Fluorimetric probes of the individual and competitive binding of 1-anilinonaphthalene-8-sulfonate, eosine and fluorescene to bovine serum albumin.
Indian J Biochem Biophys
;
1994 Apr; 31(2): 109-14
Artículo
en Inglés
| IMSEAR
| ID: sea-28329
ABSTRACT
Fluorescence of 1-anilinonaphthalene-8-sulfonate (ANS) is greatly enhanced on its binding to bovine serum albumin (BSA). Fluorimetric titration shows that three ANS molecules bind per BSA molecule. The enhanced fluorescence of BSA-ANS is quenched by eosine (EOS); and one EOS physically displaces one ANS bound to BSA. The enhanced fluorescence of free ANS in the hydrophobic environment of the nonionic surfactant Triton X 100 is also quenched by EOS but by an energy transfer mechanism. The dye fluorescene (FLSN) also quenches the fluorescence of BSA-bound ANS, but by the energy transfer mechanism. The binding region of ANS in BSA has been speculated.
Texto completo:
Disponible
Índice:
IMSEAR (Asia Sudoriental)
Asunto principal:
Espectrometría de Fluorescencia
/
Unión Competitiva
/
Albúmina Sérica Bovina
/
Cinética
/
Eosina Amarillenta-(YS)
/
Fluoresceínas
/
Colorantes Fluorescentes
/
Naftalenosulfonatos de Anilina
Idioma:
Inglés
Revista:
Indian J Biochem Biophys
Año:
1994
Tipo del documento:
Artículo
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