The properties of bovine serum albumin and chymotrypsinogen A in solvent mixtures containing phenol

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Abstract
The optical rotation and reduced viscosity of bovine serum albumin and chymotrypsinogen A in solvents containing phenol, acetic acid and water were studied. The changes brought about in the properties of the proteins by varying the composition of the solvent or by heat treatment in these solvents were established to be reversible. A method for returning the proteins to aqueous media, based on these observations, was worked out. The recovered proteins were shown to be very similar to, if not identical with, the native proteins on the basis of measurements of optical rotation, viscosity, sedimentation, ultraviolet spectroscopy, immunochemical behavior (serum albumin) and proteolytic activity (chymotrypsinogen A, after activation with trypsin). The importance of the findings for partitioning of polyelectrolytes in the phenol-aqueous buffer systems is discussed.