重组胸腺素α1的发酵、纯化及药效研究  

Fermentation,purification and drug efficacy study of recombinant thymosin alpha1

作　　者：刘中禄[1] 陶翠兰[1] 莘旭妮[2] 赵翠波[2] 李树民[2] 

机构地区：[1]第三军医大学大坪医院野战外科研究所实验动物中心,重庆400042 [2]解放军军事医学科学院军事兽医研究所,吉林长春130062

出　　处：《中国兽医学报》2013年第3期414-417,共4页Chinese Journal of Veterinary Science

基　　金：重庆市科技攻关计划资助项目(30111-14281)

摘　　要：为获得重组胸腺素α1(recombinant thymosinα1,Tα1),采用融合表达方式表达Tα1基因,重组融合表达载体Tα1/pMAL-C2x转化大肠杆菌TB1构建工程菌。对工程菌进行发酵并诱导表达,得到可溶性表达的目的蛋白。亲和层析纯化融合蛋白MBP-Tα1,经凝血酶裂解融合蛋白,Source Q离子交换,得到Tα1单体,最终目的蛋白纯度大于95%。应用犬细小病毒模型进行抗病毒药效学分析显示,重组Tα1具有抗病毒疗效,其药效与阳性药物日达仙相近。To obtain recombinant thymosin al（Tal）,we used the fusion expression system to ex- press Tal. E. coli TB1 was transformed with recombinant fusion exression vecter Tal/pMAL- C2x. We got soluble target fusion protein by engineering bacteria fermentation and induced ex- pression. The fusion protein MBP-Tal was purified by affinity chromotography and was cleavaged by thrombin,and Tal was purified by anion exchange chromatography Source Q. The purity of Tal is more than 95 %. The antivirus activity of Tal was proved in canine parvovirus model by drug effect analysis,and the drug effect of Tal is near to Zadaxin.

关 键 词：重组胸腺素α1 发酵 纯化 细小病毒 

分 类 号：S859.797[农业科学—临床兽医学]