Biomaterial Database

Effect of heparin on the interaction between thrombin and hirudin. 1987

S R Stone, and J Hofsteenge

Friedrich Miescher-Institut, Basel, Switzerland.

The effect of heparin on the interaction between thrombin and hirudin has been examined by kinetic methods. Three forms of heparin fractionated on the basis of their affinity for antithrombin III and unfractionated heparin were found to act as noncompetitive inhibitors of the formation of the thrombin-hirudin complex. A three--four fold increase in the dissociation constant of the complex was observed at saturating heparin concentrations. This increase in the dissociation constant was due to a twofold decrease in the rate of association of thrombin and hirudin together with a similar increase in the rate of dissociation of the complex. Implications for the location of the heparin binding site on thrombin and the possible therapeutic use of the hirudin are discussed.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D008962	Models, Theoretical	Theoretical representations that simulate the behavior or activity of systems, processes, or phenomena. They include the use of mathematical equations, computers, and other electronic equipment.	Experimental Model,Experimental Models,Mathematical Model,Model, Experimental,Models (Theoretical),Models, Experimental,Models, Theoretic,Theoretical Study,Mathematical Models,Model (Theoretical),Model, Mathematical,Model, Theoretical,Models, Mathematical,Studies, Theoretical,Study, Theoretical,Theoretical Model,Theoretical Models,Theoretical Studies
D008970	Molecular Weight	The sum of the weight of all the atoms in a molecule.	Molecular Weights,Weight, Molecular,Weights, Molecular
D006493	Heparin	A highly acidic mucopolysaccharide formed of equal parts of sulfated D-glucosamine and D-glucuronic acid with sulfaminic bridges. The molecular weight ranges from six to twenty thousand. Heparin occurs in and is obtained from liver, lung, mast cells, etc., of vertebrates. Its function is unknown, but it is used to prevent blood clotting in vivo and vitro, in the form of many different salts.	Heparinic Acid,alpha-Heparin,Heparin Sodium,Liquaemin,Sodium Heparin,Unfractionated Heparin,Heparin, Sodium,Heparin, Unfractionated,alpha Heparin
D006629	Hirudins	Single-chain polypeptides of about 65 amino acids (7 kDa) from LEECHES that have a neutral hydrophobic N terminus, an acidic hydrophilic C terminus, and a compact, hydrophobic core region. Recombinant hirudins lack tyr-63 sulfation and are referred to as 'desulfato-hirudins'. They form a stable non-covalent complex with ALPHA-THROMBIN, thereby abolishing its ability to cleave FIBRINOGEN.	Hirudin
D000990	Antithrombin III	A plasma alpha 2 glycoprotein that accounts for the major antithrombin activity of normal plasma and also inhibits several other enzymes. It is a member of the serpin superfamily.	Heparin Cofactor I,Antithrombin III-Alpha,Atenativ,Heparin Co-Factor I,Kybernin,Serpin C1,Thrombate III,Antithrombin III Alpha,Antithrombin IIIAlpha,Cofactor I, Heparin,Heparin Co Factor I
D013917	Thrombin	An enzyme formed from PROTHROMBIN that converts FIBRINOGEN to FIBRIN.	Thrombase,Thrombin JMI,Thrombin-JMI,Thrombinar,Thrombostat,alpha-Thrombin,beta,gamma-Thrombin,beta-Thrombin,gamma-Thrombin,JMI, Thrombin