Purification and Bioactivity of the Fusion Protein Human Interleukin-2/Human Serum Albumin

Abstract:

The purification of fusion protein of human interleukin-2 and human serum albumin(rhIL-2-HSA) that was expressed and secreted in fermentation broth with recombinent Pichia pastoris GS115/pPIH was reported in this paper.Highly purified rhIL-2-HSA was separated from fermentation supernatant by ultra filter,Blue Sepharose affinity chromatography,Octyl Sepharose hydrophobic chromatography,DEAE Sepharose ion exchange chromatography.The purified fusion protein showed one single band on SDS-PAGE.The purified fusion protein could react with antibodies to IL-2 and HSA in Western Blot analysis.CTLL-2/MTT cell proliferating assay showed that the special activity of rhIL-2-HSA was 1.147×107 IU/mg.