Kanamori M, Ibuki F, Tashiro M, Yamada M, Miyoshi M
Biochim Biophys Acta. 1976 Aug 9;439(2):398-405. doi: 10.1016/0005-2795(76)90076-3.
A protein proteinase inhibitor was isolated and purified from eggplant exocarp by heat treatment, ammomium sulfate fractionation, column chromatography on DEAE-cellulose, and gel filtration on Sephadex G-25 and G-50. The final purified preparation of the inhibitor was found homogeneous by electrophoretic analysis. The inhibitor showed strong and stoichiometric inhibition on trypsin whereas it showed weak inhibition on alpha-chymotrypsin. It displayed no inhibiting characteristics on pepsin. The molecular weight of the inhibitor was estimated to be approximately 6000. This finding, with the trypsin inhibition data, suggested that the inhibitor combined trypsin in the molar ratio of 1:1. The amino acid analysis indicated that the inhibitor is rich in half-cystine, glycine and aspartic acid, and contains no tryptophan, histidine, methionine or valine.
通过热处理、硫酸铵分级分离、DEAE - 纤维素柱色谱以及Sephadex G - 25和G - 50凝胶过滤，从茄子外果皮中分离并纯化出一种蛋白质蛋白酶抑制剂。经电泳分析，最终纯化的抑制剂制剂呈现出均一性。该抑制剂对胰蛋白酶表现出强烈的化学计量抑制作用，而对α - 糜蛋白酶表现出较弱的抑制作用。它对胃蛋白酶没有抑制特性。抑制剂的分子量估计约为6000。这一发现与胰蛋白酶抑制数据表明，抑制剂与胰蛋白酶以1:1的摩尔比结合。氨基酸分析表明，该抑制剂富含半胱氨酸、甘氨酸和天冬氨酸，且不含色氨酸、组氨酸、甲硫氨酸或缬氨酸。
