Serkhan V, Shcherbak I G
Vopr Med Khim. 1990 Nov-Dec;36(6):47-50.
Purified preparations of alpha 2-macroglobulin were preincubated with bovine trypsin at various molar ratios. Effects of the preincubation were measured before and after addition of soybean trypsin inhibitor in excess if N-benz-L-arg-p-nitroanilide was used as a substrate. Two types of interaction between alpha 2-macroglobulin and trypsin were detected. One of them was carried out depending on the "trap" hypothesis, another type of the interaction led to the enzyme loss of both proteolytic activity and its ability to hydrolyze the low molecular substrate. The data obtained suggest that various molecular forms of native alpha 2-macroglobulin were responsible for these types of interaction.
将纯化的α2-巨球蛋白制剂与牛胰蛋白酶以不同的摩尔比进行预孵育。如果使用N-苄基-L-精氨酸对硝基苯胺作为底物，在加入过量的大豆胰蛋白酶抑制剂之前和之后测量预孵育的效果。检测到α2-巨球蛋白与胰蛋白酶之间存在两种相互作用。其中一种相互作用是根据“陷阱”假说进行的，另一种相互作用导致该酶的蛋白水解活性及其水解低分子底物的能力丧失。所获得的数据表明，天然α2-巨球蛋白的各种分子形式是造成这些相互作用类型的原因。
