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基因工程血管抑素3A蛋白的分离纯化
引用本文:尹芳,陈国豪,陆兵,刘叶青,徐殿胜.基因工程血管抑素3A蛋白的分离纯化[J].华东理工大学学报(自然科学版),2004,30(4):465-469.
作者姓名:尹芳  陈国豪  陆兵  刘叶青  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,生物工程系,上海,200237
基金项目:上海-SK研究与发展基金资助项目(2002002-S)。
摘    要:在8mol/mL尿素溶液中,以二硫苏糖醇(DTT)为还原剂,对基因工程血管抑素3A包涵体进行溶解实验。结果发现:1.5h后溶解的上清液蛋白浓度达26.2mg/mL。SDS-PAGE电泳扫描结果显示,3A蛋白经过Sephadex G75分离后PAGE电泳纯达到100%,该步收率达85.82%,相对分子质量为10ku。采用分步稀释法对其进行复性,所获复性3A蛋白经MTT法检测表明:3A蛋白浓度为0.1μg/mL时,对内皮细胞的生长抑制率为93.4%。

关 键 词:3A蛋白  包涵体  复性  分离纯化
文章编号:1006-3080(2004)04-0465-05
修稿时间:2003年8月24日

Purification of Recombinant Protein 3A
Abstract:The inclusion bodies of 3A were dissolved in 8 mol/mL urea buffer, and dithiothreitol(DTT) was added as reducing agent. Result showed that after one and a half hour, the concentration of soluble protein was (26.2) mg/mL.Being separated by sephadex G75 gel filtration chromatography, the recovery and purity of protein 3A determined by SDS-PAGE were 85.82% and 100% respectively, and its molecular weight was 10 ku. By multi-step dilution, the protein 3A was refolded, and the inhibition rates measured by MTT was 93.4%.
Keywords:protein 3A  inclusion body  refolding  purification
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