摘要
利用pUC 8为载体质粒,将合成的人Cu/Zn SOD基因置于Lac Z启动子的调控下,构建了含有该基因的表达质粒pCZS Ⅰ。首次成功地在大肠杆菌中表达了合成人Cu/Zn SOD的基因。SDS聚丙烯酰胺凝胶电泳薄层扫描分析证明,SOD基因的表达产物占细胞可溶性蛋白质的13％左右,用光扩增法捡测表达产物的酶活性,每毫克蛋白质为48.6 McCord Fridovich单位。
Expression of Human Cu/Zn Superoxide Dismutase was achieved in Esc-herichia coli by using pUC8 vector which contains a LacZ promoter and a β-lactamase ribosomosal binding site. The recombinant Human SOD represented about 13% of the total bacterial protein. Enzymatic activity is 48.6 McCord Fridovich as measured in crude bacterial lysates.This article offers the first description on the expression of synthetic Cu/Zn SOD gene in E. coii. The conditions for the expression were discussed.
出处
《基础医学与临床》
CSCD
1990年第4期23-26,共4页
Basic and Clinical Medicine
基金
国家高技术发展计划资助
关键词
人Cu/ZnSOD
基因工程
基因表达
human Cu/Zn superoxide dismutase gene cloning gene expression
