Studies on Dipeptidase
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概要
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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.
- Yamaguchi University Graduate School of Medicineの論文
Yamaguchi University Graduate School of Medicine | 論文
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