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Updated: Jul 10, 2026
Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
[Refolding and purification of recombinant human granulocyte colony-stimulating factor from Escherichia coli by using
Chaozhan Wang1, Lili Wang, Xindu Geng
1Key Laboratory of Separation Science in Shaanxi Province, Institute of Modern Separation Science, Department of Chemistry, Northwest University, Xi' an 710069, China. czwang@nwu.edu.cn
Abstract:
Recombinant human granulocyte colony-stimulating factor (rhG-CSF) in the form of inclusion bodies expressed in Escherichia coli (E. coli) was simultaneously refolded and purified using protein folding liquid chromatography (PFLC). Cu2+ -iminodiacetic acid (IDA) Sepharose was selected as the stationary phase for immobilized metal ion affinity chromatography. rhG-CSF was purified and the aggregates were diminished under a linear gradient elution of imidazole in the presence of a suitable concentration of urea. Using only one PFLC run, the refolded rhG-CSF had a specific bioactivity of 1.8 x 10(8) IU/mg and a purity of 97%, with the mass recovery of 32%.
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