Enzymatic Properties of Dipeptidyl Carboxypeptidase from Bacillus pumilus(Biological Chemistry)
スポンサーリンク
概要
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Enzymatic properties of dipeptidyl carboxypeptidase (DCP) from Bacillus pumilus were investigated. The enyme was more active on tri- and tetrapeptides than angiotensin-converting enzyme (ACE) from rabbit lung. The presence of chloride ion is essential for the hydrolysis. The Km value of angiotensin I for the enzyme was 0.119×10^<-3> M. The enzyme was not inhibited by the mammalian ACE inhibitors lisinopril and enalaprilat. The enzyme is readily inhibited by EDTA but restored by Co^<2+>, Mn^<2+>, and Zn^<2+>. Therefore, it seems to be a zinc-metallo protease.
- 1991-07-23
著者
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Kusaka Kaname
Biochemical Research Laboratory Ezaki Glico Co. Ltd.
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Okada S
Biochemical Research Laboratory Ezaki Glico Co. Ltd.
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NAGAMORI YOICHI
Ezaki Glico Biochemical Research Laboratories
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KUSAKA KANAME
Ezaki Glico Biochemical Research Laboratories
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OKADA SHIGETAKA
Ezaki Glico Biochemical Research Laboratories
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FUJISHIMA Noboru
Ezaki Glico Biochemical Research Laboratories
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Nagamori Y
Ezaki Glico Biochemical Research Laboratories
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