Reconstitution of Apo-DT-diaphorase with Flavin-Adenine Dinucleotide
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概要
- 論文の詳細を見る
The binding of flavin-adenine dinucleotide (FAD) in DT-diaphorase was studies. Incubation with 4M guanidine-HCl at 0℃ rapidly dissociated FAD from the enzyme, and incubation of the apo-enzyme with FAD at 37℃ restored maximally about 50% (for menadione-reducing activity), or 330% (for ferricyanide-reducing activity) of the initial activity. The half-time required to reconstitute the apo-enzyme with FAD was 2min for menadione-reducing activity and the K_m value of the apo-enzyme for FAD was 0.23μM. These results show that DT-diaphorase contains non-covalently bound FAD as a prosthetic group.
- 社団法人日本薬学会の論文
- 1986-11-25
著者
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吉原 新一
Institute Of Pharmaceutical Sciences Hiroshima University School Of Medicine
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吉村 英敏
中村学園大・食物栄養
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吉村 英敏
Faculty Of Pharmaceutical Sciences Kyushu University
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古賀 信幸
Faculty of Pharmaceutical Sciences, Kyushu University
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和田 郁夫
Faculty of Pharmaceutical Sciences, Kyushu University
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Yoshimura Hidetoshi
Department Of Food And Nutrition Nakamura Gakuen University
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和田 郁夫
Faculty Of Pharmaceutical Sciences Kyushu University
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