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Characterization of the interaction between reserpine and bovine serum albumin: Spectroscopic approaches.
Indian J Biochem Biophys ; 2011 Dec; 48(6): 388-394
Artículo en Inglés | IMSEAR | ID: sea-140205
ABSTRACT
The characteristics of the interaction between reserpine and bovine serum albumin (BSA) were studied by fluorescence, UV-vis absorption and Fourier transform infrared (FT-IR) spectroscopy. Spectroscopic analysis revealed that fluorescence quenching of BSA by reserpine was through a static quenching procedure. The binding constant KA of reserpine with BSA at 293, 301 and 309 K was 1.63, 1.78 and 2.35 × 105 moL-1 L respectively, which indicated degree of binding force between reserpine and BSA. There was one binding site between reserpine and BSA. The entropy and enthalpy changes were positive, indicating that interaction of reserpine and BSA was driven mainly by hydrophobic forces. The average binding distance between the donor (BSA) and the acceptor (reserpine) was about 3.84 nm based on the Förster non-radiation energy transfer theory. Results of synchronous fluorescence and FT-IR spectra indicated that the conformation and microenvironment of BSA were changed by the binding of reserpine. The results may provide important insights into the physiological activity of reserpine.
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Texto completo: Disponible Índice: IMSEAR (Asia Sudoriental) Asunto principal: Reserpina / Espectrometría de Fluorescencia / Albúmina Sérica Bovina / Bovinos / Espectroscopía Infrarroja por Transformada de Fourier / Animales Idioma: Inglés Revista: Indian J Biochem Biophys Año: 2011 Tipo del documento: Artículo

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Texto completo: Disponible Índice: IMSEAR (Asia Sudoriental) Asunto principal: Reserpina / Espectrometría de Fluorescencia / Albúmina Sérica Bovina / Bovinos / Espectroscopía Infrarroja por Transformada de Fourier / Animales Idioma: Inglés Revista: Indian J Biochem Biophys Año: 2011 Tipo del documento: Artículo