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血管抑素3A工程蛋白的柱复性与离子交换纯化
引用本文:肖克,陆兵,夏杰,徐殿胜.血管抑素3A工程蛋白的柱复性与离子交换纯化[J].华东理工大学学报(自然科学版),2006,32(1):43-46.
作者姓名:肖克  陆兵  夏杰  徐殿胜
作者单位:华东理工大学生物反应器工程国家重点实验室,上海,200237;华东理工大学生物反应器工程国家重点实验室,上海,200237;华东理工大学生物反应器工程国家重点实验室,上海,200237;华东理工大学生物反应器工程国家重点实验室,上海,200237
基金项目:上海市-SK研究与发展基金
摘    要:由大肠杆菌以包涵体形式表达的一种抗内皮细胞生长工程蛋白(A nti-ang iogen ic agent,简称3A)经变性,Sephacry l S-100 HR柱复性,SP Sepharose FF离子交换吸附纯化,SephadexG-25脱盐,获得复性率为53.47%,HPLC纯度为92.52%的3A活性蛋白。以猪髋动脉内皮细胞为受检细胞,表明纯化蛋白具有抑制内皮细胞生长的特性。

关 键 词:内皮细胞生长抑素  3A蛋白  柱复性  离子交换吸附
文章编号:1006-3080(2006)01-0043-04
收稿时间:2004-12-11
修稿时间:2004年12月11

Separation of Anti-Angiogenic Agent from Inclusion Bodies by Column Refolding and Ion Exchange Adsorption
XIAO Ke,LU Bing,XIA Jie,XU Dian-sheng.Separation of Anti-Angiogenic Agent from Inclusion Bodies by Column Refolding and Ion Exchange Adsorption[J].Journal of East China University of Science and Technology,2006,32(1):43-46.
Authors:XIAO Ke  LU Bing  XIA Jie  XU Dian-sheng
Abstract:The isolation and purification of anti-angiogenic agent(3A),a new functional fragment found in the tPA was studied.This process was started with the denaturation of anti-angiogenic agent protein expressed and accumulated in the the form of inclusion bodies in the cell of Escherichia coli.After column refolding using Sephacryl S-100 HR,SP Sepharose FF ion exchange adsorption,and Sephadex G-25 desalting,the active protein recovery and the purity of 3A determined by HPLC is(53.47%) and(92.52%)(respectively).It was confirmed that the product protein can inhibit the growth of endothelioid cell.
Keywords:angiostatin  3A protein  column refolding  ion exchange adsorption  
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