title: Decarboxylated bone Gla-protein as a substrate for hepatic vitamin K-dependent carboxylase.
abstract: 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 Km of this enzyme for d-B.G.P. is low, the latter is a better substrate than the frequently used pentapeptide FLEEL or exogenous protein substrates such as descarboxyprothrombin.
mesh_terms: D000645:Ammonium Sulfate / Q000494:pharmacology; D000818:Animals; D001842:Bone and Bones / Q000032:analysis; D002135:Calcium-Binding Proteins / Q000302:isolation & purification / Q000378:metabolism*; D019735:Carbon-Carbon Ligases; D002417:Cattle; D003653:Decarboxylation; D007700:Kinetics; D008025:Ligases / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D015675:Osteocalcin; D013379:Substrate Specificity
chemical_list: D002135:Calcium-Binding Proteins; D015675:Osteocalcin; D008025:Ligases; D019735:Carbon-Carbon Ligases; C020660:glutamyl carboxylase; D000645:Ammonium Sulfate