“Subunit-exchange” chromatography of proteins: Behavior of α-chymotrypsin

Abstract

Protein subunits attached covalently to a solid matrix bind free subunits under conditions where an association-dissociation equilibrium exists in the soluble protein. This is the basis of a process which may be called “subunit-exchange chromatography”. The process, which may be applied to any self-associating protein, is exemplified here with α-chymotrypsin. The behavior of the system has been studied in detail especially with respect to the conditions of immobilization of the monomer. The results indicate the potentialities of the method for analytical and preparative purposes.