Non-ionic adsorption chromatography of proteins.
Abstract Evidence is presented indicating that protein separation by adsorption chromatography, based on differential non-ionic interaction with immobilized hydrophobic ligands, potentially is as generally applicable as ion-exchange chromatography. A procedure for the normalization of binding capacities of amine-substituted agaroses has been presented. Attempts have been made at the separation of proteins in normal human blood serum by means of hydrophobicity gradients consisting of series of interconnected columns of n -alkylamino-agaroses of increasing hydrophobicities and equilibrated with 3 M NaCl. The γ-globulin fraction, or components thereof, can be bound hydrophobically as well as through another type of salt(NaCl)-stable but non-hydrophobic binding.