Shibata H, Hara S, Ikenaka T
Department of Chemistry, Osaka University College of Science.
J Biochem. 1988 Oct;104(4):537-43. doi: 10.1093/oxfordjournals.jbchem.a122506.
The complete amino acid sequence of winged bean chymotrypsin inhibitor 3 (WCI-3) was determined by the conventional methods. WCI-3 consisted of 183 amino acid residues, but was heterogeneous in the carboxyl terminal region owing to the loss of one to four carboxyl terminal amino acid residues. The sequence of WCI-3 was highly homologous with those of soybean trypsin inhibitor Tia, winged bean trypsin inhibitor WTI-1, and Erythrina latissima trypsin inhibitor DE-3. One of the reactive site peptide bonds of WCI-3 was identified as Leu(65)-Ser(66), which was located at the same position as those of the other Kunitz-family leguminous proteinase inhibitors.
采用常规方法测定了四棱豆胰凝乳蛋白酶抑制剂3（WCI - 3）的完整氨基酸序列。WCI - 3由183个氨基酸残基组成，但由于羧基末端一至四个氨基酸残基的缺失，其羧基末端区域存在异质性。WCI - 3的序列与大豆胰蛋白酶抑制剂Tia、四棱豆胰蛋白酶抑制剂WTI - 1以及刺桐胰蛋白酶抑制剂DE - 3的序列高度同源。WCI - 3的一个活性位点肽键被鉴定为Leu(65)-Ser(66)，其位置与其他Kunitz家族豆科蛋白酶抑制剂的相同。
