Thrombosis and Haemostasis · 1960 · 15 citations · 0 references
Life SciencesBiochemistryMolecular BiologyEnzyme MechanismEnzymologyHemostasisCoagulation PhysiologyEnzyme InactivationEnzyme InhibitionEnzyme KineticsEnzyme StabilitySubstrate BindingAntithrombin FunctionAntithrombin RegulationMichaelis-menten AnalysisProthrombin ActivationThrombin Inhibition
Summary In the interaction of thrombin (Th) and antithrombin (A) the activity of both is temporarily neutralized. Later thrombin activity regenerates and antithrombin is altered (P). Thrombin inactivates antithrombin. The experiments are interpreted on the basis of the Michaelis-Menton concept: The ThA complex is quite stable and tends to form rapidly when the concentration of A is relatively high. Dissociation and formation of inactive antithrombin (P) is favored with relatively high concentrations of thrombin.