Inhibiteurs anti-trypsine et activités protéolytiques des Albumines de graine deVigna unguiculata

✍ Scribed by A. Royer; M. N. Miège; A. Grange; J. Miège; J. M. Mascherpa

• Book ID: 104752218
• Publisher: Springer-Verlag
• Year: 1974
• Tongue: English
• Weight: 885 KB
• Volume: 119
• Category: Article
• ISSN: 0032-0935
• DOI: 10.1007/bf00390817

✦ Synopsis

The presence of trypsin inhibitors is demonstrated in cotyledonary albumins of Vigna unguiculata by cross-electrophoresis against trypsin and by kinetic measurements. These inhibitors are isolated by selective trapping on insoluble trypsin. On the other hand, evidence is given showing that cotyledonary albumins hydrolyse α-N-benzoyl-DL-arginine-p-nitroanilide (BAPA) and casein. Purified trypsin-inhibitors partially inhibit the caseolytic activity of albumins but do not influence their hydrolytic activity toward BAPA. A partial characterisation of proteases and inhibitors is carried out. A model for the regulation of the proteolytic activities of the seeds by trypsin inhibitors is suggested.