外源蛋白在大肠杆菌中的折叠  

Heterologous proteins folding in Escherichia coli

作　　者：康铁军[1] 袁旭东 俞炜源[1] 

机构地区：[1]军事医学科学院生物工程研究所,北京100071 [2]沈阳空军司令部门诊部,沈阳110015

出　　处：《军事医学科学院院刊》2002年第4期304-307,共4页Bulletin of the Academy of Military Medical Sciences

摘　　要：大肠杆菌是表达外源基因最常用的宿主之一。它结构简单 ,遗传背景清楚 ,基因表达调控机制相对明确。随着对分子伴侣和折叠酶研究的深入 ,蛋白在大肠杆菌内的折叠机制逐渐为人们所认识。Escherichia coli is one of the most widely used hosts for the production of heterologous proteins and its genetics is far better characterized than those of any other microorganism. The contribution of the chaperone systems and the folding catalysts to cellular protein folding has been clarified by a number of recent papers. Recent progress in the fundamental understanding of protein folding in E.coli , together with serendipitous discoveries of soluble expression of complex eukaryotic proteins are making this bacterium more valuable than ever.

关 键 词：外源蛋白 大肠杆菌 蛋白折叠 分子伴侣 二硫键 可溶性表达 

分 类 号：Q51[生物学—生物化学]