摘要
为获得大量具天然抗原活性的恶性疟原虫HRP-Ⅱ抗原,用摇瓶发酵工程菌,诱导β-半乳糖苷酶-HRP-Ⅱ融合蛋白表达;裂菌后,洗涤沉淀2～3次,用6M脲溶解;取上清经Sephacryl-200柱层析分离纯化目的蛋白,然后复性。结果重组蛋白以包涵体的形式高效表达;Sephacryl-200柱层析后,目的蛋白纯度达86％,91.48％被复性,被Dipstick即 ParsSight-F识别,表明该重组抗原纯度高,复性效果好,可用于恶性疟原虫 HRP-Ⅱ抗体的制备等研究。
To obtain purified HRP- Ⅱ protein of plasmodium falciparun with natural antigenicity for further experiment. Methods: the cloned pWX146-HRⅡ in Escherchia coli was fermentated to induce the expression of IPTG. The lysates of the E. coli was chromotographed. Results: β-galactosidase-HRP-Ⅱ fusion protein was expressed in inclusion body. Purity of the chromotographed fusion protein is 86% . Ninety one percent of the fusion protein were renatuated and could be detected by the ParaSight-F Diagnostic Kit for Plasmodium falciparum . Conclusion: The HRP-Ⅱ fusion proteinpossesses antigenicity, and can be used in immundogical diagnosis.
出处
《广东寄生虫学会年报》
2000年第1期29-32,共4页
Journal of Tropical Medicine
基金
全军医药卫生基金资助项目(96L034)
