文献类型：期刊文献

中文题名：血管抑素3A工程蛋白的柱复性与离子交换纯化

英文题名：Separation of Anti-Angiogenic Agent from Inclusion Bodies by Column Refolding and Ion Exchange Adsorption

作者：肖克[1];陆兵[1];夏杰[1];徐殿胜[1]

机构：[1]华东理工大学生物反应器工程国家重点实验室,上海200237

年份：2006

卷号：32

期号：1

起止页码：43

中文期刊名：华东理工大学学报（自然科学版）

外文期刊名：Journal of East China University of Science and Technology

收录：CSTPCD;;EI(收录号：2006089716000);Scopus;北大核心:【北大核心2004】；CSCD:【CSCD2011_2012】；

基金：上海-SK研究与发展基金资助项目(2002002-S)

语种：中文

中文关键词：内皮细胞生长抑素;3A蛋白;柱复性;离子交换吸附

外文关键词：angiostatin; 3A protein;column refolding; ion exchange adsorption

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。
The isolation and purification of anti-angiogenic agent （3A）, a new functional iragment 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 coll. 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.