Arica M.Y.Akin-Öktem G.Denizli A.2020-06-252020-06-25200109277765https://doi.org/10.1016/S0927-7765(00)00209-5https://hdl.handle.net/20.500.12587/1678In this study, phenylalanine as a hydrophobic ligand was covalently attached to the co-monomer methacrylochloride. Then, poly(2-hydroxyethylmethacrylate-co-methacrylamidophenyalanine) [poly(HEMA-MAPA)] membranes were prepared by UV-initiated photopolymerization of HEMA and methacrylamidophenyalanine. The ?-globulins adsorption onto these affinity membranes from aqueous solutions containing different amounts of ?-globulins at different pH was investigated in a batch system. The ?-globulins adsorption capacity of the membranes was increased as the ligand density on the membrane surface increase. The non-specific adsorption of the ?-globulins on the pHEMA membranes was negligible. The adsorption phenomena appeared to follow a typical Langmuir isotherm. The maximum adsorption capacity (qm) of the poly(HEMA-MAPA4) membrane for ?-globulins was 2.37 mg g-1dry membrane. The equilibrium constant (kd) value was found to be 1.61×10-1mg ml-1. More than 87% (up to 100%) of the adsorbed ?-globulins were desorbed in 120 min in the desorption medium containing 50% ethylene glycol in 1.0 M NaCl. Copyright © 2001 Elsevier Science B.V.eninfo:eu-repo/semantics/closedAccessAffinity membraneHydrophobic ligandPhenylalanineProtein separation?-globulinsArticle21427328310.1016/S0927-7765(00)00209-52-s2.0-0035002089Q1