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 |