| Literature DB >> 10556651 |
S Uehara1, K Gotoh, H Handa, K Honjo, A Hirayama.
Abstract
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 the N-terminal (residues 26, 25, 16, 29, 20, 19, 14, 32, 7 and 6). The process of Glu carboxylation seemed to proceed three-dimensionally from inside to outside the molecule.Entities:
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Year: 1999 PMID： 10556651 DOI： 10.1016/s0009-8981(99)00152-7
Source DB: PubMed Journal: Clin Chim Acta ISSN： 0009-8981 Impact factor: 3.786