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在大肠杆菌中融合高效表达人MCP-1
引用本文:张毅,叶棋浓,刘及,苏国富,滕家波. 在大肠杆菌中融合高效表达人MCP-1[J]. 吉林大学学报(医学版), 1999, 25(6): 685-687
作者姓名:张毅  叶棋浓  刘及  苏国富  滕家波
作者单位:1. 白求恩医大预防医学院毒理教研室,长春,130021
2. 军事医学科学院吉林大学学院所
3. 吉林大学医学院卫生部长春生物制品研究所
摘    要:目的:利用含强启动子的融合表达载体pGEX-2T对编码人单核细胞趋化蛋白-1(MCP-1)的基因进行高效表达。方法:基因重组技术及蛋白纯化技术。结果:SDS-PAGE显示表达产物占菌体蛋白的50% 。Western Blot检测表明,表达产物可与抗MCP-1 抗体特异反应。生物学活性测定结果表明,表达产物具有明显的单核细胞趋化活性。结论:融合蛋白对MCP-1 趋化活性无影响

关 键 词:人单核细胞趋化蛋白-1  高表达  趋化活性
修稿时间:1998-11-16

High level expression of MCP-1 in the form of fusion protein in E.coli
Zhang Yi,Ye Qinong,Liu Ji,Su Guofu,Teng Jiabo. High level expression of MCP-1 in the form of fusion protein in E.coli[J]. Journal of Jilin University: Med Ed, 1999, 25(6): 685-687
Authors:Zhang Yi  Ye Qinong  Liu Ji  Su Guofu  Teng Jiabo
Abstract:Objective:A new overexpression plasmid pGEX 2T/MCP 1 was constructed,in which a gene fragement encoding human monocyte chemoattractant protein 1 (MCP 1) was inserted downstream of tac promoter.Methods:DNA recombinant technique was used.Results:The expression level was 50% of total bacterial proteins by SDS PAGE.Western blot analysis showed that the expressed products 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.Conclusion:Fusion protein may not affect the chemoattractant activity of MCP 1.
Keywords:MCP-1  high expression  chemoattractant
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