Adsorption of dimethylsulfoxide on proteins

A method for measuring the adsorption of dimethylsulfoxide on native and de natured trypsin and albumin was developed. On native proteins, no positive adsorption was registered, and a slight negative adsorption within the limi ts of experimental error was observed. It was shown that the properties of denatured proteins depend on the mode and conditions of denaturation. On on e of denatured trypsin specimens, positive adsorption of dymethylsulfoxide was registered, on other specimens no adsorption was observed; The reason f or this behavior lies in the hydrophobic nature of adsorption of dimethylsu lfoxide at the interface, while the surface of native protein globules and, probably, most denatured protein specimens is hydrophilic.