摘要
应用疏水层析对大肠杆菌表达的人重组白细胞介素－４（ｒｈＩＬ－４）进行了纯化，含有ｒｈＩＬ－４的包涵体，经洗涤、变性、复性后，以Ｂｕｔｙｌ－Ｓｅｐｈａｒｏｓｅ层析，得到了高纯度的ｒｈＩＬ－４．纯度达９７％；回收率为３２％；比活性为２×１０~７Ｕ／ｍｇ，讨论了ｒｈＩＬ－４疏水层析的条件，并对不同的方法纯化白细胞介素－４进行了比较．
A protocol of hydrophobic chromotography for purifying rhIL-4 expressed in E. coli was reported. After washing, denaturing and refolding the inclusion bodies separated from E. coli, the purity of the rhIL-4 obtained from this step was 97 %. The overall recovery of rhIL-4 was 32% and its specific activity was 2 ×10￣7 U/ mg.The consequence of phenyl-sepharose chromatography was showed and the optimal conditions and efficiency for purifying rhIL-4 by hydrophobic chromatography were discussed. Also compared hydrophobic protocol with other purification protocols.
关键词
重组
白细胞介素-4
疏水层析
制备
Recombinant human interleukin-4(rhIL-4), Hydrophobic chromatography, Purification of protein
