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雌性兔肾细胞质中的3(17)α-羟基类固醇脱氢酶。该酶多种形式的纯化与特性研究。

A 3(17) alpha-hydroxysteroid dehydrogenase of female rabbit kidney cytosol. Purification and characterization of multiple forms of the enzyme.

作者信息

Lau P C, Layne D S, Williamson D G

出版信息

J Biol Chem. 1982 Aug 25;257(16):9444-9.

PMID:6955302
Abstract

A mammalian hydroxysteroid dehydrogenase having both 3 alpha- and 17 alpha-enzyme activity is described for the first time. Multiple forms of this 3(17) alpha-hydroxysteroid dehydrogenase are present in the cytosol of female rabbit kidney. Four forms of this enzyme were resolved by a purification procedure which included DEAE-cellulose chromatography and isoelectric focusing and three of the isolated enzymes were homogeneous on the basis of polyacrylamide gel electrophoresis. The purified enzymes exhibited 17 alpha-enzyme activity toward both androgen and estrogen substrates and 3 alpha-enzyme activity toward androgens of the 5 alpha-androstane series. In general, the 3 alpha-enzyme activity was greater than the 17 alpha-enzyme activity and the latter activity was greater toward androgens than estrogens. There were differences in substrate specificity among the enzyme forms. In particular, with estrogen substrates one of the forms displayed a high specificity toward 17 alpha-estradiol 3-glucuronide.

摘要

首次描述了一种同时具有3α-和17α-酶活性的哺乳动物羟基类固醇脱氢酶。雌性兔肾细胞质中存在这种3(17)α-羟基类固醇脱氢酶的多种形式。通过包括DEAE-纤维素色谱和等电聚焦的纯化程序分离出该酶的四种形式,并且基于聚丙烯酰胺凝胶电泳,其中三种分离出的酶是均一的。纯化后的酶对雄激素和雌激素底物均表现出17α-酶活性,对5α-雄甾烷系列的雄激素表现出3α-酶活性。一般来说,3α-酶活性大于17α-酶活性,且后者对雄激素的活性比对雌激素的活性更高。酶的不同形式之间存在底物特异性差异。特别是,对于雌激素底物,其中一种形式对17α-雌二醇3-葡萄糖醛酸苷表现出高特异性。

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