论文部分内容阅读
采用含hIL－12P35和P40两个亚基基因的重组质粒ρ2Bac－hIL－12ρ35ρ40与野生型林状病毒通过Lipofectin膜融合法进行同源重组，产生的重组杆状病毒感染培养的昆虫细胞Sf9和Sf21，进行重组蛋白的表达。用rhIL－12酶标试剂盒检测，证实rhIL－12的表达峰值约为5mg／L．SDS－PAGE显示2条重组蛋白条带．分子量约为87ku和40ku。PHA淋巴母细胞增殖试驻显示．重组蛋白对淋巴母细胞有一定的增殖能力，并对IL－2的增殖作用有相加性的增强效应。
The recombinant plasmid p2Bac-hIL-12p35p40 containing the two subunit genes hIL-12P35 and P40 was homologously recombined with the wild-type rhabdovirus by Lipofectin membrane fusion method. The recombinant baculovirus was used to infect the cultured insect cells Sf9 and Sf21 , The recombinant protein expression. Using rhIL-12 enzyme kit detection, the peak of rhIL-12 expression was confirmed to be about 5mg / L. SDS-PAGE showed two recombinant protein bands. The molecular weight is about 87ku and 40ku. PHA lymphoblast proliferation test station showed. Recombinant protein on lymphoblasts have a certain degree of proliferation, and proliferation of IL-2 additive additive effect.