• Korean Journal of Veterinary Service
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• v.30 no.3
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• pp.291-304
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• 2007

Mutants of an obligate aerobic bacterium, Vitreoscilla, that have deficiency in heat-labile catalase-peroxidase hydroperoxidase I (HPI) were created by EMS treatment. The catalase-peroxidase HPI-deficient mutant showed substantially lower peroxidase activity in exponential and mid-stationary phase compared with the wild type strain. In late stationary phase, the mutant exhibited no peroxidase activity. Peroxidase deficiency in the mutant was revealed by polyacrylamide gels stained for peroxidase activity. Characteristically, catalase levels in the mutant increased about 14- and 8-fold during growth in the exponential and stationary phases, respectively, compared to those in the wild type, suggesting a compensatory effect for protection from $H_2O_2$ toxicity. The mutant showed differences in physiology from the wild type: retardation in growth rate and decrease in oxygen consumption. Both the wild type and the catalase-peroxidase HPI-deficient mutant of Vitreoscilla had lower growth rates in media containing increasing $H_2O_2$ concentrations. However, the mutant exhibited an additionally decreased growth rate after 6 to 8 h of growth compared to the wild type. The wild type was resistent up to 20 mM $H_2O_2$, whereas the mutant was very sensitive to high concentrations of exogenous $H_2O_2$. Although elevated catalase levels would provide protection of the bacteria from the deleterious effect of $H_2O_2$, it did not appear to be complete. Cell-free extracts of the mutant showed decreased NADH oxidation rates and higher accumulation of $H_2O_2$ during this oxidation. These results may account for the impaired growth and earlier onset of death phase by the catalase-peroxidase HPI-deficient mutant of Vitreoscilla.

• Journal of the Korean Chemical Society
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• v.37 no.12
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• pp.1068-1075
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• 1993

Catalase activities were assayed on the leaves and roots of Tomato (Lycopersicum esculentum) as a function of age for 1 year after germination. The enzyme activities of root tissue demonstrated to be insignificant through all stages of development. On the other hand, the catalase activities of leaf peroxisomal fractions showed remarkable changes with peak value of 76 ${\mu}mol$/ml/min at germination stage within 2 weeks growth, 7.2 ${\mu}mol$/ml/min at adult stage around 4∼5 months growth and very small activities at aged period around 11∼12 months growth. It is suggested that there may be two factors concerning such catalase activities in relation with age, firstly the glyoxisomal reactions including glyoxylate cycle and $\beta$-oxidation at germination stage and secondly photosynthesis hereafter seemed to affect age dependent changes of catalase activity by producing coincident amount of $H_2O_2$. In addition, NADPH coenzyme was found to have ability to restore catalytic acitivity of inactivated catalase (compound II) at all stages of development except old age, indicating NADPH would play a role as catalase protector against deleterious substrate,$H_2O_2$.

• Applied Biological Chemistry
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• v.39 no.3
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• pp.222-226
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• 1996

Lipoxygenase, peroxidase and catalase activities were determined in tissues and brines of refrigerated dill pickling cucumbers in response to pickling process, storage and $H_2O_2$. Lipoxygenase was almost inactivated within 1 day exposure to dill pickling brine, and then gradually declined during storage. In contrast, peroxidase activity in cucumber tissue decreased steadily for 4 days after exposure to dill pickling brine. Catalase was present in fresh cucumber tissues, but only slight activity was observed after submerging cucumbers in pickling brine. Lipoxygenase, peroxidase and catalase activities were rapidly inactivated in cucumbers exposed to brine containing $H_2O_2$.

• Bulletin of the Korean Chemical Society
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• v.21 no.6
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• pp.567-570
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• 2000

Bovine liver catalase was exposed to cysteine, as a natural inactivator metabolize, causing autoxidation-generating $H_2O_2$ continuously. The catalase species concentrations and activity measurement were done by spectrophotometry in phosphate buffer 10mM, pH 6.5, and 27 $^{\circ}C$. The activity of catalase decreased continuously due to the conversion of active ferricatalase species, E-Fe (III), to an inactive enzyme species, E-Fe (IV). This conversion is related to the slow production of $H_2O_2generated$ by autoxidation of cysteine. The free SH-group of cysteine has an essential role in production of $H_2O_2$ and hence inactivation of catalase. NADPH can protect catalase against inactivation due to the conversion of inactive form of E-Fe (IV) to ferricatalase species, E-Fe (III).

