Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9146733 | Clínica e Investigación en Arteriosclerosis | 2005 | 10 Pages |
Abstract
In vitro glycation of lysine and arginine residues located in the heparin-binding site of antithrombin significantly reduces its anticoagulant activity. Interestingly, heparin, aminoguanidine and catechin prevented this effect. However, the non-enzymatic glycation of antithrombin in diabetic patients seems to be mild, since the action of glucose is very slow and the half life of antithrombin in plasma is short.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Physiology
Authors
H. Cano, D. Hernández-Espinosa, A. Miñano, M.L. del Rey, F. Illán, M.S. Alcaraz, M. Pascual, J.A. Guerrero, V. Vicente, J. Corral,