Interactions of proteins with other polyelectrolytes in a two-phase system containing phenol and aqueous buffers at various pH values

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Abstract
Interactions of proteins with neutral polysaccharides and such polyacids as polygalacturonic acid, chondroitin sulphate, RNA and DNA in a 2-phase system composed of phenol and aqueous buffers in the pH range 1.5-10 were studied. Analysis of the products of the interaction was facilitated by the absolute preference of the proteins studied for the phenol-rich phase at all pH values. The polyacids, on the other hand, in the absence of interactions were recovered mainly from the aqueous phases. The interaction, the extent of which was mainly determined by the pH-dependent ionization state of the reacting partners, followed the patterns of antigen-antibody interactions with a well-defined equivalence point (maximum point of precipitation) and with the formation of soluble complexes. The soluble complexes formed below the equivalence point were composed of proteins with small amounts of polyacids attached, and so passed into the phenol-rich phase; those formed above the maximum precipitation point were polyacidic in character and found in the aqueous phases. Glycoproteins, with small amounts of covalently linked sugar residues, passed quantitatively into the phenol-rich phases. The possibilities of developing a method for the analysis of glycoproteins and other applications are discussed.