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作 者:郭淑华[1]
出 处:《安徽农业科学》2009年第8期3460-3462,共3页Journal of Anhui Agricultural Sciences
摘 要:[目的]为VP1蛋白的免疫学研究和鸡贫血病毒基因工程疫苗的研制奠定基础。[方法]将1个新克隆的鸡贫血病毒vp1基因(AF448446)在大肠杆菌DE3中进行表达,并对该蛋白进行纯化。[结果]结果表明:已成功构建了表达载体pET30(b+)v-p1;VP1蛋白已成功诱导表达并得以纯化;获得的VP1蛋白序列与已发表的VP1蛋白序列存在差异。[结论]试验克隆的vp1基因大小为1 347 bp,编码449个氨基酸的蛋白。[ Objective ] The research aimed to provide basis for the immunology study of VP1 protein and the production of genetically engineering vaccine of chicken anemia virus. [ Method] A new vpl gene (AF448446) was expressed in Escherichia coli DE3, and VP1 protein was purified then. [ Result]The results showed that pET30 (b^+ )-vp1 expression vector was constructed successfully. VP1 protein was expressed successfully and purified. The sequence of VPI protein was different with that had been published. [ Conclusion] vpl gene obtained was 1 347 bp, and coded 449 amino acid protein.
关 键 词:鸡贫血病毒(CAV) 衣壳蛋白基因 原核表达 纯化
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