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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.

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