摘要
将鳗鲡疱疹病毒(AngHV)福建株(AngHV-FJ)ORF51基因克隆至原核表达载体pGEX-4T-2中,构建表达质粒pGEX-4T-2-ORF51,将其转化至表达菌株E.coli BL21(DE3)中,IPTG诱导后,收集表达菌体,进行SDS-PAGE分析和免疫印迹试验验证,结果表明,获得了高效表达的AngHV-FJ ORF51融合蛋白.经割胶回收纯化,获得高纯度的融合表达蛋白.用纯化的表达蛋白免疫新西兰大白兔,获得了高效价的兔抗ORF51多克隆抗体.这为进一步研究ORF51蛋白的结构和功能及开展AngHV病的防治研究提供了重要的研究基础.
AngHV-FJ ORFS1 gene was inserted in prokaryofie expression vector pGEX-4T-2 to construct expression plasmid pGEX- 4T-2-ORFS1, and then the plasmid was transformed into E. coli BI21 （DE3）, and induced by IPTG. SDS-PAGE and Western blot analysis confirmed that AngHV-FJ ORFS1 protein was highly expressed in E. coli BI21 （DE3）. The expressed ORFS1 protein was obtained by gel extraction purification, and used to immunize rabbit, and high titer rabbit anti-ORFS1 polyelonal antibody was ob- tained. The results provided fundamental data and materials for the farther study on the structure and function of ORFS1 protein and AngHV prevention.
出处
《福建农林大学学报（自然科学版）》
CSCD
北大核心
2014年第5期490-494,共5页
Journal of Fujian Agriculture and Forestry University:Natural Science Edition
基金
国家自然科学基金资助项目(31101933)
福建省自然科学基金资助项目(2014J01133)
人社部留学人员科技活动择优资助优秀类项目(2013)
福建省公益类科研院所专项(2009R10035-6)
