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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Ammonium Sulfate / pharmacology
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Animals
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Bone and Bones / analysis
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Calcium-Binding Proteins / isolation & purification
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Calcium-Binding Proteins / metabolism*
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Carbon-Carbon Ligases*
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Cattle
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Decarboxylation
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Kinetics
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Ligases / metabolism*
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Liver / enzymology*
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Osteocalcin
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Substrate Specificity
Substances
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Calcium-Binding Proteins
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Osteocalcin
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Ligases
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Carbon-Carbon Ligases
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glutamyl carboxylase
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Ammonium Sulfate