【摘要】 目的:在原核中表达人卵透明带蛋白3(zone pelluc ida,ZP3)。方法:将人ZP3基因的核心片段克隆到原核表达载体pGEX-4T-1中。经酶切和序列分析后,用重组质粒转化大肠杆菌BL21,并经丙基β-D硫代半乳糖苷(IPTG)诱导产生GST-ZP3融合蛋白。结果:重组菌株明显诱导表达出预期分子质量为63 000 D的融合蛋白。结论:成功地构建GST-ZP3融合蛋白表达载体,并在大肠杆菌中表达GST-ZP3融合蛋白,为进一步开展免疫避孕与生殖免疫的研究奠定基础。更多还原

【Abstract】 Objective:To express zone pellucida3(zp3) in prokaryotic cells.Methods:The core fragment of zp3 gene was cloned into plasmid pGEX-4T-1 containing glutathiones transferase(GST) fusion protein gene.Following restriction enzyme digestion analysis and sequencing,pGEX-4T-1ZP3 was transformed into E.coli BL21.GST-ZP3 fusion protein was expressed under IPTG induction.Results:A 63 000 Dalton fusion protein was detected,as expected,was obtained evidently.Conclusion:A prokaryotic system capable of expressing GST-ZP3 fusion protein is successfully constructed.This will facilitate our study of the immunocontraception.更多还原