Relationship of human liver dihydrodiol dehydrogenases to hepatic bile-acid-binding protein and an oxidoreductase of human colon cells
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- Kazuya MATSUURA
- Biochemistry Laboratory, Gifu Pharmaceutical University, Mitahora-higashi, Gifu 502, Japan
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- Yoshiyuki TAMADA
- Biochemistry Laboratory, Gifu Pharmaceutical University, Mitahora-higashi, Gifu 502, Japan
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- Kumiko SATO
- Biochemistry Laboratory, Gifu Pharmaceutical University, Mitahora-higashi, Gifu 502, Japan
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- Yoshiyuki MIYABE
- Biochemistry Laboratory, Gifu Pharmaceutical University, Mitahora-higashi, Gifu 502, Japan
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- Yoshihiro DEYASHIKI
- Biochemistry Laboratory, Gifu Pharmaceutical University, Mitahora-higashi, Gifu 502, Japan
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- Naoko ISHIDA
- Biochemistry Laboratory, Gifu Pharmaceutical University, Mitahora-higashi, Gifu 502, Japan
書誌事項
- 公開日
- 1996-01-15
- DOI
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- 10.1042/bj3130373
- 公開者
- Portland Press Ltd.
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説明
<jats:p>We previously isolated three monomeric dihydrodiol dehydrogenases, DD1, DD2 and DD4, from human liver, and cloned a cDNA (C9) thought to encode DD2, which is identical with those for human bile-acid-binding protein and an oxidoreductase of human colon carcinoma HT29 cells. In the present study we have provided evidence that the C9 cDNA clone encodes DD1, not DD2. A recombinant enzyme expressed from the cDNA in a bacterial system was purified, and its catalytic properties, bile-acid-binding ability and primary sequence were compared with those of the hepatic dihydrodiol dehydrogenases. The results show that DD1 encoded by C9 possesses prostaglandin F synthase activity but low affinity for lithocholic acid, whereas DD2, showing differences of six amino acid residues from the DD1 sequence, exhibited high-affinity binding for the bile acid. Refined relationship between dihydrodiol dehydrogenases and their related proteins of human tissues is proposed.</jats:p>
収録刊行物
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- Biochemical Journal
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Biochemical Journal 313 (2), 373-376, 1996-01-15
Portland Press Ltd.