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鹅细小病毒vp1基因的原核表达及抗原性分析

Prokaryotic expression of vp1 gene of goose parvovirus and antigenicity analysis of the expressed protein

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【作者】 马波于天飞李俚布日额高明春王君伟

【Author】 MA Bo1,YU Tian-fei2,LI Li1,BU Ri-e3,GAO Ming-chun1,WANG Jun-wei1(1.Department of Preventive Veterinary Medicine,College of Veterinary Medicine,Northeast Agricultural University,Harbin 150030,China;2.College of Life Science and Engineering,Qiqihar University,Qiqihar 161006,China;3.College of Life Sciences,Inner Mongolia University for Nationalities,Tongliao 028043,China)

【机构】 东北农业大学动物医学院预防兽医系齐齐哈尔大学生命学院内蒙古民族大学生命科学学院

【摘要】 将鹅细小病毒(GPV)H1株vp1基因从pMD18T-vp1亚克隆至原核表达载体pGEX-6P-1的多克隆位点,构建了原核表达载体pGEX-6P-vp1,将其转化感受态细胞BL21(DE3)pLysS中,经IPTG诱导,SDS-PAGE分析,结果获得了108ku的融合蛋白,该融合蛋白经亲和层析纯化并经Western-blot检测。结果表明,纯化的融合蛋白可与GPV阳性血清发生特异性反应,具有良好的抗原性。

【Abstract】 A vp1 gene of goose parvovirus(GPV) H1 strain was cloned from the pMD18T-vp1 into the polycloning sites of pGEX-6P-1 vector.The recombinant prokaryotic expression plasmid was constructed,and named pGEX-6P-vp1.The recombinant plasmid was transformed into BL21(DE3) pLysS.The transformed bacteria were induced with IPTG and the expressed protein was analyzed by SDS-PAGE.The fusion protein of 108 ku was expressed.The protein purified by chromatography purification system could react with GPV positive serum specifically in a Western-blot test,indicating that the expressed protein had good antigenicity.

【基金】 黑龙江省教育厅重大科技项目(10541Z004);黑龙江省科技攻关项目(GB01B503-02,GB04B504)
  • 【文献出处】 中国兽医科学 ,Chinese Veterinary Science , 编辑部邮箱 ,2010年02期
  • 【分类号】S852.659.2
  • 【被引频次】6
  • 【下载频次】232
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