【摘要】 目的表达纯化重组人Jo-1抗原,免疫印迹和ELISA检测其免疫特异性。方法IPTG诱导含有Jo-1基因的重组菌,获得高表达的可溶性融合蛋白(MBP-Jo-1),亲和层析纯化该表达蛋白,免疫印迹和ELISA分别检测其抗原性并与生化提取的Jo-1抗原比对。结果表达的重组Jo-1蛋白具有Jo-1抗原的特异性。结论重组Jo-1蛋白与天然Jo- 1抗原具有相同的免疫原性和免疫原特异性。更多还原

【Abstract】 Objective To express and purify secombinant human Jo - 1 antigens and chect it’s activity and specificity of immunology. Methods The MBP - Jo - 1 fusion proteins expressed from recombinant pMAL - c - Jo -1 induced by IPTG were purfied by affinity chromatography using amyoose resin, and checked for its activity and specificity by ELISA. Results: The recombinant Jo - 1 antigens had the same specificity as natural Jo - 1 antigen. Conclusion The fusion Jo - 1 polypetide had the immune-identity with natural Jo - 1 antigen.更多还原