军事医学科学院院刊2001，Vol.25Issue(2)：129-132,4.
重组人胰岛素样生长因子Ⅰ的纯化及鉴定
Purification and identification of recombiant human IGF-Ⅰ
聂尚海 1刘宝英 1王芳 1刘农乐 1杜清友 1丁红梅 1王会信1
作者信息
摘要
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.关键词
重组人胰岛素样生长因子Ⅰ/纯化/复性/氨基酸序列分类
生物科学引用本文复制引用
聂尚海,刘宝英,王芳,刘农乐,杜清友,丁红梅,王会信..重组人胰岛素样生长因子Ⅰ的纯化及鉴定[J].军事医学科学院院刊,2001,25(2):129-132,4.
