聚乙二醇存在下的离子交换层析纯化重组人肿瘤坏死因子

Purification of Recombinant Human Tumor Necrosis Factor-αby Chromatography in the Presence of Polyethylene Glycol (PEG)

采用离子交换层析纯化了大肠杆菌表达的重组人肿瘤坏死因子（rhTNF－α），考察了PEG在离子交换层析中的作用，包括PEG分子量和浓度等的影响，初步探索了PEG和蛋白质相互作用机理。少量残余的杂蛋白继以疏水相互作用层析除去，获得了比活性为3．21×107u·mg-1的rhTNF－α，纯化倍数为253，总回收率为91．3％。

Ion-exchange chromatography (IEC) was used for purifying rhTNF-a from E.coli. Theimportant role of PEG acting on IEC was reported. The influence of PEG molecular weight,concentration and mechanism of PEG interaction with protein was discussed. The final specific activityof rhTNF-a reached 3.21×107U.mg-1 after one step IEC followed by a hydrophobic interactionchromatography. The purification factor was 253, and the total activity recovery was 91.3%.