EXPRESSION IN ESCHERICHIA-COLI - PRODUCTION AND PURIFICATION OF BOTH SUBUNITS OF THE HUMAN GENERAL TRANSCRIPTION FACTOR TFIIE

被引：8

作者：

CHALUT, C ^{[1
]}

LANG, C ^{[1
]}

EGLY, JM ^{[1
]}

机构：

[1] FAC MED STRASBOURG,INST CHIM BIOL,CNRS,INSERM,UNITE BIOL MOLEC & GENIE GENET 184,F-67085 STRASBOURG,FRANCE

来源：

PROTEIN EXPRESSION AND PURIFICATION | 1994年 / 5卷 / 05期

关键词：

D O I：

10.1006/prep.1994.1065

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Both subunits of the human class II transcription factor TFIIE (rTFIIE alpha y and rTFIIE beta) have been overexpressed in Escherichia coli at 26 degrees C using a T7 RNA polymerase expression system and further purified to apparent homogeneity. As in this system rTFIIE alpha was poorly expressed and copurified with a truncated form, we expressed rTFIIE alpha as a fusion protein. These overexpressed subunits of TPILE, are similar to the endogenous subunits according to the following criteria: molecular weight, microsequencing, and transcription activity. (C) 1994 Academic Press, Inc.

引用

页码：458 / 467

页数：10

共 23 条

[1] METAL-AFFINITY SEPARATIONS - A NEW DIMENSION IN PROTEIN PROCESSING [J].