源于大肠杆菌蛋白的表达、液相色谱复性与纯化新进展

Abstract

The development of the expression, renaturation and purification of proteins sourcing E. coli by protein folding liquid chromatography (PFLC) in past two years was briefly reviewed. PFLC has been widely employed for the separation and purification of inclusion body proteins. Besides the separation of the target protein from impure proteins, it has a character that the inclusion body proteins can be simultaneous renaturation. The preparative method of the most novel proteins employed in the modern biotechnology is generally carried out by liquid chromatography. Moreover, PFLC is more flexible for accomplishing the purification of protein producing from E. coli. When PFLC is used for enlarging protein purification to large scale, the expense of producing proteins may be greatly decreased. The review paper includes the expression of the target proteins, the sample pre-treatment of inclusion bodies, the wide range of applications. It also contains the process optimization, new technology, new methods, new equipments, and the molecular mechanism during PFLC process, some examples, and PFLC in future.