国家自然科学基金(39470785)及全军医学卫生青年基金(96Q078)资助.
为将人表皮生长因子(EGF)受体膜外第Ⅲ功能区(hEGF-RⅢ)表达于大肠杆菌菌膜上,重组构建了EGF-RⅢ表达载体,并转化获得大肠杆菌表达株.放射性受体分析发现125I-EGF可与表达菌特异性结合,其特异性结合量随反应的时间和温度而变化,Scatchard分析显示表达菌表达单一亲和性受体,其解离常数为3.0×10-11 mol/L,每个细菌约有738个结合位点.免疫电镜显示EGF-RⅢ多分布于细菌菌膜上.
An E.coli strain which could express domain Ⅲ of the extracellular region of the human EGF-R(EGF-RⅢ) in its membrane had been obtained. The results of EGF receptor radiobinding assay showed that 125I-EGF could bind specifically to the intact bacterial body, the amount of specific binding varied with the time and temperature of the reaction. The data of Scatchard analysis indicated that the number of the human EGF-RⅢ expressed in the bacteria was about 738 sites/cell, and its dissociation constant was about 3.0×10-11 mol/L. The sites of the bacteria to which EGF bound were discovered mainly on its membrane by immunoelectronmicroscopy.
王雨田,胡家露,高磊,陈苏民,杨胜利,龚毅,樊代明,张学庸.人表皮生长因子受体在大肠杆菌菌膜上功能性表达[J].生物化学与生物物理进展,1997,24(6):557-559
复制生物化学与生物物理进展 ® 2024 版权所有 ICP:京ICP备05023138号-1 京公网安备 11010502031771号