Isolation, renaturation, and formation of disulfide bonds of eukaryotic proteins expressed inEscherichia colias inclusion bodies
作者:
Bernhard Fischer,
Ian Sumner,
Peter Goodenough,
期刊:
Biotechnology and Bioengineering
(WILEY Available online 1993)
卷期:
Volume 41,
issue 1
页码: 3-13
ISSN:0006-3592
年代: 1993
DOI:10.1002/bit.260410103
出版商: Wiley Subscription Services, Inc., A Wiley Company
关键词: recombinant protein;Escherichia coli;inclusion body;renaturation;disulfide bond
数据来源: WILEY
摘要:
AbstractExpression of recombinant proteins inEscherichia colioften results in the formation of insoluble inclusion bodies, In case of expression of eukaryotic proteins containing cysteine, which may form disulfide bonds in the native active protein, often nonnative inter‐ and intramolecular disulfide bonds exist in the inclusion bodies. Hence, several methods have been developed to isolate recombinant eukaryotic polypeptides from inclusion bodies, and to generate native disulfide bonds, to get active proteins. This article summarizes the different steps and methods of isolation and renaturation of eukaryotic proteins containing disulfide bonds, which have been expressed inE. colias inclusion bodies, and shows which methods originally developed for studying the folding mechanism of naturally occurring proteins have been successfully adapted for reactivation of recombinant eukaryotic proteins. © 1993 John Wiley&Sons, I
点击下载:
PDF
(1101KB)
返 回