Studies on Dipeptidase

The hydrolytic activity of the acetone powder of hog intestinal mucosa and hog pancreas on four series of sipeptides, i. e. Gly-X, X-Gly, X-D, L-Val and X-D, L-Ileu, was examined at both low and high substrate concentrations. The hydrolytic activity of hog intestinal mucosa was much more active than that of pancreas. In particular, Gly-X was the most actively hydrolyzed dipeptide by acetone powder of intestinal mucosa, except Gly-Gly. Further, this enzyme was named glycine-amino-peptidase (GAPase). Although the purification of GAPase was tried with calcium phosphate gel, no remarkable results were obtained. GAPase requires a metal ion as co-factor, however, neither the definite netao ion nor an activation method have been found as yet.