• Microbiology and Biotechnology Letters
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• v.5 no.3
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• pp.113-118
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• 1977

Into the precontaminated farm milk hydrogen peroxide ($H_2O$$_2$) was added at the concentrations ranging from 0.01％ to 0.05％ and kept at 3$0^{\circ}C$ for 16 hours with periodical determinations for viable counts, residual $H_2O$$_2$, and lactic acid. Under the tested conditions the initial level of contaminated bacteria could be arrested from growing at least for 8, 12, and 16 hours by treating the milk with 0.01, 0.02. and 0.03 per cent of $H_2O$$_2$, respectively. Furthermore, when the $H_2O$$_2$concentrations ware limited within the level of 0.03 Per cent the added $H_2O$$_2$was completely decomposed within 12 hours without the aid of external catalase and the decomposition time decreased in parallel with the $H_2O$$_2$ concentrations. A safer use of $H_2O$$_2$for preserving farm milk temporarily by limiting its concentration has been discussed.

• Tuberculosis and Respiratory Diseases
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• v.40 no.3
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• pp.236-249
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• 1993

Background: Among the injurious agents to which the lung airspaces are constantly exposed are reactive species of oxygen. It has been widely believed that reactive oxygen species may be implicated in the etiology of lung injuries. In order to elucidated how this oxidant causes lung cell injury, we investigated the effects of exogenous $H_2O_2$ on alveolar epithelial barrier characteristics. Methods: Rat type II alveolar epithelial cells were plated onto tissue culture-treated polycarbonate membrane filters. The resulting confluent monolayers on days 3 and 4 were mounted in a modified Ussing chamber and bathed on both sides with HEPES-buffered Ringer solution. The changes in short-circuit current (Isc) and monolayer resistance (R) in response to the exogenous hydroperoxide were measured. To determine the degree of cellular catalase participation in protection against $H_2O_2$ injury to the barrier, experiments were repeated in the presence of 20 mM aminotriazole (ATAZ, an inhibitor of catalase) in the same bathing fluid as the hydroperoxide. Results: These monolayers have a high transepithelial resistance (>2000 ohm-$cm^2$) and actively transport $Na^+$ from apical fluid. $H_2O_2$(0-100 mM) was then delivered to either apical or basolateral fluid. Resulting indicated that $H_2O_2$ decreased Isc and R gradually in dose-dependent manner. The effective concentration of apical $H_2O_2$ at which Isc (or R) was decreased by 50% at one hour ($ED_{50}$) was about 4 mM. However, basolateral $H_2O_2$ exposure led to $ED_{50}$ for Isc (and R) of about 0.04 mM. Inhibition of cellular catalase yielded $ED_{50}$ for Isc (and R) of about 0.4 mM when $H_2O_2$ was given apically, while $ED_{50}$ for basolateral exposure to $H_2O_2$ did not change in the presence of ATAZ. The rate of $H_2O_2$ consumption in apical and basolateral bathing fluids was the same, while cellualr catalase activity rose gradually with time in culture. Conclusion: Our data suggest that basolateral $H_2O_2$ may affect directly membrane component (e.g., $Na^+,\;K^+$-ATPase) located on the basolateral cell surface. Apical $H_2O_2$, on the other hand, may be largely degraded by catalase as it passes through the cells before reaching these membrane components. We conclude that alveolar epithelial barrier integrity as measured by Isc and R are compromised by $H_2O_2$ being relatively sensitive to basolateral (and insensitive to apical) $H_2O_2$.

• Biomolecules & Therapeutics
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• v.4 no.4
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• pp.402-407
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• 1996

Effects of oxidative stress on the induction of apoptosis and the activity of antioxidant enzymes were investigated in HL-60 cells using $H_2O$$_2$and cisplatin which generate oxygen species in the cell. Various concentrations of oxidants were treated to cells and at different incubation time, cells were harvested for assays. Cell viability, morphology by propidium iodide staining and DNA fragmentation by agarose gel electrophoresis were observed to determine whether they induce apoptosis. The activity of antioxidant enzymes such as superoxide dismutase and catalase was also measured to evaluate the cellular response to the oxidative damage. The results are as follows: $H_2O$$_2$ induced apoptosis at 10 $\mu$M after 6h incubation, while it took 12h for cisplatin. Both oxidants induced the superoxide dismutase activity at a tolerable low concentration. However, at a concentration which causes apoptotic cell death, the enzyme level was dropped markedly at first and then recovered to the normal level after which it declined again, probably due to cell death. On the other hand, changes in the activity of catalase were not significant at most concentrations except the statistically significant decrease at 24h after 10 $\mu$M-$H_2O$$_2$treatment. In this study, $H_2O$$_2$- and cisplatintreated cells showed similar results in apoptotic response and enzyme activities, suggesting that anticancer activity of cisplatin may be related, at least in part, to the production of oxygen free radicals.

