大肠杆菌
包涵体
二硫键
化学
分离(微生物学)
蛋白质二硫键异构酶
包裹体(矿物)
生物化学
生物
微生物学
基因
矿物学
作者
Bernhard Fischer,Ian G. Sumner,Peter W. Goodenough
标识
DOI:10.1002/bit.260410103
摘要
Abstract Expression of recombinant proteins in Escherichia coli often 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 in E. coli as 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, Inc.
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