Denaturation of bovine serum albumin initiated by sodium dodecyl sulfate as monitored via the intrinsic fluorescence of the protein

Abstract

The tryptophan fluorescence of bovine serum albumin (BSA) is used to study the denaturation transitions in BSA under the influence of sodium dodecyl sulfate (SDS) at various pH values. The stepwise quenching of BSA tryptophan fluorescence and the gradual increase in the degree of anisotropy of BSA tryptophan fluorescence with increasing SDS concentration in solutions indicate the stepwise nature of denaturation: the first stage is a loosening of protein globules, whereas the second is a complete unfolding of the protein amino acid chain. At pH > pI of BSA, the denaturation BSA proceeds through both stages. At pH > pI of BSA, the denaturation BSA runs poorly and stops after the first stage. A more efficient BSA denaturation under the action of SDS occurs at pH < pI of BSA, with the efficiency of BSA denaturation under the influence of SDS decreasing with increasing pH.