Kanamori M, Ibuki F, Yamada M, Tashiro M, Miyoshi M
J Nutr Sci Vitaminol (Tokyo). 1975;21(6):429-36. doi: 10.3177/jnsv.21.429.
A proteinase inhibitor was isolated and partially purified from the exocarp of eggplant, Solanum melongena L., by means of acetate buffer extraction, heat treatment, salting-out and column chromatography on DEAE-cellulose. This preparation showed inhibitory activities on various proteinases; trypsin [EC 3.4.4.4] and Pronase were strongly inhibited while alpha-chymotrypsin [EC 3.4.4.5] and Nagarse were weakly inhibited. The inhibitor was a protein substance, and, therefore, it was gradually inactivated by the long-time incubation with Pronase. The inhibition mode was non-competitive on trypsin and competitive on Pronase on the basis of Lineweaver-Burk plots. The investigations on the inhibition behavior in the co-existence of two kinds of proteinases suggested that the inhibitor was not of multi-headed type.
通过乙酸盐缓冲液提取、热处理、盐析和DEAE-纤维素柱色谱法，从茄子（Solanum melongena L.）的外果皮中分离并部分纯化了一种蛋白酶抑制剂。该制剂对多种蛋白酶具有抑制活性；胰蛋白酶[EC 3.4.4.4]和链霉蛋白酶受到强烈抑制，而α-胰凝乳蛋白酶[EC 3.4.4.5]和纳加酶受到微弱抑制。该抑制剂是一种蛋白质物质，因此，与链霉蛋白酶长时间孵育会使其逐渐失活。根据Lineweaver-Burk图，其抑制模式对胰蛋白酶是非竞争性的，对链霉蛋白酶是竞争性的。对两种蛋白酶共存时抑制行为的研究表明，该抑制剂不是多头型的。
