BINDING OF ROSE BENGAL TO BOVINE SERUM ALBUMIN

The association of Rose Bengal (RB) with bovine serum albumin (BSA) was investigated by absorbance spectroscopy. The binding constant was determined from the effect observed in the absorbance of RB at 548 nm upon addition of the protein according with the Benesi-Hildebrand treatment. Results were ob...

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Autores principales:	ABUIN,E, ASPÉE,A, LISSI,E, LEÓN,L
Lenguaje:	English
Publicado:	Sociedad Chilena de Química 2007
Materias:	Rose Bengal bovine serum albumin
Acceso en línea:	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-97072007000200017
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spelling	oai:scielo:S0717-970720070002000172007-09-13BINDING OF ROSE BENGAL TO BOVINE SERUM ALBUMINABUIN,EASPÉE,ALISSI,ELEÓN,L Rose Bengal bovine serum albumin The association of Rose Bengal (RB) with bovine serum albumin (BSA) was investigated by absorbance spectroscopy. The binding constant was determined from the effect observed in the absorbance of RB at 548 nm upon addition of the protein according with the Benesi-Hildebrand treatment. Results were obtained in phosphate buffer at pH = 7.0. The effect of the salinity of the buffer and the sensitivity of the binding constant to the presence of urea were also studied. The results obtained allow to conclude that the binding of RB to BSA is dominated by hydrophobic effectsinfo:eu-repo/semantics/openAccessSociedad Chilena de QuímicaJournal of the Chilean Chemical Society v.52 n.2 20072007-06-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-97072007000200017en10.4067/S0717-97072007000200017
institution	Scielo Chile
collection	Scielo Chile
language	English
topic	Rose Bengal bovine serum albumin
spellingShingle	Rose Bengal bovine serum albumin ABUIN,E ASPÉE,A LISSI,E LEÓN,L BINDING OF ROSE BENGAL TO BOVINE SERUM ALBUMIN
description	The association of Rose Bengal (RB) with bovine serum albumin (BSA) was investigated by absorbance spectroscopy. The binding constant was determined from the effect observed in the absorbance of RB at 548 nm upon addition of the protein according with the Benesi-Hildebrand treatment. Results were obtained in phosphate buffer at pH = 7.0. The effect of the salinity of the buffer and the sensitivity of the binding constant to the presence of urea were also studied. The results obtained allow to conclude that the binding of RB to BSA is dominated by hydrophobic effects
author	ABUIN,E ASPÉE,A LISSI,E LEÓN,L
author_facet	ABUIN,E ASPÉE,A LISSI,E LEÓN,L
author_sort	ABUIN,E
title	BINDING OF ROSE BENGAL TO BOVINE SERUM ALBUMIN
title_short	BINDING OF ROSE BENGAL TO BOVINE SERUM ALBUMIN
title_full	BINDING OF ROSE BENGAL TO BOVINE SERUM ALBUMIN
title_fullStr	BINDING OF ROSE BENGAL TO BOVINE SERUM ALBUMIN
title_full_unstemmed	BINDING OF ROSE BENGAL TO BOVINE SERUM ALBUMIN
title_sort	binding of rose bengal to bovine serum albumin
publisher	Sociedad Chilena de Química
publishDate	2007
url	http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-97072007000200017
work_keys_str_mv	AT abuine bindingofrosebengaltobovineserumalbumin AT aspeea bindingofrosebengaltobovineserumalbumin AT lissie bindingofrosebengaltobovineserumalbumin AT leonl bindingofrosebengaltobovineserumalbumin
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BINDING OF ROSE BENGAL TO BOVINE SERUM ALBUMIN

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