Odani S, Ono T, Ikenaka T
J Biochem. 1980 Aug;88(2):297-391. doi: 10.1093/oxfordjournals.jbchem.a132974.
Two silktree (Albizzia julibrissin) seed proteinase inhibitors, A-II and B-II, which are homologs with soybean trypsin inhibitor (Kunitz), were cleaved with cyanogen bromide. Sequence analyses of the resulting fragments and comparison with the soybean inhibitor revealed the amino acid sequences around the reactive sites of both inhibitors. The primary reactive site of trypsin-chymotrypsin inhibitor A-II was identified as Arg66-Ile67 and that for chymotrypsin-elastase inhibitor B-II as Leu62-Met63. These results are the first reports of the reactive site sequences of homologous of soybean trypsin inhibitor (Kunitz).
两种合欢（Albizzia julibrissin）种子蛋白酶抑制剂A-II和B-II，它们是大豆胰蛋白酶抑制剂（Kunitz）的同源物，用溴化氰进行了切割。对所得片段进行序列分析，并与大豆抑制剂进行比较，揭示了两种抑制剂活性位点周围的氨基酸序列。胰蛋白酶-糜蛋白酶抑制剂A-II的主要活性位点被确定为Arg66-Ile67，糜蛋白酶-弹性蛋白酶抑制剂B-II的主要活性位点被确定为Leu62-Met63。这些结果是关于大豆胰蛋白酶抑制剂（Kunitz）同源物活性位点序列的首次报道。
