Stopped-flow studies on drug-protein binding. 1. Kinetics of warfarin binding to human serum albumin.
Naunyn Schmiedebergs Arch Pharmacol
; 313(3): 269-74, 1980 Sep.
Article
en En
| MEDLINE
| ID: mdl-7432558
We have studied the binding of warfarin to human serum albumin (HSA) with the stopped-flow method. At 37 degrees C the rate constant for the velocity of dissociation of the stable warfarin-HSA complex is 10 S-1 (t50% = 0.07 s). Concentration and temperature dependent association constants for warfarin binding to HSA have been measured (2.5 x 10(5) M-1 S-1 at 6 degrees C, 9.8 x 10(5) M-1 S-1 at 22 degrees C and 15.3 x 10(5) M-1 S-1 at 37 degrees C). Our experimentally obtained relaxation constants are best explained by the existence of 5 equivalent low affinity binding sites for warfarin on the HSA molecule, each capable of conversion into a high affinity site. The measured energy of activation for this conversion is 57.5 kJ M-1.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Warfarina
/
Albúmina Sérica
Límite:
Humans
Idioma:
En
Revista:
Naunyn Schmiedebergs Arch Pharmacol
Año:
1980
Tipo del documento:
Article
Pais de publicación:
Alemania