マサバ血合肉組織グルタチオンレダクタ-ゼの単離と性質〔英文〕

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Glutathione reductase[EC 1.6.4.2] from the mackerel's dark muscle was purified 12, 400-fold with a 16% yield in electrophoretically homogeneous state, as judged by polyacry lamide disc gel electrophores in the presence and absence of sodium dodecylsulfate. The protein was highly fluorescent and showed a spectrum characteristic to flavoprotein. The molecular weight of the enzyme was estimated to be 110, 000 for the native and 56, 000 for the denatured. The enzyme was most active at around PH 7.3, less stable below PH 5, with the incubation at 75°C for 15 min brought about a complete loss of activity. An apparent Km of 9.7×10-5M was obtained for oxidized glutathione and 5.5×10-6M for NADPH. Effect of thiol inhibitors and metal ions before and after treatment with NADPH on catalytic activity was investigated. The fact strongly suggested the involvement of active site disulfide hond in the catalytic activity was investigated. The fact strongly suggested the involvement of active site disulfide hond in the catalytic mechanism as proposed on desulfide reductases.
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