Purification and Properties of Glutathione Peroxidase from Mucor hiemalis
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概要
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Selenium-independent glutathione peroxidase was purified from a cell-free extract of Mucor hiemalis by ammoniumsulfate fractionation, column chromatographies on DEAE-Sephadex and hydroxylapatite, and gel filtration on Bio-Gel P-100. The purified enzyme was homogeneous on ultracentrifugation. The enzyme had a molecular weight of 45, 000 and an isoelectric point of 5.2. The enzyme could reduce cumenehydroperoxide and r-butyl hydroperoxide, but could not reduce hydrogen peroxide. The enzymewas highly specific for glutathione as a hydrogen donor. Mucor glutathione peroxidase was proved to be different from mammalian selenium-dependent glutathione peroxidase I and selenium-independent glutathione peroxidase II in some physicochemical and enzymatic properties.
- 社団法人 日本農芸化学会の論文
著者
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Aisaka Kazuo
Tokyo Research Laboratories Kyowa Hakko Kogyo Co. Ltd.
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Uwajima Takayuki
Tokyo Research Laboratories Kyowa Hakko Kogyo Co. Ltd.
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TERADA Osamu
Tokyo Research Laboratory, Kyowa Hakko Kogyo Co.
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