Refolding and Purification of the huGM-CSF(9-127)-IL-6(29-184) Fusion Protein
huGM-CSF(9-127)-IL-6(29-184)融合蛋白的复性及纯化研究

The huGM-CSF(9-127)-IL-6(29-184) fusion protein was precipitated on column when being purified by Q Sepharose H.P. ion exchange chromatography after renaturation by dilution. To solve this problem, a novel purification and refolding stra- tegy was adopted.Inclusion bodies was first purified by Q Sepharose H.P. ion exchange in 8mol/L urea,followed by in situ refolding on column by Sephacryl S-200. Renatured fusion protein was obtained in a purity of more than 95%.It was showed that the method of refolding on gel filtration column is efficient, with relative refolding rate at 80% .By the whole procedure,refolding and purification of recombinant protein can be performed within one day.This strategy is also promising to be applied in large scale puification and refolding of recombinant protein from inclusion bodies in E.coli.