Larionova N I, Gladysheva I P, Tikhonova T V, Kazanskaia N F
Biokhimiia. 1993 Aug;58(9):1437-44.
A classical soybean inhibitor (Bowman-Birk inhibitor, BBI 2-IV) and two high molecular weight glycine-enriched inhibitors of the same type (3-II and 4-II) have been isolated, purified to homogeneity and characterized. All of the BBI isoforms have been found to effectively inhibit cathepsin G and human granulocyte elastase. The constants for leucocyte cathepsin G inhibition by classical BBI 2-IV (Ki = 1.2 x 10(-9) M) and high molecular mass BBI 3-II (Ki = 8.0 x 10(-8) M) as well as for leucocyte elastase inhibition by high molecular mass BBI 3-II (Ki = 1.1 x 10(-7) M) have been determined.
一种经典的大豆抑制剂（鲍曼-伯克抑制剂，BBI 2-IV）以及两种相同类型的高分子量富含甘氨酸的抑制剂（3-II和4-II）已被分离、纯化至同质并进行了表征。已发现所有BBI同工型均能有效抑制组织蛋白酶G和人粒细胞弹性蛋白酶。已测定经典BBI 2-IV（Ki = 1.2 x 10(-9) M）和高分子量BBI 3-II（Ki = 8.0 x 10(-8) M）对白细胞组织蛋白酶G的抑制常数，以及高分子量BBI 3-II（Ki = 1.1 x 10(-7) M）对白细胞弹性蛋白酶的抑制常数。
