Study of interaction between catechin and native and modified bovine serum albumin by physico-chemical methods.
Indian J Biochem Biophys
;
1989 Feb; 26(1): 14-8
Artículo
en Inglés
| IMSEAR
| ID: sea-28251
ABSTRACT
The interaction of native and modified bovine serum albumin (BSA) with catechin, a flavanoid having vitamin P activity, has been studied using equilibrium dialysis, pH-metric, viscosity and spectrophotometric methods. The order of reactivity of catechin binding to proteins was found to be esterified BSA greater than BSA greater than formylated BSA greater than acetylated BSA with log K values of 3.778, 3.879, 3.748 and 3.813 and free energy change equal to -5.11, -5.16, -5.07 and -5.15 kcal/mole, respectively.
Texto completo:
Disponible
Índice:
IMSEAR (Asia Sudoriental)
Asunto principal:
Unión Proteica
/
Espectrofotometría
/
Viscosidad
/
Albúmina Sérica Bovina
/
Cinética
/
Catequina
/
Diálisis
/
Concentración de Iones de Hidrógeno
Idioma:
Inglés
Revista:
Indian J Biochem Biophys
Año:
1989
Tipo del documento:
Artículo
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