Purification and identification of recombiant human IGF-Ⅰ
- VernacularTitle:重组人胰岛素样生长因子Ⅰ的纯化及鉴定
- Author:
ShangHai NIE
;
Baoying, LIU
;
Fang, WANG
;
NongLe, LIU
;
Qingyou, DU
;
Hongmei, DING
;
Huixin, WANG
- Publication Type:Journal Article
- From:Bulletin of The Academy of Military Medical Sciences
2001;25(2):129-132
- CountryChina
- Language:Chinese
-
Abstract:
Objective:To obtain highly purified recombinant human IGF-Ⅰ(rhIGF-Ⅰ) and identify it.Methods:rhIGF-Ⅰ Was purified through ion-exchange chromatography and gel filtration chromatography after the inclusion bodies of rhIGF-Ⅰ were extracted from Escherichia coli. The recombinant protein was characterized through molecular weight assay, Western-blot, and fluorescent chromatography. The renaturation and biological assay of rhIGF-Ⅰ were investigated. Results and Conclusions: The purity of rhIGF-Ⅰ was higher than 99%. The analysis of molecular weight, Western-blot, fluorescent chromatography and sequences of NH2-terminal 15 amino acids were same as those anticipated. 3-10 mg/ml was the concentration of renatured rhIGF-Ⅰ to support half-maximal stimulation of cell proliferation with BALB/c 3T3 cells.
