DENATURATION OF HUMAN SERUM ALBUMIN AT THE PRESENCE OF UREA–DIMETHYLSULFOXID COMPLEXES

Abstract

Human serum albumin (HSA) chemical denaturation at 60 ^oC in aqueousdimethylsulfoxide (DMSO) solutions at the presence of urea has been investigated by the Uv/vis spectroscopy method. It has been shown that DMSO–urea complexes, which have been formed in the solution, induce the HSA denaturation. A suggestion has been made that the HSA denaturation has two stages at the presence of these complexes: the first stage – protein globule loosening and the second – full unfolding of protein molecule. In the HSA–urea–DMSO system predominate hydrophobic interactions.