Ser^(125)突变型重组人白介素2的纯化研究

PURIFICATION OF Ser^(125) SITE-DIRECTED MUTAGENIC RECOMBINANT HUMAN INTERLEUKIN-2(RHIL-2)

对E．Coli表达的Ser125突变型白细胞介素2的纯化方式进行了研究。依次经包含体提取、SephacrylS200凝胶柱层析、复性、RP－HPLC、SephacrylS100凝胶柱层析，实验最终获得电泳纯度为一条带的、比活约为2.0×107IU／mg的rIL－2。结果表明采用建立的提地方法可稳定地获得较高纯度及比活性的突变型rIL－2。

A purification method of Ser125 site-directed recombinant human interleukin-2 (IL-2) which expressed in E.coli was studied. After preparation of inclusion talies, Sephacryl S200 gel filtration, refolding, revelse-phase HPLC and Sephacry S100 gel filtration were applied successively. The final purified Ser125 rhIL-2 showed a single band wtth SDS-PAGE electrophoresis, its specific bioactivity were ahaut 2. 0 ×10 7 IU/mg.