【摘要】 目的 对解脲支原体（ＵＵ）血清３型ＭＢ抗原Ｎ端作蛋白的表达、纯化。方法 采用pGEX2T载体构建的重组质粒，用化学诱导剂 IPTG诱导表达，应用 Western斑点印迹法检测纯化融合蛋白的免疫学活性。结果 得到的ＵＵ ３型 ＭＢ抗原基因 ５’端重组克隆菌株，成功地诱导表达并纯化了 Ｎ端 ４３ＫＤ的融合蛋白，通过斑点印迹法证实该蛋白具有很好的免疫活性。结论 本实验成功地对解脲支原体血清３型ＭＢ抗原Ｎ端作了蛋白的表达与纯化，并证明具有很好的免疫活性。更多还原

【Abstract】 Objective Expression, purification and immunological assay of the peptide at the N-terminal of the MB antigen of ureaplasma urealyticum, serotype 3. Methods We cloned the appropriate cDNA into the expression vector pGEX-2T, induced the expression of this recombinant plasmid using IPTG, and identified the purified fusion protein and its immunological characteristics by western blot. Results We obtained a recombinant plasmid containing the 5’-end of MB antigen cDNA from UU, type 3, successfully expressed and purified this 43 kD fusion protein, and defined its good immunogenicity by western blot. Conclusion The N-terminal of the MB antigen of UU was successfully Expressed, Purified and proved to have good immunogenicity.更多还原