Protein-protein interactions as a means of purification
Hetero-association-based separations are characterized by great specificity and large protein-protein interaction energies and are well suited to application early in separation trains. Research efforts involving reverse micellar extraction and affinity chromatography processes, particularly with respect to affinity ligand engineering and processing, are improving selectivity and decreasing process, but not molecular, complexity. Self-association-based separations are less specific because the underlying interaction energies are smaller; they are prone to interference from contaminants. Efforts in precipitation processes are improving our understanding of protein solubility behavior. In spite of recent progress, the full ultrapurification potentials of bulk crystallization and self-interaction chromatography processes remain unrealized.
Applied Biophysics Laboratory Howard P Isermann Department of Chemical Engineering Rensselaer Polytechnic Institute Troy, NY 12180-3590, USA przybt@rpi.edu
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