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疏水层析纯化人重组白细胞介素-4
引用本文:戴燕,李燕,刘洁,王宏,陈慰峰. 疏水层析纯化人重组白细胞介素-4[J]. 中国生物化学与分子生物学报, 1996, 12(1): 83-87
作者姓名:戴燕  李燕  刘洁  王宏  陈慰峰
作者单位:北京医科大学免疫室
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.

关 键 词:人重组白细胞介素-4  疏水层析  蛋白质纯化  
收稿时间:1996-02-20

Purification of rhIL-4 by Hydrophobic Chromatography
Dai Yan,Li Yan,Liu Jie,Wang Hong,Chen Wei-Feng. Purification of rhIL-4 by Hydrophobic Chromatography[J]. Chinese Journal of Biochemistry and Molecular Biology, 1996, 12(1): 83-87
Authors:Dai Yan  Li Yan  Liu Jie  Wang Hong  Chen Wei-Feng
Affiliation:(Department of Immunology, Beijing Medical Unicersity, Beijing 100083
Abstract:
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.
Keywords:Recombinant human interleukin-4(rhIL-4)   Hydrophobic chromatography   Purification of protein  
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