利用聚合脂质体的沉淀可逆性固定STI及其PL-STI对胰蛋白酶的亲和作用

Immobilization of STI on Polymerized Liposome by Inter Arm and Its Affinity Adsorption for Trypsin

通过双功能试剂戊二醛、二甘醇二酸酐和 1 ,4-丁二醇双缩水甘油醚等将大豆胰蛋白酶抑制剂 STI固定到由二十五 -1 0 ,1 2 -二块 -1 -醇磷脂乙醇胺形成的聚合脂质体上 .同时探讨了其作为亲和沉淀吸附剂对对胰蛋白酶的亲和作用 .在 PL沉淀过程中 ,胰蛋白酶有 2 0 %～ 60 %从 PL-STI上解离下来 .PL-STI可作为酶的亲和沉淀吸附剂 .

Soybean trypsin inhibitor(STI) was immobilized on polymerized liposome of pentacose-10,12-diene-1-ol-phospho ethanolamine by diglycolic anydride, glutaraldehyde and 1,4-butanediol diglycidyl ether. In the course of precipitation, 20% to 60% trypsin does cleavage from PL-STI and shows PL-STI can be used as the affinity precipitation adsorbent of enzyme.