypochlorous acid and it is suggested that the decrease in catalase/haemoglobin ratio observed in rheumatoid serum is due to oxidant stress associated with inflammation.

Arthritis, Rheumatoid↗

[Super-oxide dismutase and catalase in smokers].

In this work, the results of a study concerning the variation of superoxid dismutase (SOD) and catalase activities to smokers are presented. The study has been performed on volunteers, blood donors, men, between 20-60 years. In the smokers group, 20 donors who smoke over 10 cigarettes/day over 5 years have been included. In the control group, 12 donors who never smoked or stopped to smoke over 4 years have been included. SOD and catalase activities have been determined spectrophotometrically from erythrocytes lysis; the enzymatic activity has been reported to g Hb. The results show a decreasing of SOD activity to smokers reporting to the control group, totally with 17.7% (from 69.6 +/- 18.6 to 57.3 +/- 26.6 U/gHb). Comparing with control group, the catalase has been induced to smokers with 0.04%, from 8.82 +/- 3.32 to 9.18 +/- 8.66 x 10(3) U/gHb. Statistically, the variations are insignificant and we suspect the interferation of alcohol as an important oxidative stress inductor.

Adult↗

[Change in various properties of catalase in the small intestine of rats after vagotomy].

To evaluate the antioxidative system of the small intestine in disturbed parasympathetic innervation, the authors studied the activity of catalase, its resistance to substrate inactivation (catalytic capacity) and reduction potential (reduction of Fe3+ to Fe2+) in the enteric homogenate in different periods (on day 14 and 30) after bilateral subdiaphragmatic truncal vagotomy. Vagotomy did not change catalase activity but was attended by an increase of catalase catalytic capacity and reduction potential. It is suggested that the discovered changes of the studied parameters are manifestations of responses of the antioxidative protective system of the small intestine to the activation of lipid peroxidation.

Animals↗

Effects of hypothyroidism induced by 6-n-propylthiouracil and its reversal by T3 on rat heart superoxide dismutase, catalase and lipid peroxidation.

The present study critically evaluates the effects of hypothyroid and hyperthyroid states on lipid peroxidation and two enzymes of active oxygen metabolism, namely superoxide dismutase (SOD) and catalase (CAT) in the rat heart mitochondrial and post-mitochondrial fractions. Lipid peroxidation, an index of oxidative stress, was elevated in the heart tissue in hypothyroid state but reduced upon T3 supplementation. Hyperthyroidism registered increased SOD activity in post-mitochondrial fraction. Mitochondrial SOD activity was reduced in hypothyroid state, which was further reduced by T3 administration. In contrast, different thyroid states had no effect on catalase activity in the mitochondrial fraction. The hypothyroid state however, significantly augmented catalase activity in post-mitochondrial fraction. The results suggest that the antioxidant defence status of cardiac tissue is well modulated by thyroid hormone.

Animals↗

[Covalent immobilization of catalase on molded cellulose carriers].

We optimized the conditions of the covalent binding of bovine liver catalase to phosphate-cellulose matrices (gauze, granules, and paper with various surface density) and to acetate-cellulose porous membranes of different productivity. The capacity of the catalase binding to the molded cellulose carriers depends on the physico-chemical characteristics of the latter. The maximum concentration of the bound catalase after periodate oxidation of the carriers at room temperature was determined. The catalytic activity of the immobilized enzyme was quantified; under optimal conditions it is 24% for acetate-cellulose membranes and 24.3% for phosphate-cellulose paper and reduces with the increase of the total protein binding capacity of both the carriers.

Animals↗

The effect of melatonin on lipid peroxidation and nitrite/nitrate levels, and on superoxide dismutase and catalase activities in kainic acid-induced injury.

