包涵体蛋白体外复性的研究进展  

Advances inin vitro Refolding of Inclusion Body Proteins

作　　者：方敏[1] 黄华樑[1] 

机构地区：[1]中国科学院遗传研究所,北京100101

出　　处：《生物工程学报》2001年第6期608-612,共5页Chinese Journal of Biotechnology

基　　金：国家 8 63项目 ( 863 10 2 0 9 0 4 0 1)资助~~

摘　　要：外源基因在大肠杆菌中高水平表达时 ,通常会形成无活性的蛋白聚集体即包涵体。包涵体富含表达的重组蛋白 ,经分离、变性溶解后须再经过一个合适的复性过程实现变性蛋白的重折叠 ,才能够得到生物活性蛋白。近年来 ,发展了许多特异的策略和方法来从包涵体中复性重组蛋白。最近的进展包括固定化复性以及用一些低分子量的添加剂等来减少复性过程中蛋白质的聚集 ,提高活性蛋白的产率。Overexpression of recombinant proteins in \%E.coli\% often results in formation of insoluble, inactive inclusion bodies. These inclusion bodies, which contain the recombinant proteins in a highly enriched form, can be isolated by solid/liquid separation. After solubilization, active proteins can be generated through an appropriate refolding process. Within the last decade, specific strategies and methods have been developed for preparing active recombinant proteins from inclusion bodies. Recent developments in renaturation procedure include the inhibition of aggregation during refolding by the application of low molecular weight additives and matrix\|bound renaturation techniques.

关 键 词：重组蛋白 包涵体 重折叠 复性 二硫键形成 

分 类 号：Q51[生物学—生物化学]