Ibuki F, Yamada M, Tashiro M, Kanamori M
J Nutr Sci Vitaminol (Tokyo). 1977;23(2):133-43. doi: 10.3177/jnsv.23.133.
The trypsin inhibitor in eggplant, Solanum melongena L., was isolated and purified by the improved method with the techniques of dialysis using acetylated cellulose tube and ion-exchange chromatography on DEAE-Sephadex. The final preparation was found to be homogeneous by disc and SDS-polyacrylamide gel electrophoresis. This inhibitor had the molecular weight of about 6,200, the pI value of 4.7, and furthermore characteristic amino acid composition lacking in tryptophan, histidine, valine and methionine. The trypsin inhibition data indicated that the purified inhibitor combined with bovine trypsin [EC 3.4.21.4] in the molar ratio of 1:1. These properties of this inhibitor were in agreement with those of the dialyzable eggplant trypsin inhibitor previously purified, indicating that the dialyzable and non-dialyzable inhibitors in eggplant are identical.
采用改进方法，利用乙酰化纤维素管透析技术和DEAE - 葡聚糖离子交换色谱法，从茄子（Solanum melongena L.）中分离并纯化了胰蛋白酶抑制剂。通过圆盘电泳和SDS - 聚丙烯酰胺凝胶电泳发现最终制剂是均一的。该抑制剂的分子量约为6200，pI值为4.7，此外其特征性氨基酸组成中缺乏色氨酸、组氨酸、缬氨酸和甲硫氨酸。胰蛋白酶抑制数据表明，纯化后的抑制剂与牛胰蛋白酶[EC 3.4.21.4]以1:1的摩尔比结合。该抑制剂的这些特性与先前纯化的可透析茄子胰蛋白酶抑制剂的特性一致，表明茄子中的可透析和不可透析抑制剂是相同的。
