Abstract
The dipeptidase-free polypepti-dase splits d, 1-leucyl-glycyl-glycin into leucine and glycyl-glycine, and glycyl-glycyl-1-leucine into glysin and glycyl-leucine, i.e., the enzyme attacks the end with the free amino group. Leucyl-diglycyl-glycine is split into leucine and diglycylglycine; triglycyl glycine into glycine and the tripeptide. The tripeptide resulting from the hydrolysis of the leucyl-diglycylglycine is not attacked because of inhibition by leucine; but leucine has little effect on the hydrolysis of the tetra or dipep-tide. Substitution of the amino group destroys the affinity of the enzyme for the substrate.