Abstract

Subunit exchange chromatography exploits the observation that subunits immobilized on a solid matrix retain the capacity to recognize the subunits in solution in a highly specific way. Hence, oligomeric and self-associating proteins can be extracted in a simple and efficient way from a multicomponent mixture under conditions that favour subunit association; subsequently, the protein is eluted under conditions that favour its dissociation into subunits. The method lends itself also to the isolation of homologous proteins capable of forming hybrids with the immobilized subunits.

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