Decarboxylated bone Gla-protein as a substrate for hepatic vitamin K-dependent carboxylase

FEBS Lett. 1984 Jan 2;165(1):16-20. doi: 10.1016/0014-5793(84)80005-8.


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

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ammonium Sulfate / pharmacology
  • Animals
  • Bone and Bones / analysis
  • Calcium-Binding Proteins / isolation & purification
  • Calcium-Binding Proteins / metabolism*
  • Carbon-Carbon Ligases*
  • Cattle
  • Decarboxylation
  • Kinetics
  • Ligases / metabolism*
  • Liver / enzymology*
  • Osteocalcin
  • Substrate Specificity


  • Calcium-Binding Proteins
  • Osteocalcin
  • Ligases
  • Carbon-Carbon Ligases
  • glutamyl carboxylase
  • Ammonium Sulfate