Effect of temperature on dynamic viscoelasticity during the clotting reaction of fibrin.
The dynamic rigidity and loss moduli for fibrinogen-thrombin solution were determined during clotting in the temperature range between 15 and 45 degrees C. The rigidity of fibrin gel decreased with increasing clotting temperature, owing to the dissociation of cross-links. The rate constant of the dissociation of cross-links increased with increasing temperature. The rate constant of the cross-linking reaction increased and then decreased through a maximum with increasing temperature. It is explained by assuming that denaturation of fibrin occurs at high temperature. The irreversible denaturation becomes appreciable at high ionic strength. The activation energy and the enthalpy change for the cross-linking reaction of fibrin is about 35 and 15 kcal/mol, respectively. The enthalpy change for the reversible denaturation is about 46 kcal/mol.
D000818:Animals; D001777:Blood Coagulation; D002417:Cattle; D004548:Elasticity; D004789:Enzyme Activation; D005337:Fibrin / Q000378:metabolism; D005340:Fibrinogen / Q000378:metabolism*; D007700:Kinetics; D009994:Osmolar Concentration; D011489:Protein Denaturation; D013696:Temperature; D013816:Thermodynamics; D013917:Thrombin / Q000378:metabolism*; D014783:Viscosity
D005337:Fibrin; D005340:Fibrinogen; D013917:Thrombin