结核分枝杆菌TB15.3蛋白的原核表达及纯化  

The prokaryotic expression and purification of TB15.3 protein of Mycobacterium tuberculosis

作　　者：刘元[1,2] 朱中元[1,2] 王海波[1,2] 

机构地区：[1]海南省农垦总医院,海南海口570311 [2]海南大学环境与植物保护学院,海南海口570000

出　　处：《中国热带医学》2011年第11期1301-1302,1322,共3页China Tropical Medicine

基　　金：海南省2008年度重点科技项目(No.080209)

摘　　要：目的通过原核表达及亲和层析技术,得到纯化的重组TB15.3蛋白。方法通过PCR从结核分枝杆菌H37Rv菌株的基因组中扩增出TB15.3蛋白的编码基因,再将其连接入PET-30a表达载体中,以E.coli BL21(DE3)菌株为宿主菌通过IPTG诱导表达,并通过亲和层析法纯化目的蛋白。结果通过IPTG诱导后得到目的蛋白,并且目的蛋白以可溶性蛋白形式表达。结论成功得到纯化的目的蛋白,为以后的实验奠定基础。Objective To evaluate the potential in serodiagnosis of TB by extraction of purified TB15.3 gene that cloned and expressed in Escherichia coli.Methods The gene coding TB15.3 protein was amplified by PCR from genome of Mycobacterium tuberculosis H37Rv,and then inserted into expression vector PET-30a and expressed recombinant TB15.3 protein in E.coli BL21（DE3）.The protein was purified by affinity chromatography.Results The target protein was expressed in E.coli after induction with IPTG.The solubility analysis showed that the recombinant protein was a soluble protein.Conclusion The recombinant TB15.3 protein plasmid was successfully constructed and the protein has successfully expressed and purified.

关 键 词：原核表达 TB15.3 蛋白 纯化 

分 类 号：R521[医药卫生—内科学]