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Several properties of the partially purified proteinase inhibitor in eggplant exocarp.
- Source :
-
Journal of nutritional science and vitaminology [J Nutr Sci Vitaminol (Tokyo)] 1975; Vol. 21 (6), pp. 429-36. - Publication Year :
- 1975
-
Abstract
- 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.
- Subjects :
- Chymotrypsin antagonists & inhibitors
Enzyme Inhibitors isolation & purification
Enzyme Inhibitors pharmacology
Plants analysis
Pronase antagonists & inhibitors
Structure-Activity Relationship
Subtilisins antagonists & inhibitors
Trypsin Inhibitors isolation & purification
Trypsin Inhibitors pharmacology
Vegetables analysis
Protease Inhibitors
Subjects
Details
- Language :
- English
- ISSN :
- 0301-4800
- Volume :
- 21
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Journal of nutritional science and vitaminology
- Publication Type :
- Academic Journal
- Accession number :
- 1225945
- Full Text :
- https://doi.org/10.3177/jnsv.21.429