REFOLDING AND RELEASE OF TUBULINS BY A FUNCTIONAL IMMOBILIZED GROEL COLUMN

被引：26

作者：

PHADTARE, S ^{[1
]}

FISHER, MT ^{[1
]}

YARBROUGH, LR ^{[1
]}

机构：

[1] UNIV KANSAS,MED CTR,DEPT BIOCHEM & MOLEC BIOL,KANSAS CITY,KS 66160

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1994年 / 1208卷 / 01期

关键词：

TUBULIN; REFOLDING; IMMUNOAFFINITY CHROMATOGRAPHY; GROEL; CHAPERONE PROTEIN;

D O I：

10.1016/0167-4838(94)90178-3

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：

Denatured tubulins form stable complexes with groEL upon dilution into refolding buffer. These complexes are retained on an immunoaffinity column which contains chemically immobilized antibodies to groEL. Tubulin remains bound to the immobilized groEL column after extensive washing and is released upon incubation with groES and ATP. Similar results were obtained with glutamine synthetase. These data suggest that groEL can function while it is attached to a solid support system.

引用

页码：189 / 192

页数：4

共 19 条

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