HIGH-AFFINITY THYROXINE BINDING TO PURIFIED RAT-LIVER PLASMA-MEMBRANES

被引：54

作者：

GHARBI, J ^{[1
]}

TORRESANI, J ^{[1
]}

机构：

[1] FAC MED MARSEILLE,INSERM,U38,F-13385 MARSEILLE,FRANCE

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 88卷 / 01期

关键词：

D O I：

10.1016/0006-291X(79)91712-1

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：

Two sets of high-affinity thyroxine binding sites (KD 0.39 ± 0.06 nM and 23 ± 5 nM) were detected on purified rat liver plasma membranes. Thyroxine is bound with high stereospecificity regarding iodine substituents and alanine side chain modifications of the molecule. Thyroxine binding is inhibited by -SH blocking agents and proteases. The highest affinity thyroxine binding site is also affected by phospholipase A and is distinct from triiodothyronine binding sites present in the membrane preparations; arguments are given for its plasmalemma origin. © 1979.

引用

页码：170 / 177

页数：8

共 29 条

[1]

Aronson N N Jr, 1974, Methods Enzymol, V31, P90

[2] ACTION OF THYROID-HORMONE [J].