AFFINITY PURIFICATION OF HISTIDINE-TAGGED PROTEINS TRANSIENTLY PRODUCED IN HELA-CELLS

被引：37

作者：

JANKNECHT, R ^{[1
]}

NORDHEIM, A ^{[1
]}

机构：

[1] HANNOVER MED SCH,INST MOLEK BIOL,KONSTANTY GUTSCHOW STR 8,W-3000 HANNOVER 61,GERMANY

来源：

GENE | 1992年 / 121卷 / 02期

关键词：

TRANSFECTION; EUKARYOTIC EXPRESSION VECTOR; METAL CHELATE AFFINITY CHROMATOGRAPHY; HUMAN ELK-1 PROTEIN; SERUM-RESPONSE FACTOR; DNA-PROTEIN INTERACTION;

D O I：

10.1016/0378-1119(92)90137-E

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

In order to produce eukaryotic proteins in a functional state, it is often necessary to use eukaryotic instead of prokaryotic expression systems. We have designed vectors which can be employed to express either N- or C-terminally histidine-tagged proteins in transiently transfected eukaryotic cells. The histidine tag allows the rapid enrichment of these proteins by metal chelate affinity chromatography in a native and functional state. Yields of up to 5 mug protein/5 X 10(7) cells were achieved.

引用

页码：321 / 324

页数：4

共 12 条

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