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- W2375287029 abstract "Objective:To establish a simple method to refold and purify the recombinant human granulocyte-macrophage colony stimulating factor(rhGM-CSF) expressed in Escherichia coli rapidly. Methods:Based on the refolding and purification mechanisms of rhGM-CSF in hydrophobic interaction chromatography (HIC),we investigated the stationary phase type and the mobile phase factors including salts,pH values,ratios of GSH / GSSG,and urea concentrations. Results:We chose PEG600 as the stationary phase and (NH4)2SO4 as the salt in mobile phase. The optimized conditions are pH7.0,addition of 2.0 mol / L urea,1.8 mmol / L GSH and 0.3 mmol / L GSSG into mobile phase. Under the optimal conditions,rhGM-CSF was renatured and purified simultaneously on HIC column. Its specific bioactivity,purity,and mass recovery reached 1.58× 107 U / mg,95.7% and 56.8% respectively. Conclusion:Using this craft,we got the purified rhGM-CSF with high specific bioactivity in one step. This craft has the advantages of simplicity and time-saving." @default.
- W2375287029 created "2016-06-24" @default.
- W2375287029 creator A5078269935 @default.
- W2375287029 date "2009-01-01" @default.
- W2375287029 modified "2023-09-25" @default.
- W2375287029 title "Refoding and Purification of Recombinant Human Granulocyte-Macrophage Colony Stimulating Factor with Hydrophobic Interaction Chromatography" @default.
- W2375287029 hasPublicationYear "2009" @default.
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