Binding of heparin or dermatan sulfate to thrombin is essential for the sulfated polysaccharide-accelerated inhibition of thrombin by heparin cofactor II
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(87)81140-7/fullpdf
Reference17 articles.
1. Identification of two distinct heparin cofactors in human plasma
2. Detection of a new heparin-dependent inhibitor of thrombin in human plasma.
3. Heparin cofactor II. Purification and properties of a heparin-dependent inhibitor of thrombin in human plasma.
4. Antithrombin bm from human plasma: An antithrombin binding moderately to heparin
5. Reactive site peptide structural similarity between heparin cofactor II and antithrombin III.
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1. Blood compatibility of heparin-inspired, lactose containing, polyureas depends on the chemistry of the polymer backbone;Polymer Chemistry;2016
2. Highly sulfated dermatan sulfate from the skin of the ray Raja montagui: anticoagulant activity and mechanism of action;Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology;2010-07
3. Long Range Communication between Exosites 1 and 2 Modulates Thrombin Function;Journal of Biological Chemistry;2009-09
4. Mechanism of thrombin inhibition by heparin cofactor II and antithrombin in the presence of the ray (Raja radula) skin dermatan sulfate;Thrombosis Research;2009-04
5. Heparinkofaktor-II-Mangelerkrankungen: Pathophysiologie, Klinik, Diagnostik und Therapie;Hämostaseologie;1999
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