摘要
利用 PCR扩增乙型脑炎病毒 E蛋白基因 5′端片段 ,克隆入原核表达载体 p ET-2 8a,转化大肠杆菌 BL2 1 ( ED3 )。经 IPTG诱导表达后 ,SDS-PAGE分析表达产物。结果表明 ,所表达的E蛋白片段的分子量约为 3 .4万 ,表达量约占菌体总蛋白的 3 5%。 JEV E蛋白片段在大肠杆菌中的成功表达 ,为制备 JE实验室诊断抗原和分析
In order to express N-terminal fragment of Japanese encephalitis virus E protein in Escherichia coli, the gene of the truncated Japanese encephalitis virus E protein was amplified by using PCR, and cloned into plasmid pET-28a. The constructed plasmid was transformed into E.coli BL21 (DE3). The recombinant transformants were induced by IPTG for expression. The protein expressed was analyzed by SDS-PAGE. Results showed that the protein was produced at a yield of 35% total bacteria protein and sized about 34 000. We make conclusion that the Japanese encephalitis virus E protein is expressed successfully in E.coli, which should be useful for the production of diagnostic antigen and the analysis of gene structure/function correlation of the E protein.
出处
《动物医学进展》
CSCD
2003年第4期108-109,共2页
Progress In Veterinary Medicine
