No Abstract Available.
Catalase* ; Streptococcus pneumoniae* ; Streptococcus*

Proteins are known to be carbamylated as a result of reactions with ureaderived cyanate. We investigated the effect of carbamylation by cyanate on the catalase activity which is known that its decreased activity contributes to cataract formation, and on the lens protein. Catalase and lens protein were carbamylated by incubation with cyanate at 37degrees C. The extent of carbamylation was monitored by following the loss of free amino group using trinitrobenzenesulphonic acid. The level of carbamylated protein was 76% in patients with cataract. Carbamylated proteins in normal lens from rabbits and carbamylated catalase were increased as the time of exposure to cyanate activity. Our results suggest that cyanate is an inhibitor of catalase, and carbamylation of catalase as a result of reaction with ureaderived cyanate may contribute to cataract formation.
Catalase* ; Cataract ; Humans ; Rabbits

No abstract available.
Animals ; Catalase* ; Glutathione* ; Lung* ; Rats*

OBJECTIVES: This study was performed in order to investigate the molecular mechanism regulating nitric oxide synthase(NOS) induced by alpha-quartz in Rat2 fibroblast. METHODS: alpha-quartz-induced nitric oxide(NO) and H2O2 formation and alpha- quartz-induced iNOS protein expression in Rat2 fibroblast were monitored. With iNOS inhibitor(L-N6- (1-iminoethyl)lysine hydrochloride, L-NIL) or antioxidant(catalase), we observed NO and H2O2 formation and iNOS protein expression in Rat2 fibroblast stimulated with alpha-quartz. RESULTS: alpha-quartz stimulated iNOS-induced NO and H2O2 formation in Rat2 fibroblast. L-NIL inhibited H2O2 formation and iNOS protein expression by alpha-quartz in Rat2 fibroblast. Pretreatment with catalase blocked the autoinhibitory pathway of iNOS by iNOSinduced H2O2, therefore H2O2 and NO production and iNOS protein expression were increased in Rat2 fibrobalst stimulated with alpha-quartz CONCLUSIONS: alpha-quartz-induced iNOS stimulated H2O2 formation in Rat2 fibroblast. INOS-induced H2O2 by alpha-quartz plays an important role in the autoinhibition pathway for regulating the iNOS function in Rat2 fibroblast
Catalase ; Fibroblasts* ; Homeostasis* ; Hydrogen Peroxide* ; Hydrogen* ; Nitric Oxide ; Quartz

This study investigated the effect of coffee intake and exercise on the antioxidative activity and plasma cholesterol profile of physically trained rats while they were exercising. Forty eight rats were under either the control diet with water (C) or control diet with coffee (CF) and at the same time they were given physical training for 4 weeks. In terms of physical training, the rats were exercised on a treadmill for 30 minutes everyday. At the end of 4 weeks, animals in each dietary group were subdivided into 3 groups: before-exercise (BE); during-exercise (DE); after-exercise (AE). Animals in the DE group were exercised on a treadmill for one hour, immediately before being sacrificed. Animals in the AE group were allowed to take a rest for one hour after exercise. TG levels were significantly high in coffee intake group than in control group. Also TG level of AE group was significantly higher than that of BE group. Exercise and coffee-exercise interaction effects were significant in total cholesterol (P = 0.0004, 0.0170). The AE of coffee intake group showed highest total cholesterol levels. HDL-cholesterol was significantly lower in coffee intake group than in control group. Coffee, exercise, and coffee-exercise interaction effects were significant in SOD (P = 0.0001, 0.0001, and 0.0001). The AE and BE of coffee intake group showed higher SOD levels than the other four groups. Catalase activities were significantly higher in coffee intake group than control group. No significant main effect was found in GSH/GSSG. Coffee, exercise, and coffee-exercise interaction effects were significant in MDA levels (P = 0.0464, 0.0016, and 0.0353). The DE and AE of coffee intake group and the DE of control group showed higher MDA levels than the BE of control group. Therefore, coffee intake can promote activities of antioxidant enzyme but it also increases MDA and decreases HDL-cholesterol in physically trained rats.
Animals ; Catalase ; Cholesterol ; Coffee ; Diet ; Plasma ; Rats ; Water

