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Studies on Dipeptidase

The bulletin of the Yamaguchi Medical School Volume 11 Issue 4 Page 203-219
published_at 1964-12
A020011000403.pdf
[fulltext] 824 KB
Title
Studies on Dipeptidase
Creators Muramatu Mutumi
Creators Hirohata Ryozo
Source Identifiers
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.
Subjects
医学 ( Other)
Languages eng
Resource Type departmental bulletin paper
Publishers Yamaguchi University Graduate School of Medicine
Date Issued 1964-12
File Version Version of Record
Access Rights open access
Relations
[ISSN]0513-1812
[NCID]AA00594272
Schools 医学部