The control of food mobilization in seeds of Cucumis sativus L.

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Abstract
An analysis of the in vitro activities of proteolytic enzymes from cotyledons of germinating cucumber seeds has been carried out and the effects of protein degradation products on such activities monitored. Aminopeptidase activity is substantially inhibited with either L-leucine or L-phenylalanine and trypsin activity with L-arginine. Aminopeptidase activity was also markedly reduced in the presence of individual di- and tripeptides. Of the peptides tested, however, only L-tryptophyl-L-phenylalanine inhibited the degradation of native cucumber seed protein by the endogenous cucumber seed protease(s) (autodigestive activity).