• Journal of Microbiology
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• v.33 no.3
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• pp.239-243
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• 1995

Deinococcus radiophilus, an UV resistant bacterium seemed to contain three issoenzymes of catalase. Among them, the samllest and most abundant species in cell-free extract, catalase-3 which also exhibited peroxidase activity was purified to electrophoretic homogeneity (145-fold purification) by chromatographic procedures. Its molecular weight was 155 kDa composed of four 38 kDa subunits. The $K_{m}$ value of catalase-3 for H$\_$2/O$\_$2/ was approximately 0.5 mM. This enzyme showed a typical ferric heme spectrum with maximum absorption at 405 nm. Upon binding to cyanide, the 405 nm peak shifted to 420 nm. Catalase-3 was very sensitive to inhibitors of heme proteins, such as cyanide, azide and hydroxylamine. A ratio of A$\_$405/A$\_$28O/ was 0.5 Catalase-3 was active over a wide range of pH, between pH 7 and 10. The enzyme was rather heat-labile and partially sensitive to edthanol-chloroform treatment, but resistant to 3-amino-1, 2, 4-triazole. Catalase-3 of D. radiophilus, which is a bifunction catalatic peroxidatic enzyme seemed to share certain molecular properties with the typical catalase and the catalase-[roxidase along with its own unique features.

• YAKHAK HOEJI
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• v.43 no.5
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• pp.598-605
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• 1999

The hot water and mathanol extracts of Artemisia argyi showed considerable cytotoxicities against H9(ATCC HTB 176) cancer cell with IC50 values of $48.6{\;}\mu\textrm{g}/ml$ and $51.9{\;}\mu\textrm{g}/ml$, respectively. These cytotoxicities were found to be dependent on the extract concentrations and culture days. CuZnSOD and MnSOD activities were significantly increased in the cytoplasm and mitochondria fractions of cancer cell, and media in the presence of Artemisia argyi. Such enhanced SOD activities were generally in the range of two to threefolds. In contrast to SOD, catalase and glutathione peroxidase activities were not detected at all. These results suggest that Artemisia argyi have generated $O_2^-$ in the mitochondria and cytoplasm of H9 cancer cell with concurrent induction of CuZnSOD and MnSOD in situ, which dismutate $O_2^-{\}to{\;}H_2O_2$. Without coordinated actions of catalase and/or glutathione peroxidase $H_2O_2$ is easily converted to very toxic OH and these reactive oxygen species together might have induced necrosis and/or apoptosis of H9 cell.

• The Journal of Korean Medicine
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• v.19 no.1
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• pp.38-48
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• 1998

This study was undertaken to determine whether Salviae-radix (SVR) extraction prevents the oxidant-induced cell injury and thereby exerts protective effect against oxidant-induced inhibition of tetraethylammonium uptake (TEA) in renal corticaJ sices. SVR (5%) attenuated $H_2O_2-induced$ inhibition of TEA uptake. $H_2O_2$ increased LDH release and lipid peroxidation in a dose-dependent manner. These changes were prevented by SVR extraction. The protective effect of SVR on LDH release was dose-dependent over the concentration range of 0.1-0.5%, and that on lipid peroxidation over the concentration ranges of 0.05-2%. SVR significantly prevented Hg-induced lipid peroxidation. SVR extraction (0.5%) increased cellular GSH content in normal and $H_2O_2-treated$ tissues. When slices were treated with 100 mM $H_2O_2$, catalase activity was decreased, which was prevented by 0.5% SVR extraction. The activity of glutathione peroxidase but not superoxide dismutase was significantly increased by 0.5% SVR extraction in $H_2O_2-treated$ tissuces. These results suggest that SVR has an antioxidant action and thereby exerts benefical effect against oxidant-induced impairment of membrane transport function. This effect of SVR is attributed to an increase in endogenous antioxidants such as GSH, catalase and glutathione peroxidase.