类固醇硫酸盐的酶促合成。十三。人胎儿肾上腺脱氢表雄酮磺基转移酶的分离与性质。
Enzymic synthesis of steroid sulphates. XIII. Isolation and properties of dehydroepiandrosterone sulphotransferase from human foetal adrenals.
作者信息
Adams J B, McDonald D
出版信息
Biochim Biophys Acta. 1980 Sep 9;615(1):275-8. doi: 10.1016/0005-2744(80)90031-5.
PMID:6932974
Abstract
Human foetal adrenals have provided a rich source of steroid alcohol sulphotransferase (EC 2.8.2.-). The latter was isolated in pure form in one step by affinity chromatography on an (NH4)2SO4 cut derived from the cytosol fraction of the glands. The yield was 6-fold higher than that obtained from adult human adrenals. General properties of the enzyme are given and it appears to be identical to that obtained previously from adult human adrenals.
摘要
人类胎儿肾上腺一直是甾体醇硫酸转移酶（EC 2.8.2.-）的丰富来源。通过对源自肾上腺胞质溶胶部分的硫酸铵分级分离物进行亲和层析，一步法将后者分离为纯形式。产量比从成年人类肾上腺获得的产量高6倍。给出了该酶的一般特性，它似乎与先前从成年人类肾上腺获得的酶相同。
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