Refolding with Simultaneous Purification of Recombinant Human Granulocyte Colony-stimulating Factor from Escherichia coli Using Strong Anion Exchange Chromatography  

作　　者：ChaoZhanWANG JiangFengLIU XinDuGENG 

机构地区：[1]InstituteofModernSeparationScience,KeyLaboratoryofSeparationScienceinShanxiProvince,NorthwestUniversity,Xi＇an710069 [3]InstituteofModernSeparationScience,KeyLaboratoryofSeparationScienceinShanxiProvince,NorthwestUniversity,Xi＇an710069

出　　处：《Chinese Chemical Letters》2005年第3期389-392,共4页中国化学快报（英文版）

基　　金：This work is supported by the National Natural Science Foundation of China(No．20175016)

摘　　要：The urea denatured recombinant human granulocyte colony-stimulating factor (rhG- CSF) which was expressed in Escheriachia coli (E. coli) was refolded with simultaneous purification by strong anion exchange chromatography (SAX) in the presence of low concentration- of urea. The effect of urea concentration on this refolding process was investigated. The obtained refolded rhG-CSF has a high specific activity of 2.3×108 U/mg, demonstrating that the proteins were completely refolded during the chromatographic process. With only one step by SAX in 40 min, purity and mass recovery of the refolded and purified rhG-CSF were 97% and 43%, respectively.

关 键 词：Recombinant human granulocyte colony-stimulating factor inclusion bodies protein refolding PURIFICATION strong anion exchange chromatography. 

分 类 号：R378.21[医药卫生—病原生物学]