亲和基质在从牛卵泡液中纯化抑制素中的应用。

The use of affinity matrices in the purification of inhibin from bovine follicular fluid.

作者信息

Jansen E H, Steenbergen J, de Jong F H, van der Molen H J

出版信息

Mol Cell Endocrinol. 1981 Feb;21(2):109-17. doi: 10.1016/0303-7207(81)90048-4.

Abstract

The protein associated with inhibin-like activity in bovine follicular fluid was purified 80- to 120-fold after successive adsorptions on different affinity matrices, i.e. Matrex gel red A, phenyl sepharose, omega-aminohexyl agarose and concanavalin-A sepharose. Partial characterization of the active protein resulted in the conclusion that inhibin from bovine follicular fluid is a hydrophobic glycoprotein with an apparent molecular weight between 60 000 and 70 000 daltons. An antiserum, raised against an 80-fold purified preparation, prevented the inhibin-like action of bovine follicular fluid on pituitary cells in vitro.

摘要

通过在不同的亲和基质（即Matrex凝胶红A、苯基琼脂糖、ω-氨基己基琼脂糖和伴刀豆球蛋白A琼脂糖）上连续吸附，牛卵泡液中与抑制素样活性相关的蛋白质被纯化了80至120倍。对活性蛋白的部分特性分析得出结论，牛卵泡液中的抑制素是一种疏水糖蛋白，其表观分子量在60000至70000道尔顿之间。针对80倍纯化制剂产生的抗血清，在体外可阻止牛卵泡液对垂体细胞的抑制素样作用。