Birkenmeier G, Vijayalakshmi M A, Stigbrand T, Kopperschläger G
Institute of Biochemistry, Karl-Marx-Universität Leipzig, Germany.
J Chromatogr. 1991 Feb 22;539(2):267-77. doi: 10.1016/s0021-9673(01)83935-2.
Immobilized metal ions were used for the affinity extraction of proteins in aqueous two-phase systems composed of polyethylene glycol (PEG) and dextran or PEG and salt. Soluble chelating polymers were prepared by covalent attachment of metal-chelating groups to PEG. The effect on the partitioning of proteins of such chelating PEG derivatives coordinated with different metal ions is demonstrated. The proteins studied were alpha 2-macroglobulin, tissue plasminogen activator, superoxide dismutase and monoclonal antibodies. The results indicate that immobilized metal ion affinity partitioning provides excellent potential for the extraction of proteins.