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Decarboxylated bone Gla‐protein as a substrate for hepatic vitamin K‐dependent carboxylase
Author(s) -
Vermeer Cees,
Soute Berry A.M.,
Hendrix Hans,
de Boer-van den Berg Marian A.G.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80005-8
Subject(s) - pyruvate carboxylase , chemistry , substrate (aquarium) , biochemistry , osteocalcin , endocrinology , enzyme , biology , alkaline phosphatase , ecology
Bovine bone Gla‐protein (B.G.P.) was prepared and decarboxylated into descarboxy‐B.G.P. (d‐B.G.P.). The latter was purified and identified as decarboxylated osteocalcin. Both crude and purified d‐B.G.P. are good substrates for vitamin K‐dependent carboxylase. Because the K m of this enzyme for d‐B.G.P. is low, the latter is a better substrate than the frequently used pentapeptide F L E E L or exogenous protein substrates such as descarboxyprothrombin.