重组恶性疟原虫乳酸脱氢酶的纯化及免疫活性测定  

Studies on Purification and Immunocompetence Characterization of Plasmodium falciparum Lactzte Dehydrogenase

作　　者：李莉[1] 宁云山[1] 吴英松[1] 李明[1] 

机构地区：[1]广州第一军医大学热带卫生学系热带病研究所,广州510515

出　　处：《热带医学杂志》2004年第1期22-24,52,共4页Journal of Tropical Medicine

基　　金：广州市科技计划项目(No.2002E3-E4012)

摘　　要：目的 研究恶性疟原虫乳酸脱氢酶(LDH)重组蛋白纯化和复性的最佳条件。方法 重组质粒PGEX-4T-1-LDH在E.coli BL21中表达,表达产物用酶裂解法洗涤、变性、复性、Q-Sepharose High Performance离子交换层析方法纯化。结果 获得具有生物活性的蛋白,其纯度达到95％。结论 此方法操作简便,纯化效果好。Objective To study the optimal condition for the purification and renaturation of Plasmodium falciparum lactzte dehydrogenase recombinant protein. Methods The recombinant gene PGEX-4T-1-LDH was expressed in E. coli BL21. The transformed bacteria were lysed by lysozyme so that the enclosed inclusion bodies were released. After the washing, denaturing and renaturing, the expression product was purified by Q-Sepharose High Performance ion-exchange chromatography. Results The purified product manifested biological activity with purity of up to 95%. Conclusions The procedure employed in this experiment is easy to handle and the purification efficiency is ideal.

关 键 词：恶性疟原虫 乳酸脱氢酶 蛋白纯化 

分 类 号：R382.31[医药卫生—医学寄生虫学]