PARTIAL-PURIFICATION AND CHARACTERIZATION OF NUCLEAR TRIIODOTHYRONINE BINDING-PROTEINS

被引：36

作者：

TORRESANI, J ^{[1
]}

ANSELMET, A ^{[1
]}

机构：

[1] FAC MED MARSEILLE,INSERM U38,MARSEILLE,FRANCE

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1978年 / 81卷 / 01期

关键词：

D O I：

10.1016/0006-291X(78)91642-X

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：

Nuclear high affinity triiodothyronine binding proteins from rat liver were purified about 500-fold over Triton-washed nuclei by a three-step procedure using gel filtration, DEAE-Sephadex and DNA-Sepharose chromatography. Although unstable, they retain most of the properties exhibited in crude nuclear extract: affinity and stereospecificity for T3, thermolability, molecular size. Furthermore, their isolation from several chromatin constituents under reducing conditions allows their study with decreased aggregation risks. © 1978.

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页码：147 / 153

页数：7

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