• Journal of Plant Biology
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• v.17 no.1
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• pp.3-8
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• 1974

The experiments were conducted to examine the effects of sulfur dioxide on catalase activity in germinating seeds under dark conditions and in green plants under light conditions. Three kinds of plants, bean (Glycine max M.), cabbage (Brassica oleracea L. Chungbang No.1) and rice (Oryza sativa L. Suwon No.213-1) were used in this study. Both thegerminating seeds and the leaves were treated with various concentrations of sulfur dioxide for both one green plants with two and twelve hours. In the results of the measurement of catalase activity it was found that plant injuries by sulfur dioxide for the period of photosynthesis were higher than those for the period of respiration. In the control, apparent catalase activity under the light condition of photosynthesis showed a considerable decrease in comparison with catalase activity under the dark condition of respiration. This tendency also appeared markedly in the gas treatment. In the gas treatment for twelve hours, the decrease of catalase activity was higher than that of one hour in both photosynthesis and respiraton. It was thought that sulfur dioxide was an inhibitor of catalase activity in higher concentration of the gas.

• Preventive Nutrition and Food Science
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• v.7 no.1
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• pp.28-32
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• 2002

A Micrococcus sp. producing catalase was isolated from soil, and a commercial-scathe cultivation and purification of catalase were conducted. The maximum catalase activity was about 103 BU/mL obtained after 46 hr of cultivation in a 30 L fermenter containing 2% glucose, 2% peptone, 4% yeast extract, and 0.5% NaCl. Soybean sauce, CSL (corn steep liquor), and yeast extract were also studied as media substitutes in the media 30 L fermenter. The optimum medium components for the production catalase were found to be 2% glucose, 4% soybean sauce, and 16% CSL. In a 18 kL fermenter, the stationary phase in the cell growth and maximum catalase activity (112 BU/mL) were reached after 46 hr of cultivation, which was the same result as in the 30 L fermenter. The catalase activity was purified with over 17 folds in four steps with a 33.6% yield. From 104,250 mg of protein after cell lysis, 1,966 mg of the purified enzyme with a specific activity of 192.7 kBU/mg was obtained. The residual activity with the addition of 10% NaCl exhibited more than 100%. The use of just NaCl produced a higher residual activity than combination of bencol (benzyldimethyl ammoniumchloride) and PG (propyleneglycol).

• Journal of radiological science and technology
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• v.15 no.1
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• pp.123-130
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• 1992

This study was prepared to observe the change of enzyme activities in kidney treated with red ginseng extract in the gamma ray irradiated mice. Determine the activity of SOD, peroxidase, catalase in the kidney a period of 1 day, 2 day, 3 day, 4 day, 5 day after a saline injection or injection of red ginseng extract or gamma ray irradiatied group into four classify. The activity SOD and catalase showed a tendency to increase and recovery at the early state but pay no regard. Wherease, the activity of peroxide restored and increased pay regard. A physiological saline injection group after gamma ray irradiation showed a tendency to diminish after remakable increase of activity of SOD, peroxidase and catalase than control group. Injection group of red ginseng extract after gamma ray irradiation observed rapid recovery on activity of SOD, peroxidase, catalase than a saline injection group. Experimental result suggested that injection of red ginseng extract after irradiation have the recovery effect on the changed of activity of SOD, peroxidase and catalase against radiation injury.

• Journal of Microbiology
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• v.44 no.2
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• pp.185-191
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• 2006

The photosynthetic bacterium, Rhodospirillum rubrum S1, when grown under anaerobic conditions, generated three different types of catalases. In this study, we purified and characterized the highest molecular weight catalase from the three catalases. The total specific catalase activity of the crude cell extracts was 88 U/mg. After the completion of the final purification step, the specific activity of the purified catalase was 1,256 U/mg. The purified catalase evidenced an estimated molecular mass of 318 kDa, consisting of four identical subunits, each of 79 kDa. The purified enzyme exhibited an apparent Km value of 30.4 mM and a Vmax of 2,564 U against hydrogen peroxide. The enzyme also exhibited a broad optimal pH $(5.0{\sim}9.0)$, and remained stable over a broad temperature range $(20^{\circ}C{\sim}60^{\circ}C)$. It maintained 90% activity against organic solvents (ethanol/chloroform) known hydroperoxidase inhibitors, and exhibited no detectable peroxidase activity. The catalase activity of the purified enzyme was reduced to 19 % of full activity as the result of the administration of 10 mM 3-amino-1,2,4-triazole, a heme-containing catalase inhibitor. Sodium cyanide, sodium azide, and hydroxylamine, all of which are known heme protein inhibitors, inhibited catalase activity by 50 % at concentrations of $11.5{\mu}M,\;0.52{\mu}M,\;and\;0.11{\mu}M$, respectively. In accordance with these findings, the enzyme was identified as a type of monofunctional catalase.

