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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
