Dipeptidase development in cotyledons of Cucurbita maxima during germination

The dipeptidase activity of an unpurified soluble extract of the cotyledons of Cucurbita maxima Duch. var. Hubbard remained unchanged during the first 2 days of germination and then increased at a rapid rate during the next 3 days. The dipeptidase activity of two of three lots of seeds required the presence of the embryo axis for maximal dipeptidase activity, whereas the third lot was uninfluenced by the embryo axis. This discrepancy was possibly due to genetic differences. In those seeds which required the presence of the embryo axis for maximal dipeptidase activity, the cytokinin benzyladenine could replace the embryonic axis. When the protein synthesis inhibitor cycloheximide was added to the seeds at the beginning of germination, it inhibited dipeptidase activity of the cotyledons from 26 to 55 per cent, depending of the basis of calculation, at 5 days. When the cycloheximide was added to 3-day-old seedling the inhibition of dipeptidase activity in the cotyledons was almost immediate. The relative hydrolysis of -leucylglycine and glycylglycine were compared after temperature inactivation and purification; the results showed that more than one enzyme was responsible for the dipeptidase activity. The presence of a dialysable dipeptidase inhibitor(s) was demonstrated. Relatively high dipeptidase activity was also found in the roots and shoots.