• BMB Reports
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• v.33 no.5
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• pp.412-416
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• 2000

The obligate aerobic Deinococcus are highly resistant against lethal effect of UV-and ionizing-radiation. Only five mesophilic Deinococcus species, i. e. D. radiodurans, D. radiophilus, D. proteolyticus, D. radiopugnans, and D. grandis are known. Since an indispensable role of catalase has been suggested in protecting cells against oxidative stress and UV radiation, Deinococcal catalase activity of each species and electrophoretic profiles of catalases were investigated on gel. Total catalase activity was varied among the species in the aerobically grown culture at stationary phase. The occurrence of multiple forms of catalases with different molecular weights in four species of Deinococcus and of a single catalase in D. radiopugnans suggests that each species shows the unique catalase profiles on gel. Some Deinococcal catalases also exhibit peroxidase activity. Since Deinococcus spp. are less-distinct to each other in their morphology, biochemical and physiological properties, the catalase profiles on PAGE would be useful in identifying the species of Deinococcus.

• Molecules and Cells
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• v.20 no.2
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• pp.247-255
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• 2005

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.

• BMB Reports
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• v.36 no.6
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• pp.608-610
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• 2003

Escherichia coli has two catalases, HPI and HPII. HPI is induced during logarithmic growth in response to low concentrations of hydrogen peroxide. This induction is OxyR-dependent. On the other hand, HPII is not peroxide-inducible but is induced in entry to the stationary phase. We demonstrate here that E. coli displayed higher HPI catalase activity when compared to the cultures that were grown in a normal medium, if grown in a medium supplemented with iron-citrate. Iron supplementation had no effect on HPII catalase. This increase of HPI activity was OxyR-independent and not observed in a ${\Delta}fur$ mutant. The physiological significance of the increase of HPI activity is unclear, but it appears that the katG gene that codes for HPI catalase is among the genes that are regulated by Fur.

• Journal of Periodontal and Implant Science
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• v.25 no.3
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• pp.529-538
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• 1995

It has been believed that the increased release of free oxygen radicals ($O_2^-,H_2O_2$, and $OH^-$) might be a factor in the pathogenesis of periodontal diseases. Antioxidant enzymes such as glutathione peroxidase(GSH-PX) and catalase can protect the tissue damage from the $H_2O_2$. In order to investigate the GSH-PX and catalase activity in the blood plasma and red blood cells(RBCs) of the patients with periodontitis, 19 patients who had good general health, attachment loss more than 6 mm and bone loss were selected as periodontitis group, 7 patients who had severely inflamed gingiva were selected as gingivitis group, and 15 volunteers with good general and periodontal health were selected as normal group. 17 of 26 patients were performed scaling and root planing to reduce the gingival inflammation for gingivitis and periodontitis groups, and were selected as posttreatment group. After blood plasma and RBCs were collected and separated 1 ml of peripheral blood from each subject, GSH-PX activity in blood plasma and RBCs was measured by the same method that Stefan et al. did, and catalase activity in RBCs was measured by the same method that Beers et al. did. The difference of GSH-PX and catalase activity between normal, gingivitis, and periodontitis groups was statistically analyzed by ANOVA with SPSS/PC+ program, and the difference between pretreatment and posttreatment groups was analyzed by Student t-test. The results were as follows : 1. GSH-PX activity in blood plasma was significantly lower in the gingivitis group($0.8683{\pm}0.0658$), periodontitis group($0.7130{\pm}0.1333$) than in the normal group($1.0241{\pm}0.0801$)(p<0.05), and GSH-PX activity in RBCs was significantly lower in the gingivitis groupt. $0.8156{\pm}0.1167$), periodontitis group($0.7533{\pm}0.1185$) than in the normal group($l.1963{\pm}0.2044$)(P<0.05), but there was no statistical significance in the difference of GSH-PX activity in RBCs between the gingivitis group and periodontitis group(p>0.05). 2. Catalase activity in RBCs was siginficantly lower in the periodontitis group($117.34{\pm}35.01$) than in the normal group($l52.38{\pm}32.09$)(p<0.05). 3. GSH-PX activity in blood plasma was significantly increased in the posttreatment groupe $1.0376{\pm}0.2820$) compared to the pretreatment group(0.7608 0.1600) (p<0.05), and GSH-PX activity in RBC was significantly increased in the posttreatment group($1.0421{\pm}0.2330$) compared to the pretreatment group($0.7728{\pm}0.1210$)(p<0.05). 4. There was no statistical significance in the difference of catalase activity in RBCs between the pretreatment group($112.04{\pm}43.65$) and posttreatment group($l33.41{\pm}39.16$)(p>0.05).The results, within the limits of the present experiment, suggest that the lowered activity of GSH-PX and catalase in blood plasma and RBCs may be related with periodontopathogenesis.

