Abstract
The binding of rose bengal (RB) to bovine serum albumin (BSA) occurs with both the folded (atpH 7·4) and the unfolded (pH 12·7) forms of BSA. Absorption spectroscopy has revealed an identical red-shift of 15nm in λmax of RB in presence of BSA both atpH 7·4 and 12·7. The affinity constants (K) atpH 12·7 have been reduced only by 50% in magnitude from those atpH 7·4. These lead us to infer that neither disulphide loops nor buried residues are involved but that the binding of RB occurs at the sites near the surface of BSA. Moreover, the drastic alterations in the near-UV circular dichroism suggest tertiary structural changes induced by RB on binding to BSA. The conformational changes at the binding sites of BSA atpH 7·4 and the affinity of RB particularly towards the exposed residues in BSA atpH 12·7 are the significant factors in the binding of RB to BSA.
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