蛋白质的排阻色谱复性的新进展  

Recent Developments of Protein Refolding by Size Exclusion Chromatography

作　　者：王超展[1] 耿信笃[1] 

机构地区：[1]西北大学现代分离科学研究所现代分离科学陕西省重点实验室,西安710069

出　　处：《中国生物工程杂志》2004年第7期45-49,共5页China Biotechnology

基　　金：国家自然科学基金资助项目 (2 0 175 0 16)

摘　　要：外源蛋白在大肠杆菌中高效表达时 ,常常形成不溶的、无活性的包涵体 ,包涵体蛋白的复性是重组蛋白生产过程中的一个技术难题。排阻色谱 (sizeexclusionchromatography ,SEC)用于蛋白复性是一种较新的、适用于任何一种蛋白的方法 ,与常用的稀释复性法相比 ,它能在高的起始蛋白浓度下对蛋白进行复性 ,活性回收率较高 ,同时又能使目标蛋白得到一定程度的纯化。对使用SEC复性的进展进行了评述 ,其内容包括SEC复性的原理及其复性过程中的影响因素 。High level expression of recombinant proteins in Escherichia coli often results in the formation of insoluble and inactive inclusion bodies,protein refolding from inclusion bodies is a puzzle in the production of recombinant proteins. Protein refolding by size exclusion chromatography (SEC) is a new and universal technology,which can refold many kinds of proteins of higher initial protein concentration,and has high bioactivity recovery compared with the common dilution method. The recent developments of protein refolding by SEC were reviewed.The mechanism of protein refolding by SEC,the factors affecting protein refolding,the future of this method were analyzed.

关 键 词：包涵体 重组蛋白 蛋白折叠 复性 排阻色谱 

分 类 号：Q51[生物学—生物化学]