Process of carboxylation of glutamic acid residues in the gla domain of human des-gamma-carboxyprothrombin.

@article{Uehara1999ProcessOC,
  title={Process of carboxylation of glutamic acid residues in the gla domain of human des-gamma-carboxyprothrombin.},
  author={Soichiro Uehara and Katuhiro Gotoh and Hiroshi Handa and Kaori Honjo and Aki Hirayama},
  journal={Clinica chimica acta; international journal of clinical chemistry},
  year={1999},
  volume={289 1-2},
  pages={33-44}
}
In the absence of vitamin K (VK) or in the presence of VK antagonists, hepatic VK-dependent carboxylase activity is inhibited and des-gamma-carboxyprothrombin (DCP) is released into the blood. We analyzed the number of glutamic acid (Glu) residues and their positions in the Gla domain (GD) of DCP to investigate the gamma-carboxylation mechanism of VK-dependent carboxylase. Several DCPs were found in each subject studied. The 10 Gla residues of human prothrombin were carboxylated in order from… CONTINUE READING