dc.creatorABUIN,E
dc.creatorASPÉE,A
dc.creatorLISSI,E
dc.creatorLEÓN,L
dc.date2007-06-01
dc.date.accessioned2017-03-07T15:52:04Z
dc.date.available2017-03-07T15:52:04Z
dc.identifierhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-97072007000200017
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/392179
dc.descriptionThe 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
dc.formattext/html
dc.languageen
dc.publisherSociedad Chilena de Química
dc.sourceJournal of the Chilean Chemical Society v.52 n.2 2007
dc.subjectRose Bengal
dc.subjectbovine serum albumin
dc.titleBINDING OF ROSE BENGAL TO BOVINE SERUM ALBUMIN
dc.typeArtículos de revistas


Este ítem pertenece a la siguiente institución