期刊名称：Journal of Nutritional Science and Vitaminology
印刷版ISSN：0301-4800
电子版ISSN：1881-7742
出版年度：1975
卷号：21
期号：6
页码：429-436
DOI：10.3177/jnsv.21.429
出版社：Center for Academic Publications Japan
摘要：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 DEAF-cellulose. This preparation showed inhibitory activities on various proteinases; trypsin [EC 3. 4. 4, 4] and Pronase were strongly inhibited while α-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.
