Studies on Dipeptidase

Studies on Dipeptidase

Creators Muramatu Mutumi

Creators Hirohata Ryozo

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.

[ISSN]0513-1812

[NCID]AA00594272