Inactivation of Yeast Alcohol Dehydrogenase by Dehydroascorbic Acid and D-Arabinosone
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概要
- 論文の詳細を見る
Treatment of yeast alcohol dehydrogenase [EC 1.1.1.1] (YADH) with dehydroascorbic acid (DHA) or D-arabinosone resulted in inactivation of the enzyme. Effects of other dicarbonyl compounds, such as D-glucosone and triosone, on YADH were also examined, and they were found to be less effective than D-arabinosone or ineffective.The inactivation by DHA or D-arabinosone was accompanied by decrease of free sulfhydryl (SH) groups of the protein, and it was completely prevented by addition of SH compound. Treatment of the inactivated enzyme with β-mercaptoethanol led to partial reactivation with concomitant restoration of SH groups.The inactivation of YADH was accelerated by NAD+ as well as NADH specifically.These results strongly supported a possibility that DHA and D-arabinosone afforded the inhibitory effect on YADH through oxidation or modification of SH groups of the protein, which was favored in the presence of the coenzyme.
- 日本ビタミン学会の論文
著者
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藤本 貞毅
Laboratory Of Biochemistry Kyoto Pharmaceutical University
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上原 喜八郎
Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University
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藤本 貞毅
Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University
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