大鼠肝微粒体中3α-羟基类固醇脱氢酶的增溶与纯化（作者译）
[Solubilization and purification of a 3alpha-hydroxysteroid dehydrogenase in rat liver microsomes (author's transl)].
作者信息
Golf S W, Graef V, Nowotny E
出版信息
Hoppe Seylers Z Physiol Chem. 1976 Jan;357(1):35-40. doi: 10.1515/bchm2.1976.357.1.35.
PMID:2535
Abstract
The microsomal 3-hydroxysteroid dehydrogenases were solubilized with lubrol, a non-ionic detergent. A 3alpha-hydroxysteroid dehydrogenase is purified about 100-fold by double affinity chromatography on 5alpha-dihydrotestosterone-Sepharose. This enzyme can use both NADH and NADPH as coenzymes.
摘要
微粒体3-羟基类固醇脱氢酶用非离子去污剂卢勃罗尔溶解。通过在5α-二氢睾酮-琼脂糖上进行双亲和层析，一种3α-羟基类固醇脱氢酶被纯化了约100倍。这种酶可以使用NADH和NADPH作为辅酶。
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