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Survey of Rabbit Skeletal Muscle Peptidases Active at Neutral pH Regions
Author(s) -
OKITANI AKIHIRO,
OTSUKA YUZURU,
KATAKAI RYOICHI,
KONDO YASUHIRO,
KATO HIROMICHI
Publication year - 1981
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1981.tb14528.x
Subject(s) - aminopeptidase , skeletal muscle , dipeptidase , leucine , substrate (aquarium) , biochemistry , chemistry , tetrapeptide , oligopeptide , substrate specificity , enzyme , hydrolysis , rabbit (cipher) , peptide , biology , amino acid , anatomy , ecology , statistics , mathematics
A survey of oligopeptide hydrolases active at neutral pH regions responsible for increased free ammo acids on aging of high ultimate pH muscles were performed examining chromatographic behavior and substrate specificity of rabbit skeletal muscle extract. The DEAE‐cellulose chromatography of muscle extract revealed five major activity peaks respectively ascribable to a dipeptidase, an aminotripeptidase, an ammopeptidase, leucine aminopeptidase and the 160,000 dalton‐aminopeptidase purified previously by us. Since the 160,000 dahon‐ammopeptidase showed a broader substrate specificity than the two other aminopeptidases, it is most likely that this enzyme shares the largest part in the tetrapeptide hydrolysis in rabbit skeletal muscle at neutral pH regions.