【摘要】 目的建立旋毛虫p49抗原基因原校表达产物的纯化方法。方法菌体经冻融、超声破菌及提取包涵体后，用离子交换和凝胶过滤层析纯化蛋白质。结果纯化后的融合蛋白P49／GST经SDS－PAGE电冰鉴定达电泳纯。双抗体夹心ELISA法检测结果表明纯化的P49／GST融合蛋白能与旋毛虫感染的鼠血清和纯化融合蛋白免疫的兔血清反应，而不与正常民和兔血清反应。结论纯化后的融合蛋白P49／GST具有较高的纯度及较强的免疫活性，可望作为旅毛虫病的免疫诊断抗原。更多还原

【Abstract】 Aim To establish a purification procedure for p49 antigen gene product of Trichinella spiralis expressed inEschedchia coli. Methods After centrifugation of the bacterial culture, the bacterial pellet was resuspended and lysed byfreezing-thawing treatment and ultrasonication. Ion exchanged and gel filtration chromatography were used to purify the fu-sion protein p49/GST from the inclusion bodies- Re8ultS The purity of the fusion protein p49/GST was verified using SDS-PAGE. The purified p49/GST protein could react with mouse antisera against Tricinella sPiralis and rabbit antisera againstpurified p49/GST protein, but not with normal mouse and rabbit sera by sandwich EL1SA. Concluslon The purified fusionprotein p49/GST with high purity and good immune activity could be used for the immune aasay of trichinellosis.更多还原