Shibata H, Hara S, Ikenaka T, Abe J
J Biochem. 1986 Apr;99(4):1147-55. doi: 10.1093/oxfordjournals.jbchem.a135578.
Seven proteinase inhibitors were isolated from winged bean seeds by ion-exchange chromatographies. These inhibitors had molecular weights of around 20,000, included four half-cystine residues, and were Kunitz-type inhibitors. Two (WTI-2 and 3) inhibited bovine trypsin strongly and four (WCI-1, 2, 3, and 4) inhibited bovine alpha-chymotrypsin, but in different ways. One mole of WCI-2 or -3 could inhibit 2 mol of alpha-chymotrypsin. The remaining inhibitor (WTCI-1) could bind both bovine trypsin and alpha-chymotrypsin at the molar ratio of 1:1, but not simultaneously. All four chymotrypsin inhibitors cross-reacted with rabbit anti-WCI-3 serum, while the other inhibitors did not.
通过离子交换色谱法从四棱豆种子中分离出七种蛋白酶抑制剂。这些抑制剂的分子量约为20,000，含有四个半胱氨酸残基，属于库尼茨型抑制剂。其中两种（WTI-2和3）对牛胰蛋白酶有强烈抑制作用，四种（WCI-1、2、3和4）对牛α-糜蛋白酶有抑制作用，但作用方式不同。一摩尔的WCI-2或-3可以抑制两摩尔的α-糜蛋白酶。其余的抑制剂（WTCI-1）可以以1:1的摩尔比结合牛胰蛋白酶和α-糜蛋白酶，但不能同时结合。所有四种糜蛋白酶抑制剂都能与兔抗WCI-3血清发生交叉反应，而其他抑制剂则不能。
