Binding of Fibrin Monomer and Heparin to Thrombin in a Ternary Complex Alters the Environment of the Thrombin Catalytic Site, Reduces Affinity for Hirudin, and Inhibits Cleavage of Fibrinogen
Open Access
- 1 October 1996
- journal article
- Published by Elsevier
- Vol. 271 (42) , 26088-26095
- https://doi.org/10.1074/jbc.271.42.26088
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- Thrombin inhibitors A new generation of antithromboticsTrends in Cardiovascular Medicine, 1995
- The clot thickens: clues provided by thrombin structureTrends in Biochemical Sciences, 1995
- Thrombin Functions and Antithrombotic InterventionThrombosis and Haemostasis, 1995
- The fibrinogen sequences that interact with thrombinBlood, 1993
- A player of many parts: The spotlight falls on thrombin's structureThrombosis Research, 1993
- The refined 1.9‐Å X‐ray crystal structure of d‐Phe‐Pro‐Arg chloromethylketone‐inhibited human α‐thrombin: Structure analysis, overall structure, electrostatic properties, detailed active‐site geometry, and structure‐function relationshipsProtein Science, 1992
- Characterization of the kinetic pathway for fibrin promotion of .alpha.-thrombin-catalyzed activation of plasma factor XIIIBiochemistry, 1991
- Anion-binding exosite of human .alpha.-thrombin and fibrin(ogen) recognitionBiochemistry, 1988
- Clotting of bovine fibrinogen. Kinetic analysis of the release of fibrinopeptides by thrombin and of the calcium uptake upon clotting at high fibrinogen concentrationsBiochemistry, 1988
- Regulation of the formation of factor XIIIa by its fibrin substratesBiochemistry, 1985