A stoichiometric analysis of bovine serum albumin-gossypol interactions: a fluorescence quenching study.
Indian J Biochem Biophys
;
1992 Apr; 29(2): 179-82
Artículo
en Inglés
| IMSEAR
| ID: sea-29126
ABSTRACT
The interaction of gossypol with bovine serum albumin, human serum albumin and n-bromosuccinimide-modified bovine serum albumin has been followed by fluorescence quenching measurements. The presence of a high affinity site (association constant K = 2.2 x 10(6) M-1) for gossypol on bovine serum albumin and human serum albumin is indicated. The stoichiometry of binding for the high affinity site was evaluated using Job's method of continuous variation, thereby suggesting the formation of 11 complex. Modification of the tryptophan residues on bovine serum albumin does not affect the binding of gossypol to either high or low affinity site of albumin.
Texto completo:
Disponible
Índice:
IMSEAR (Asia Sudoriental)
Asunto principal:
Conformación Proteica
/
Espectrometría de Fluorescencia
/
Humanos
/
Albúmina Sérica
/
Albúmina Sérica Bovina
/
Gosipol
/
Cinética
Idioma:
Inglés
Revista:
Indian J Biochem Biophys
Año:
1992
Tipo del documento:
Artículo
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