Citation: Chao Zhan WANG, Jiang Feng LIU, Xin Du GENG. Refolding with Simultaneous Purification of Recombinant Human Granulocyte Colony-stimulating Factor from Escherichia coli Using Strong Anion Exchange Chromatography[J]. Chinese Chemical Letters, ;2005, 16(3): 389-392. shu

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

Institute of Modern Separation Science, Key Laboratory of Separation Science in Shanxi Province, Northwest University, Xi'an 710069

Received Date: 1 March 2004

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

The urea denatured recombinant human granulocyte colony-stimulating factor (rhGCSF) 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.
- Recombinant human granulocyte colony-stimulating factor,
- inclusion bodies,
- protein refolding,
- purification,
- strong anion exchange chromatography.
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