Kainic acid (KA) initiates neuronal injury and death by inducing oxidative stress and nitric oxide release from various regions of the brain. It was recently shown that melatonin has free radical-scavenging action and may protect against kainate-induced toxicity. In order to assess the possible supportive effect of melatonin treatment in KA-induced injury in the rat brain cortex, we determined malondialdehyde (MDA) levels as an index of lipid peroxidation, and assessed the activities of catalase (CAT) and superoxide dismutase (SOD) and the levels of nitrite/nitrate 35 male rats were divided into five groups, each receiving a different intraperitoneal treatment: saline solution (0.2 ml), kainic acid (15 mg/kg), melatonin (20 mg/kg), KA then melatonin (each as above, 15 min apart), or melatonin then KA (each as above, 30 min apart). Administration of KA caused an about five-fold increase in the catalase activity and an increase in the SOD activity in the cortex relative to the activities for the controls. Treatment with melatonin 15 min after KA injection kept malondialdehyde levels and catalase and superoxide dismutase activities at the normal levels, and led to an increase in the levels of nitrite/nitrate. Our data suggests that melatonin treatment following KA administration has a protective effect on antioxidant enzyme activities and thus supports the role of melatonin and oxidative stress in the regulation of antioxidative enzyme activity.

Animals↗

[Hydrogen peroxide content and catalase activity at inoculation with root tubercle bacteria of pea seedlings with the various nodulation ability].

Hydrogen peroxide (H2O2) content and catalase activity were studied in pea (Pisum sativum L.) seedlings with normal (cultivar Marat) and disrupted (pea mutants) process of nodulation, which were inoculated with the nitrogen-fixing bacterium Rhizobium leguminosarum strain CIAM 1026. Differences in hydrogen peroxide content and catalase activity in pea seedlings with different ability for nodulation, which were inoculated with rhizobia, were found. It was assumed that H2O2 and catalase are involved in defensive and regulatory mechanisms in the host plant.

Catalase↗

The effect of repeated administration of selected benzene bromoderivatives on the liver catalase activity in rats.

OBJECTIVES: Hexabromobenzene (HBB) is used as a flame retardant mainly added to plastics, timber and textiles. Tetrabromobenzene (TBB) is its metabolite. Both these compounds are present in the environment and in human and animal tissues. 1,4-Dibromobenzene (1,4-dBB) has found application in agriculture, pharmaceutical and some other industries as well as in households. It can also occur in the form of an environmental product of HBB debromination. It is known from laboratory experiments that animals after repeated exposure to these compounds, show the increase in relative liver weight. These results enable us to presume that benzene bromoderivatives may prove to be potential peroxisome proliferators. MATERIALS AND METHODS: The investigated compounds were administrated intragastrically in three different doses for 1, 3, 7, 14, 21 and 28 days. Catalase was determined according to the method of Johansson and Borg with use of Purpald. RESULTS: Repeated administration of the aforesaid compounds decreased catalase activity in the rat liver. CONCLUSIONS: The decreased level of catalase may point to its possible inactivation by metabolites of HBB, TBB and 1,4-dBB.

Animals↗

[Changes in erythrocyte superoxide dismutase and catalase activity in premature newborns with intraventricular haemorrhages].

Superoxide dismutase and catalase activities have been studied in peripherical blood erythrocytes of 49 premature newborns at 28-37 weeks gestation. Superoxide dismutase and catalase activities were lower in patients with bacterial infection of meninges. The standard therapy did not restore superoxide dismutase and catalase activities by the end of the neonatal period.

Catalase↗

[Effect of afobazole on the accumulation of free radical oxidation products and the catalase activity in rats with cerebral ischemia].

The influence of afobazole on the accumulation of free radical oxidation products (reactive oxygen species, ROS) and on the activity of antioxidative enzyme catalase was studied in striatum and cortex of rats under cerebral ischemia damage conditions. Afobazole showed a tendency to decrease the extent of ROS accumulation in the cortex. In striatum, the intensity of ROS accumulation in rats after ischemia wasa reliably lower as compared to that in control rats, but afobazole produced a partial recovery of this parameter. Afobazole induced an increase in the catalase activity in the cortex of rats with ischemia. In contrast, afobazole did not change the activity of this enzyme in striatum (where it was also decreased by ischemia). Thus, afobazole increased the resistance of neuron membrane structures to free radical oxidation in cortex and striatum and stimulated the catalase activity in the cortex in rats with global reversible cerebral ischernia.

Animals↗

[Study on interaction between sulfonylurea herbicides and catalase by fluorescence spectroscopy].

