绿豆胰蛋白酶抑制剂属于Bowman Birk类抑制剂,MW约8000,有7对二硫键,其一级结构已经测定。它有两个活性区域,活性中心分别为Lys-Set及Arg-Ser,可以以1:2或1:1的克分子比和胰蛋白酶络合。经胃蛋白酶降解后的两个活性片段也已分离提纯。这一切为开展X-射线晶体结构测定提供了有利条件。在以往对绿豆抑制剂及其酶复合物能形成晶体 Mung bean trypsin inhibitor belongs to the class of Bowman Birk inhibitor with a MW of about 8000 and seven pairs of disulfide bonds. Its primary structure has been determined. It has two active regions, active centers are Lys-Set and Arg-Ser, respectively, and can be 1: 2 or 1: 1 molar ratio and trypsin complex. The two active fragments degraded by pepsin have also been isolated and purified. All these provide favorable conditions for the determination of X-ray crystal structure. In the past of mung bean inhibitors and enzyme complexes to form crystals