• Applied Biological Chemistry
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• v.49 no.4
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• pp.287-292
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• 2006

The effects of cadmium on the catalase activity and isozyme patterns under light and dark conditions of rice(Oryza sativa L. cv. Dongjin) seedlings were examined. Cadmium treatment resulted in the notable enhancement of $H_2O_2$ contents in the seedling roots and leaves under light and dark conditions. The catalase isozyme patterns in the roots were different from those in the leaves, showing tissue-specific expression of the enzyme. Moreover, the expression patterns of catalase isozymes in the green seedling roots were different from those in the etiolated seedling roots following cadmium treatment. The increase of total catalase activity was about 16 times at 1 mM cadmium and marked inductions of the isozyme CAT1 and CAT2 contributed to this increase in the green seedling roots. On the other hand, in the etiolated seedling roots, total catalase activity was lower than that of control at 0.5 and 1 mM cadmium, even though catalase activity increased about 3 times at 0.1 mM cadmium. The 3 fold increase of total catalase activity was mainly due to the increase of CAT1, CAT3 and CAT4 at 0.1 mM cadmium. However, treatment with higher concentrations of cadmium decreased the activity of CAT2 and CAT4 in the etiolated roots. In the leaves, the catalase existed as three isozymes; one cationic isozyme CATc, one neutral isozyme CATn and one anionic isozyme CAT1 in the control. The isozyme patterns and total activities remained unaffected by cadmium under light and dark conditions in the seedling leaves. Taken together, it seems that cadmium-induced changes of catalase might be regulated by light in the roots, but not in the leaves.

• Toxicological Research
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• v.13 no.4
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• pp.393-400
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• 1997

The effects of superoxide dismutase(SOD) and catalase on the toxicity of paraquat(PQ) were studied using diethyldithiocarbamate(DDC), 3-amino-1,2,4-triazole(AT) which are inhibitors of Cu, Zn-SOD and catalase in rats. Sprague Dawley rats were divide into 6 groups: control, DDC, PQ, AT, DDC+PQ, and AT+PQ group. The PQ (50 mg/kg body weight(BW); about half dose of $LD_{50}$) was administered with orally, otherwise AT(1.0g/kg BW) and DDC(1.0g/kg BW) were administered by intrperitoneal(iP) injection. The survival rate of rats in PQ+AT group was significantly decreased compared with PQ group while the difference of survival rate between DDC group and DDC+PQ group was not significant. The SOD activity after administration of DDC was decreased in liver, lung and kidney, but catalase activity was not changed. The catalase activity in liver, lung and kidney of AT treated rats was decreased, while SOD activity was not changed in this group. The effects of DDC and AT to the PQ toxicity was also observed in primary cultured rat Skin fibroblasts. The viable cells that was measured with MTT method, was decreased in AT+PQ treated group compared to PQ treated group, but the difference of cell viability between DDC treat group and DDC+PQ treated group was not observed. This result, AT potentlate PQ toxicity while DDC were not affect, suggested that the decreased catalase activity lead to elevation of hydrogen peroxide levels and PQ toxicity may be correlate with the hydrogen peroxide rather than the superoxides.