The binding of Sulfonylurea herbicides to catalase in aqueous solution was studied using fluorescence spectroscopy. It was shown that herbicides have a strong ability to quench the catalase fluorescence mainly through a static quenching procedure. The binding constant K and the number of binding site n were calculated according to the fluorescence quenching results. For chlorsufuron, K=8.69 x 10(5) L x mol(-1) and n = 1.16; for metsufuron methyl, K = 1.01 x 10(6) L x mol(-1) and n = 1.21; and for bensufuron methyl, K = 3.52 x 10(3) L x mol(-1), n = 0.77. It is clear that the binding of metsufuron methyl with catalase is stronger than that of chlorsufuron, while the binding of chlorsufuron stronger than that of bensufuron methyl.

Algorithms↗

Protective effect of liposome-entrapped superoxide dismutase and catalase on bleomycin-induced lung injury in rats. I. Antioxidant enzyme activities and lipid peroxidation.

The influence of liposome-entrapped catalase and/or superoxide dismutase on bleomycin-induced rat lung injury was studied. Liposome-entrapped catalase and/or superoxide dismutase increase antioxidant enzyme activities in the lung tissue of bleomycin-treated rats. The level of lipid peroxidation products (malondialdehyde, conjugated dienes, lipid hydroperoxides) was significantly lower in liposome-entrapped catalase and/or superoxide dismutase supplemented rats with bleomycin-injured lungs. It is suggested that liposomes are good vectors for drugs in the treatment of bleomycin-induced lung fibrosis.

Animals↗

Evidence that the M antigen of Histoplasma capsulatum var. capsulatum is a catalase which exhibits cross-reactivity with other dimorphic fungi.

A panel of monoclonal antibodies (Mabs) was raised against histoplasmin, the antigen derived from the mycelial phase of Histoplasma capsulatum var. capsulatum which contains the diagnostically useful H and M antigens. A number of Mabs were obtained which recognized a 70-75 kD component of an antigenic preparation of H. capsulatum var. capsulatum by Western blotting. When reacted with histoplasmin by Western blotting the Mabs recognized a similar 70-75 kD band, together with a series of higher molecular mass bands at approximately 130, 190 and 230 kD, a pattern which correlates strongly with both the published relative molecular mass (Mr) of the M antigen and the known subunit structure of the enzyme catalase. These Mabs were also shown to recognize a commercial preparation of Aspergillus niger catalase by ELISA. Other dimorphic fungi were also reactive with these Mabs by Western blotting, indicating the presence of common epitopes on the catalase molecules of these species.

Antibodies, Monoclonal↗

Glutathione-S-transferase, superoxide dismutase, xanthine oxidase, catalase, glutathione peroxidase and lipid peroxidation in the liver of exercised rats.

Glutathione-S-transferase (GST), superoxide dismutase (SOD), Xanthine oxidase, selenium-dependent glutathione peroxidase (GPxI), catalase activities and malondialdehyde (MDA) content were determined in liver of three groups of exercised rats (E) viz., one day (E1), 10 days (E10) and 60 days (E60). GST, SOD and xanthine oxidase activities increased significantly with the increase in exercise period. Lipid peroxidation, expressed in terms of MDA formation, also increased in the liver of all the three groups. But catalase activity decreased significantly during exercise. Further, GPxI did not show any significant change in its activity in response to exercise. Our findings indicate that: 1) The significant increase in GST activity suggests their induction aimed at counteracting the oxidant stress induced during exercise; 2) The significant increase in xanthine oxidase and SOD activities indicates the generation of more superoxide anion radicals and their removal, respectively. 3) The significant reduction in catalase activity denotes the decreased formation of hydrogenperoxides during exercise; and 4) The pattern of changes in the activity level of GPxI indicate its least participation during exercise. However, in another way it is giving a scope for the involvement of GPxII associated with GST in the reduction of organic hydroperoxides. Further more, the relative increase in MDA is considered as the indicator of the rate of lipid peroxidation in the wake of exhaustive exercise.

Animals↗

Catalase T deficient mutants of Saccharomyces cerevisiae.

A method for the isolation of catalase T deficient mutants of Saccharomyces cerevisiae is described. Ten mutants lacking catalase T and belonging to 5 complementation groups were isolated. CTT1 locus was identified as the structural gene for catalase T. It is under the control of CTT2, CTT3 and CTT4 loci.

Catalase↗