Biospecific-elution chromatography with 'imphilytes' as stationary phases

Six out of seven enzymes tested (four of them nicotinamide nucleotide-dependent dehydrogenases) showed differences in chromatographic behaviour in the presence and absence of their biospecific ligands, when chromatographed on immobilized amphipathic ampholytes ('imphilytes') as stationary phases. Some enzymes were adsorbed more tightly, others less tightly, in the presence of ligands. These results have implications for enzyme purification in general, and for some types of affinity chromatography in particular.