标题:
包涵体溶解与复性的策略与方法Solubilization and Refolding of Inclusion Body Proteins Expressed in Bacterial Host
作者:
王苹, 井健
关键字:
包涵体, 蛋白质复性, 溶解, 蛋白质结构Inclusion Body; Solubilization; Protein Refolding; Structure; Biological Activtiy
期刊名称:
《Bioprocess》, Vol.2 No.4, 2012-12-28
摘要:
原核细胞表达外源基因常常会导致包涵体的产生。包涵体的复性是制备有效的功能蛋白质的必需途径。每一种蛋白质的基本结构与性质不同，决定了包涵体中外源蛋白质的复性方法多种多样。本文总结并介绍了目前在包涵体复性方面的几种方法与策略。初步讨论了在复性过程中蛋白质的结构变化。
Inclusion bodies produced in Escherichia coli are composed of densely packed denatured protein molecules in the form of particles. Refolding of inclusion body proteins into bioactive forms is cumbersome, results in poor re- covery and accounts for the major cost in production of recombinant proteins from E. coli. With new information available on the structure and function of protein aggregates in bacterial inclusion bodies, it has been possible to de- velop improved solubilization and refolding procedures for higher recovery of bioactive protein indexed at this paper.