Abstract Inclusion bodies are easily formed when recombinant proteins are expressed in E.coli system, and how to renature these inclusion bodies is now becoming the key problem in the genetic engineering. The protein refolding assisted by the molecular chaperone systems is promised to improve the protein renaturation efficiency. Some kinds of molecular chaperone systems and their functions as well were reviewed in this paper. Meantime, the mechanism and applications of molecular chaperone systems in the renaturation of proteins were presented. The artificial molecular chaperone systems were also briefly introduced.
Key words Molecular chaperone, Renaturation, Purification, Heat shock protein, GroE

分子伴侣及其在蛋白质复性中的应用**

张佳艺 关怡新 姚善泾^*
(浙江大学化学工程与生物工程学系 杭州 310027)

摘要 E.coli作为目前应用最为广泛的原核表达系统，在异体表达蛋白质的过程中容易形成无活性的包涵体。蛋白质复性，即如何高效地将无活性的包涵体转变成为有活性的蛋白质，已成为基因工程蛋白产业化的瓶颈。而利用分子伴侣的协助折叠特性进行的蛋白质复性技术正成为这一领域的研究热点。本文针对这一技术，综述了分子伴侣的功能和种类、各种分子伴侣体系的作用原理及在蛋白质复性中的应用情况，并简单介绍了人工分子伴侣。
关键词 分子伴侣 复性 纯化 热休克蛋白 GroE