Title : Effect of temperature on the association step in thrombin-fibrinogen interaction.

Pub. Date : 1993 Sep 1

PMID : 8373370






3 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 In addition, the values of Km for thrombin-fibrinogen reaction were measured at different solution viscosities in order to derive the equilibrium dissociation constant, Ks, of this interaction. Potassium coagulation factor II, thrombin Homo sapiens
2 These experiments showed that the Ks values for thrombin-fibrinogen binding was equal to 1.8 microM at 25 degrees C. Altogether these results indicated that fibrinogen, though interacting with both the catalytic pocket and the fibrinogen recognition site on the thrombin molecule, dissociates from Michaelis complex with a rate comparable with that shown by amide substrates, which interact only with the catalytic site. Potassium coagulation factor II, thrombin Homo sapiens
3 These experiments showed that the Ks values for thrombin-fibrinogen binding was equal to 1.8 microM at 25 degrees C. Altogether these results indicated that fibrinogen, though interacting with both the catalytic pocket and the fibrinogen recognition site on the thrombin molecule, dissociates from Michaelis complex with a rate comparable with that shown by amide substrates, which interact only with the catalytic site. Potassium coagulation factor II, thrombin Homo sapiens