A generic protein purification method for protein complex characterization and proteome exploration

被引：2102

作者：

Rigaut, G ^{[1
]}

Shevchenko, A ^{[1
]}

Rutz, B ^{[1
]}

Wilm, M ^{[1
]}

Mann, M ^{[1
]}

Séraphin, B ^{[1
]}

机构：

[1] European Mol Biol Lab, D-69117 Heidelberg, Germany

来源：

NATURE BIOTECHNOLOGY | 1999年 / 17卷 / 10期

关键词：

D O I：

10.1038/13732

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

We have developed a generic procedure to purify proteins expressed at their natural level under native conditions using a novel tandem affinity purification (TAP) tag. The TAP tag allows the rapid purification of complexes from a relatively small number of cells without prior knowledge of the complex composition, activity, or function. Combined with mass spectrometry, the TAP strategy allows for the identification of proteins interacting with a given target protein. The TAP method has been tested in yeast but should be applicable to other cells or organisms.

引用

页码：1030 / 1032

页数：3

共 16 条

[11] SM AND SM-LIKE PROTEINS BELONG TO A LARGE FAMILY - IDENTIFICATION OF PROTEINS OF THE U6 AS WELL AS THE U1, U2, U4 AND U5 SNRNPS [J].