INTERACTION OF BOVINE ESTROGEN-RECEPTOR WITH IMMOBILIZED ZINC

被引：2

作者：

ATKINSON, HC ^{[1
]}

RATAJCZAK, T ^{[1
]}

HAHNEL, R ^{[1
]}

机构：

[1] UNIV WESTERN AUSTRALIA,KING EDWARD MEM HOSP WOMEN,DEPT OBSTET & GYNAECOL,ENDOCRINE RES LAB,SUBIACO,WA,AUSTRALIA

来源：

STEROIDS | 1990年 / 55卷 / 09期

关键词：

STEROIDS; ESTROGEN RECEPTOR; ZINC BINDING; SALT-DISSOCIATED RECEPTOR; DITHIOTHREITOL REQUIREMENT;

D O I：

10.1016/0039-128X(90)90099-W

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The metal-binding properties of partially purified untransformed or salt-dissociated bovine estrogen receptors were studied using zinc-chelated iminodiacetic acid gels. Only the salt-dissociated 5S recept or retained by the metal-chelated resin, and this interaction is dependent on the presence of dithiothreitol. The untransformed 9S receptor is not retained, indicating that the zinc-interacting amino acid residues may be masked by receptor-associated proteins such as 90K heat-shock protein or because of an unfavorable receptor conformation.

引用

页码：405 / 409

页数：5

共 26 条

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