大肠杆菌表达的重组人肿瘤坏死因子的分离纯化

Separation and Purification of Recombinant Human Tumor Necrosis Factor-α Expressed in E. coli

目的 对表达在大肠杆菌里的重组人肿瘤坏死因子（ｒｈＴＮＦ－α）进行分离纯化。方法 采用疏水相互作用层析和离子交换层析。结果 考察了影响疏水相互作用导析纯化的因素，优化了层析操作条件；样品经疏水相互作用层析后，少量残余的杂蛋白可通过离子 交换层析除去。结论 获得了比活性为２．８９×１０＾７ｕ／ｍｇ的ｒｈＴＮＦ－α，总回收率为４０．６％。

Purpose: The purpose of this study is to purify recombinant human tumor necrosis factor-α expressed in E. coli. Methods: Hydrophobic interaction chromatography (HIC ) and ion exchange chromatography were performed for purification of rhTNF-a. Results: The conditions of hydrophobic interaction chromatography were investigated and optimized. Conclusion: The final specific activity of rhTNF-a reached 2. 89 X 10~7 u/mg after one step HIC followed by an ion exchange chromatography. The total recovery was 40. 6 %.