中文摘要：

目的对构建细粒棘球蚴（Echinococcus granulosus，Eg）延伸因子-1（Elongmionfactor1，EF-1）基因的重组质粒，并原核表达、纯化及对其免疫特性进行鉴定。方法从重组质粒EF-1／pGEM—T中酶切出EF-1目的片段，亚克隆入表达载体pET28a，转化人大肠杆菌E．coli BL21（DE3）plysS进行融合表达，经His—band树脂纯化试剂盒小量纯化，SDS—PAGE和Westernblot方法鉴定表达产物。结果成功构建Eg．EF-1／pET28a，／E．coliBL21基因工程菌株，诱导表达重组蛋白和纯化分离得到31KDaEg．EF-1均能被细粒棘球蚴天然抗原免疫的兔多克隆抗血清识别。结论初步证实该重组蛋白具有较好的抗原性。

英文摘要：

Objective To establish the expression plasmid Eg. EF - 17pET28a of Echinococcus granulosus and to express, purify Eg. EF - 1/6His fusion protein. Methods Eg. EF - 1/6His fusion protein Eg. EF - 1 gene was attained from Eg. EF - 1/pGEMT recombinant plamid and subcloned into expression vector pET28a, then transformed into E. coli BL21 （DE3） plysS to express the fusion protein induced by IPTG. The Eg. EF - 1/6His was purified by His - bind protein purification kit. Results The recombinant protein was immunoblotted with rabbit antisera immunized by protoscolices in western blot. Conclusion The recombinant protein Eg. EF - 1/ 6His has a good antigenicity.