Large-scale isolation of proteins of the large subunit from Escherichia coli ribosomes

被引：11

作者：

Diedrich, G ^{[1
]}

Burkhardt, N ^{[1
]}

Nierhaus, KH ^{[1
]}

机构：

[1] GKSS FORSCHUNGSZENTRUM GEESTHACHT GMBH, D-21502 GEESTHACHT, GERMANY

来源：

PROTEIN EXPRESSION AND PURIFICATION | 1997年 / 10卷 / 01期

关键词：

D O I：

10.1006/prep.1996.0702

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A strategy has been developed and optimized that allows the isolation of proteins of the large subunit from Escherichia coli ribosomes and combines the following advantages: speed, applicability for the isolation of milligram amounts of a single protein, and preservation of the biological activity of the proteins. The method consists of the following steps: ion-exchange chromatography on MonoS and MonoQ, gel filtration on Sephadex 75, and salt washes. Eleven proteins can be purified by a single chromatographic step, and a combination of two steps enables the isolation of the other proteins. (C) 1997 Academic Press.

引用

页码：42 / 50

页数：9

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