OVERPRODUCTION AND PURIFICATION OF SIGMA-32, THE ESCHERICHIA-COLI HEAT-SHOCK TRANSCRIPTION FACTOR

被引：40

作者：

NGUYEN, LH ^{[1
]}

JENSEN, DB ^{[1
]}

BURGESS, RR ^{[1
]}

机构：

[1] UNIV WISCONSIN,MCARDLE LAB CANC RES,MADISON,WI 53706

来源：

PROTEIN EXPRESSION AND PURIFICATION | 1993年 / 4卷 / 05期

关键词：

D O I：

10.1006/prep.1993.1056

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

This paper reports the overproduction and the details of a rapid method to purify active σ32 that is free of core RNA polymerase enzyme. Maximal overproduction of σ32 in a T7 RNA polymerase-based expression system is achieved only in the presence of rifampicin. This 2-day procedure involves solubilizing inclusion bodies in Sarkosyl, removal of Sarkosyl hy dialysis, and a single S-Sepharose column chromatography step. The final yield of σ32 is about 4.1 mg of approximately 95% purity from 1 g of wet weight cells. © 1993 Academic Press. All rights reserved.

引用

页码：425 / 433

页数：9

共 25 条

[1]

BURGESS RR, 1969, J BIOL CHEM, V244, P2168

[2] PHYSICAL INTERACTION BETWEEN HEAT-SHOCK PROTEINS DNAK, DNAJ, AND GRPE AND THE BACTERIAL HEAT-SHOCK TRANSCRIPTION FACTOR-SIGMA(32) [J].