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SARS病毒刺突蛋白片段在大肠杆菌中的表达和纯化
引用本文:方勇 张秀霞 王宣军 王志武 李洋 盛军. SARS病毒刺突蛋白片段在大肠杆菌中的表达和纯化[J]. 中国生物制品学杂志, 2005, 18(3): 215-217
作者姓名:方勇 张秀霞 王宣军 王志武 李洋 盛军
作者单位:[1]吉林大学生命科学学院,长春130012 [2]长春生物制品研究所,长春130062
摘    要:目的获得SARS病毒表面刺突蛋白片段。方法用PCR方法克隆SARSS2片段基因,并在大肠杆菌中进行表达。表达产物经SDSPAGE及Westernblot鉴定,阴离子交换层析纯化。结果SARS病毒S2片段基因在大肠杆菌中获得了高表达,表达量占总蛋白的50%以上;得到纯度大于90%的SARS蛋白样品。结论获得了能够应用于SARS疫苗研究的SARS蛋白样品。

关 键 词:SARS病毒  刺突蛋白  表达  纯化
修稿时间:2004-12-23

Expression of Spike Protein Fragment of SARS Virus in E. coli and Purification of Expressed Product
FANG Yong,ZHANG Xiu-xia,WANG Xuan-jun,et al. Expression of Spike Protein Fragment of SARS Virus in E. coli and Purification of Expressed Product[J]. Chinese Journal of Bilogicals, 2005, 18(3): 215-217
Authors:FANG Yong  ZHANG Xiu-xia  WANG Xuan-jun  et al
Abstract:Objective To obtain the spike protein fragment of SARS virus and use for the development of SARS vaccine.Methods The gene encoding S2 fragment of SARS virus was amplified by PCR and expressed in E.coli.The expressed product was identified by SDS-PAGE and Western blot and purified by DEAE-Sepharose FF ion exchange chromatography.Results The gene encoding S2 fragment of SARS virus was highly expressed in E.coli.The expressed product contained more than 50% of total somatic protein and reached a purity of more than 90% after purification.Conclusion The SARS virus protein for developing vaccine was obtained.
Keywords:SARS virus  Spike protein  Expression  Purification
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