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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。
Objective To establish a purification method of the primary expression product of p49 antigen of Trichinella spiralis. Methods After the cells were freeze-thawed, sonicated and the inclusion bodies were extracted, the proteins were purified by ion exchange and gel filtration chromatography. Results The purified fusion protein P49 / GST was purified by SDS-PAGE electroblotting. The results of double antibody sandwich ELISA showed that the purified P49 / GST fusion protein reacted with rabbit serum immunized with Trichinella infected serum and purified fusion protein without reacting with normal human and rabbit serum. Conclusion The purified fusion protein P49 / GST has high purity and strong immunogenicity and is expected to be used as an immunodiagnostic antigen of Trichinella.