Characterization of multiple forms of carbonyl reductase from chicken liver.

Enzyme Pub Date : 1992-01-01 DOI:10.1159/000468791
T Nishinaka, Y Kinoshita, N Terada, T Terada, T Mizoguchi, T Nishihara
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引用次数: 13

Abstract

Three enzyme forms (CR1, CR2 and CR3) of carbonyl reductase were purified from chicken liver with using 4-benzoylpyridine as a substrate. CR1 was a dimeric enzyme composed of two identical 25-kD subunits. CR2 and CR3 were monomeric enzymes whose molecular weights were both 32 kD. CR1 exhibited 17 beta-hydroxysteroid dehydrogenase activity as well as carbonyl reductase activity in the presence of both NADP(H) and NAD(H). CR2 and CR3 had similar properties with regard to substrate specificity and inhibitor sensitivity. They could exhibit the activity only with NADPH and had no hydroxysteroid dehydrogenase activity. CR2 and CR3 cross-reacted with anti-chicken kidney carbonyl reductase antibody, though CR1 did not. The results suggest that CR1 is a hydroxysteroid dehydrogenase, and CR2 and CR3 are similar to each other and to the kidney enzymes.

鸡肝中多种形式羰基还原酶的研究。
以4-苯甲酰基吡啶为底物,从鸡肝脏中纯化出三种羰基还原酶(CR1、CR2和CR3)。CR1是由两个相同的25-kD亚基组成的二聚体酶。CR2和CR3均为单体酶,分子量均为32 kD。CR1在NADP(H)和NAD(H)存在下均表现出17 β -羟基类固醇脱氢酶活性和羰基还原酶活性。CR2和CR3在底物特异性和抑制剂敏感性方面具有相似的特性。它们只对NADPH有活性,没有羟基类固醇脱氢酶活性。CR2和CR3与抗鸡肾羰基还原酶抗体发生交叉反应,而CR1不发生交叉反应。结果表明,CR1是一种羟基类固醇脱氢酶,CR2和CR3与肾酶相似。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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