[Study of alcohol binding with serum albumin by NMR spectra of frozen aqueous solutions].

Interaction of alcohols (methanol, glycerol, sorbitol) with human serum albumin (HSA) was studied by the use of NMR spectroscopy in frozen aqueous solutions. The amount of binding was shown to increase in the series methanol-glycerol-sorbitol, on this basis a suggestion is made that interaction of alcohols with HSA occurs due to the formation of hydrogen bonds in which the hydroxyl groups act as proton donors. It is found that the presence of albumin influences significantly the outcome of eutectics from a diluted methanol solution and glycerol solution, the temperature of eutectics decreases in case of methanol and increases in case of glycerol.