Refolding of Escherichia coli produced membrane protein inclusion bodies immobilised by nickel chelating chromatography

被引：148
|
作者：
Rogl, H
Kosemund, K
Kühlbrandt, W
Collinson, I
机构：
[1] Max Planck Inst Biophys, D-60528 Frankfurt, Germany
[2] Univ Mainz, Inst Allgemeine Bot, D-55099 Mainz, Germany
来源：
FEBS LETTERS | 1998年 / 432卷 / 1-2期
关键词：
inclusion body; refolding; light harvesting complex II; translocation pore; chloroplast;
D O I：
10.1016/S0014-5793(98)00825-4
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Two distinctly different membrane proteins, which produced inclusion bodies in Escherichia coli, have been refolded to reconstitute properties appropriate to their native counterparts. The method employed utilises nickel chelating chromatography, where the solubilised inclusion bodies bind, refold and elute, Our aims were to release a large pool of membrane protein for functional, mutational and crystallisation screening studies, It is hoped that the methods described here will have a general application for other membrane proteins which have formed inclusion bodies. (C) 1998 Federation of European Biochemical Societies.
引用
收藏
页码：21 / 26
页数：6
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