In order to elucidate the mechanism of oxidative damage of cadimu(Cd) on culturedmouse preimplantation embyors.The embryotoxocity of Cd was examined after cultured mouse preimplantation embryoswere exposed to various concentrations of CdCl2. In addition, the protected effect of antioxidant,catalase against Cd-induced embryotoxicity was investigated.CdCl2 decreased the development of cultured mouse preimplantation embryos in dose andtime-dependent manners, and also oxidative damage was involoved in Cd-induced embryotoxicityin mouse preimplantation embryos by the prevention of catalase on Cd-induced toxicity.
Animals ; Blastocyst ; Cadmium Chloride ; Cadmium* ; Catalase ; Embryonic Structures* ; Mice

In order to elucidate the mechanism of oxidative damage of cadimu(Cd) on culturedmouse preimplantation embyors.The embryotoxocity of Cd was examined after cultured mouse preimplantation embryoswere exposed to various concentrations of CdCl2. In addition, the protected effect of antioxidant,catalase against Cd-induced embryotoxicity was investigated.CdCl2 decreased the development of cultured mouse preimplantation embryos in dose andtime-dependent manners, and also oxidative damage was involoved in Cd-induced embryotoxicityin mouse preimplantation embryos by the prevention of catalase on Cd-induced toxicity.
Animals ; Blastocyst ; Cadmium Chloride ; Cadmium* ; Catalase ; Embryonic Structures* ; Mice

Since Mycobacterium leprae, the causative organism of Leprosy, proliferate inside macrophages, it has been speculated that catalase encoded by the katG gene may protect acid-fast bacilli from the deleterious effects of peroxide generated from macrophage and may play a crucial role in the survival of M. leprae in vivo. The homology of E. coli katG gene is also identified from M. tuberculosis and M. leprae recently. However, the katG gene of M. leprae is thought to be a pseudogene, unlike that of M. tuberculosis, because it contains multiple deletions, implicating that isoniazid(INH), which is activated to a potent tuberculocidal agent by catalase encoded by the katG gene, is unlikely to be of therapeutic benefit to leprosy patients. We have tested 1) the role of KatG protein in activation of INH by using INH susceptible test of M. smegmatis mc(2)155 and BH1, and 2) the effect of INH on M. leprae growth by radiorespirometric assay to examine the catalase-like activity in M. leprae. It was found that the viability of M. leprae was decreased at 20 microgram/ml of INH and higher concentrations. We confirmed the role of KatG protein in activation of INH and our results suggest that a catalase-like activity other than katG is present in M. leprae.
Catalase ; Humans ; Isoniazid* ; Leprosy ; Macrophages ; Mycobacterium leprae ; Pseudogenes ; Tuberculosis

No abstract available.
Catalase ; Erythrocytes* ; Glutathione Peroxidase ; Humans ; Infant, Newborn* ; Superoxide Dismutase

OBJECTIVETo characterize the property of uricase loaded in uricase-catalase liposomes (BUCLPs) prepared using borate buffer.

METHODSBUCLPs were prepared using reverse-phase evaporation, and the physicochemical properties of uricase in the prepared BUCLPs were examined.

RESULTSThe optimal temperature of BUCLP and URI was 40 degrees celsius, their optimal pH values were 8.0 and 8.5, and their Michaelis-Menten constants were 14.207 µmol/L and 13.623 µmol/L, respectively. Fluorescence intensity of nanoliposome-loaded uricase-catalase that bound to FITC was higher than that of uricase-catalase binding directly with FITC; the fluorescence intensity of BUCLP was higher than that of free uricase-catalase at 280 nm.

CONCLUSIONUricase activity is enhanced after loading in uricase and catalase liposomes.