Modification in the purification of the sex steroid-binding protein of human serum by affinity chromatography.
Modification in the purification of the sex steroid-binding protein of human serum by affinity chromatography.
复制标题
通过亲和层析纯化人血清性类固醇结合蛋白的改进。
DOI：
10.1016/0003-2697(80)90440-6
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发表时间：
1980
影响因子：
2.9
通讯作者：
J. Lewis
中科院分区：
文献类型：
--
作者：
P. Pétra;J. Lewis
本文描述了一种人血清性类固醇结合蛋白的纯化方法。该程序是显着上级最近公布的（K。E. Mickelson，D. C. Teller和P. H. Pétra，1978，Biochemistry 17，1409-1415），并且应该取代它用于相对大量的同质蛋白质的常规制备。步骤包括二乙氨基乙基纤维素层析、5α-二氢睾酮-17 α-己基二氨基乙基-（1，4-丁二醇二缩水甘油醚）-琼脂糖亲和层析和制备型聚丙烯酰胺凝胶电泳。该新方法与先前发表的方法之间最重要的区别是亲和吸附剂含有共价连接在17α-位而不是17β-位的类固醇。这种改进允许以63%的总产率纯化每个制备物至少12 mg的均质蛋白。同质蛋白质的性质与先前描述的相同。
A purification procedure for the sex steroid-binding protein of human serum is described. The procedure is significantly superior to that recently published (K. E. Mickelson, D. C. Teller, and P. H. Pétra, 1978, Biochemistry17, 1409–1415) and should replace it for the routine preparation of homogeneous protein in relatively larger quantities. The steps involved diethylaminoethyl-cellulose chromatography, affinity chromatography on 5α-dihydrotestosterone-17α-hexanyldiaminoethyl-(1,4-butanediol diglycidyl ether)-agarose, and preparative polyacrylamide gel electrophoresis. The most important difference between this new procedure and that previously published is the affinity adsorbent with contains the steroid covalently linked at the 17α-position rather than the 17β-position. This modification allows the purification of at least 12 mg of homogeneous protein per preparation with a 63% total yield. The properties of the homogeneous protein are the same as previously described.