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以融合蛋白形式在大肠杆菌中表达人MCP-1
引用本文:叶棋浓,苏国富,徐永强,黄翠芬.以融合蛋白形式在大肠杆菌中表达人MCP-1[J].中国生物化学与分子生物学报,1995,11(2):146-149.
作者姓名:叶棋浓  苏国富  徐永强  黄翠芬
作者单位:军事医学科学院生物工程研究所
摘    要:将编码人单核细胞趋化蛋白-1(MCP-1)的基因亚克隆到大肠杆菌表达载体pEX31A中,在大肠杆菌中表达出MS2/MCP-1融合蛋0白,该表达产物约占菌体总蛋白的15%左右,Westernblot检测表明,表达产物可与MCP-1抗体特异反应。采用琼脂糖平板法进行活性测定表明,表达产物具有明显的单核细胞趋化活性,说明N端融合一段细菌蛋白对MCP-1有无趋化活性可能没有影响。

关 键 词:人单核细胞趋化蛋白-1  基因的克隆与表达  融合蛋白  
收稿时间:1995-04-20

Expression of MCP-1 in the Form of Fusion Protein in E.coli
Ye Qi-Nong,Su Guo-Fu,Xu Yong-Qiang,Huang Cui-Feng.Expression of MCP-1 in the Form of Fusion Protein in E.coli[J].Chinese Journal of Biochemistry and Molecular Biology,1995,11(2):146-149.
Authors:Ye Qi-Nong  Su Guo-Fu  Xu Yong-Qiang  Huang Cui-Feng
Institution:(Institute of Biotechnology, Beijing 100850
Abstract:A gene fragment encoding human monocyte chemoattratctant protein-1 (MCP-1) was subcloned into pEX31A. MS2/MCP-1 fusion protein was expressed in E. coli and accounted for about 15% of total cell proteins. Western blot analysis indicated that the expression product reacted specifically with anti-MCP-1 antibodies. Detection of activity by the method of agarose plates showed that the expression product had obvious monocyte chemoattractant activity, suggesting that bacterial protein at N-terminus may not affect the chemoattractant activity of MCP-1.
Keywords:Human monocyte chemoattractant protein-1  Gene cloning and expression  Fusion protein  
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