Interactions of human serum albumin with some alkylureas.

The interactions of human albumin with urea, methyl-, N,N'-dimethyl-, ethyl-, N,N'-diethyl-, propyl-, and butylurea were studied by means of calorimetry and circular dichroism. It has been found that the enthalpies of interaction of the alkylureas with human serum albumin are distinctly different from those of urea. Thus, the transfer of the protein from water to aqueous urea solutions is accompanied by release of heat, i.e., the overall reaction is exothermic, whereas the transfer of the same protein of solutions of alkylureas is characterized by consumption of heat, i.e., the overall reaction is endothermic. By examining the far ultraviolet circular dichroism in behavior reflects the presence of the hydrophobic moiety in the urea molecule.