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用聚合酶链式反应（ＰＣＲ）从ＨＩＶ１ｇａｇ基因中扩增出衣壳蛋白Ｐ２４截短体（ｔＰ２４）基因，插入质粒ｐＧＥＸ４Ｔ３中构成重组表达质粒ｐＧＥＸｔｐ２４，将ｐＧＥＸｔｐ２４转化大肠杆菌ＢＬ２１后获得了高效表达，表达量占菌体总蛋白量的３４３８％。经Ｇｌｕｔａｔｈｉｏｎｅ－Ｓｅｐｈａｒｏｓｅ４Ｂ亲和层析纯化的截短体Ｐ２４纯度为９２７７％。纯化的截短体Ｐ２４在间接ＥＬＩＳＡ和免疫印迹检测ＨＩＶ抗体阳性血清和正常人血清中，具有很高的抗原特异性和免疫反应性。
The capsid protein P24 truncated (tP24) gene was amplified from HIV-1 gag by polymerase chain reaction (PCR) and inserted into the plasmid pGEX-4T3 to construct the recombinant expression plasmid pGEX-tp24. The pGEX-tp24 was transformed into the large intestine Bacillus BL21 was highly expressed, the expression amount accounted for 34 38% of total bacterial protein. The purity of truncated P24 purified by Glutathione-Sepharose 4B affinity chromatography was 9277%. The purified truncated P24 was highly antigen-specific and immunoreactive in both indirect ELISA and Western blot for the detection of HIV antibody-positive sera and normal human sera.