Abstract

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