摘要
将含禽流感病毒M2蛋白膜外区(M2e)且偶联了鸡IgG Fc片段的重组质粒pET32a(+)的大肠杆菌,用终浓度为0.5 mmol/LIPTG在37℃下诱导表达,获得了包涵体表达的目的蛋白。Western-blotting试验表明,M2e能与兔抗禽流感H5阳性血清发生反应,且在47kD处出现一条特异性条带,具有良好的免疫学活性.表达产物通过His-Ni2+柱亲和层析后,得到了较好的纯化效果。本实验为进一步研究M2蛋白的生物学活性、检测方法及通用疫苗的开发奠定了基础。
The purpose protein of inclusion body expression is obtained by conducting inducible expression on plasmid pErlB2a of E. coli BL21, which contains avian influenza virus matrix2 protein eetodomain segments （ M2e ） and couples avian IgG Fc segment, under the condition of IPTG of 0. 5mmol/L at 37℃. Western-blotting demonstrates that M2e, which can react with the rabbit anti-AIV H5 positive serum, and produces a special band in the 47kD area, and possesses good antigenicity. The fusion protein is purified by His-Ni2 ＋ affinity chromatography and good purification result is obtained. This paper lays a foundation for the further research of M2 protein immunological characteristics and the development of universal vaccines and detection methods.
出处
《重庆理工大学学报（自然科学）》
CAS
2010年第1期38-41,共4页
Journal of Chongqing University of Technology：Natural Science
