引用本文:
Jia Hua LIU, Chao Zhan WANG, Xin Du GENG. A New Protocol for Solubilization, Refolding and Purification of Recombinant Human Granulocyte Colony-stimulating Factor in Inclusion Bodies[J]. Chinese Chemical Letters,
2006, 17(6): 799-802.
Citation: Jia Hua LIU, Chao Zhan WANG, Xin Du GENG. A New Protocol for Solubilization, Refolding and Purification of Recombinant Human Granulocyte Colony-stimulating Factor in Inclusion Bodies[J]. Chinese Chemical Letters, 2006, 17(6): 799-802.
Citation: Jia Hua LIU, Chao Zhan WANG, Xin Du GENG. A New Protocol for Solubilization, Refolding and Purification of Recombinant Human Granulocyte Colony-stimulating Factor in Inclusion Bodies[J]. Chinese Chemical Letters, 2006, 17(6): 799-802.
A New Protocol for Solubilization, Refolding and Purification of Recombinant Human Granulocyte Colony-stimulating Factor in Inclusion Bodies
摘要:
Recombinant human granulocyte colony-stimulating factor (rhG-CSF) in inclusion bodies was solubilized by 8 mol/L urea solution and subsequently precipitated by acetone to improve its purity. After that, the precipitates were solubilized by sodium hydroxide solution containing 2 mol/L urea. Then the solubilized rhG-CSF was passed through a size exclusion chromatography for refolding and extensive purification, and further purified by a weak anion exchange chromatography. The purity and mass recovery of refolded rhG-CSF were 96.5% and 75.6%, respectively. The bioactivity was 8.4×107 IU/mg.
English
A New Protocol for Solubilization, Refolding and Purification of Recombinant Human Granulocyte Colony-stimulating Factor in Inclusion Bodies
Abstract:
Recombinant human granulocyte colony-stimulating factor (rhG-CSF) in inclusion bodies was solubilized by 8 mol/L urea solution and subsequently precipitated by acetone to improve its purity. After that, the precipitates were solubilized by sodium hydroxide solution containing 2 mol/L urea. Then the solubilized rhG-CSF was passed through a size exclusion chromatography for refolding and extensive purification, and further purified by a weak anion exchange chromatography. The purity and mass recovery of refolded rhG-CSF were 96.5% and 75.6%, respectively. The bioactivity was 8.4×107 IU/mg.
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