【摘要】 目的:表达并纯化HLXN编码蛋白latexin。方法:用IPTG诱导含重组质粒HLXN-pQE30的E.coli M15表达latexin蛋白;HiTrapTMChelating层析柱纯化基因工程his6-latexin蛋白;SDS-PAGE检测目的蛋白纯度和相对分子质量;考马斯亮蓝法测定超滤液中蛋白浓度。结果:由HLXN表达产物制备和提纯得到了纯化his6-latexin蛋白;该蛋白的分子量为32kD;蛋白含量为2.67g/L。结论:HLXN编码蛋白latexin的成功表达与纯化为进一步研究探讨HLXN基因的生物学功能、与人类临床疾病的关系以及在临床的应用奠定了基础。更多还原

【Abstract】 Objective: To express and purify latexin protein,a carboxypeptidase A（CPA）inhibitor.Methods:Latexin protein was expressed in E.coli M15 which had HLXN-pQE30 plasmid.The his6-hLXN protein was purified by using HiTrap^TM Chelating affinity chromatography colum and identified;its molecular mass and concentration were determined by SDS-PAGE analysis and Coomassie blue staining method separately.Results: SDS-PAGE analysis demonstrated that the obtained protein was of high purity;Its relative molecular mass was 32 kDa and concentration was 2.67 g/L.Conclusion: Purified latexin has been prepared successfully which is useful to further study on the function of HLXN and the role of Latexinprotein as CPA inhibitor in clinic medicine.更多还原