Immunoglobulin G adsorption behavior of L-histidine ligand attached and Lewis metal ions chelated affinity membranes

Basit Öğe Kaydı
dc.contributor.authorBayramoğlu, Gülay
dc.contributor.authorÇelik, Gökçe
dc.contributor.authorArica, M. Yakup
dc.date.accessioned2020-06-25T17:41:27Z
dc.date.available2020-06-25T17:41:27Z
dc.date.issued2006
dc.description.abstractImmobilized metal affinity membranes were prepared by chelating Cu(II) and Fe(III) ions on poly(2-hydroxyethyl methacrylate-glycidyl methacrylate), poly(HEMA-GMA) membranes using L-histidine as a chelating ligand. To achieve this goal, the poly(HEMA-GMA) membrane was prepared via UV initiated photopolymerization. A spacer-arm (i.e., 1,6-diaminohexane) was introduced through the epoxy groups of the membrane (poly(HEMA-GMA)-SA). A chelating ligand (i.e., L-histidine amino acid) was covalently attached on the poly(HEMA-GMA) and/or poly(HEMAGMA)-SA using glutaric dialdehyde as a coupling agent, poly(HEMA-GMA)-H and poly(HEMA-GMA)-SAH membranes, respectively. Then, Cu(II) and Fe(III) ions were chelated through poly(HEMA-GMA)-SAH membrane. The binding characteristics of human immunoglobulin G (IgG) to IMAC membranes and the selectivity of Cu(II) and Fe(III) ions to the IgG have been investigated from aqueous solution using L-histidine attached membrane (poly(HEMA-GMA)-SAH) as a control system. The experimental data was analyzed using two adsorption kinetic models, the pseudo-first-order and the pseudo-second-order, to determine the best-fit equation for the adsorption of IgG onto L-histidine incorporated and/or different metals ion immobilized affinity membranes. The first-order equation in the affinity membrane systems is the most appropriate equation to predict the adsorption capacity for all the tested adsorbents. Moreover, the effect of spacer-arm on the adsorption capacity was evaluated using poly(HEMA-GMA)-H membrane as a control system. The IgG binding order on the affinity membranes was poly(HEMA-GMA)-SAHCu(II) > poly(HEMA-GMA)-SAH-Fe(III) > poly(HEMA-GMA)-SAH > poly(HEMA-GMA)-H. Finally, the polarities and the surface free energies of the affinity membranes were determined by contact angle studies. (c) 2006 Elsevier B.V. All rights reserved.en_US
dc.identifier.citationclosedAccessen_US
dc.identifier.doi10.1016/j.colsurfa.2006.03.027
dc.identifier.endpage85en_US
dc.identifier.issn0927-7757
dc.identifier.issue1-3en_US
dc.identifier.scopus2-s2.0-33751080111
dc.identifier.scopusqualityQ1
dc.identifier.startpage75en_US
dc.identifier.urihttps://doi.org10.1016/j.colsurfa.2006.03.027
dc.identifier.urihttps://hdl.handle.net/20.500.12587/3717
dc.identifier.volume287en_US
dc.identifier.wosWOS:000240521800011
dc.identifier.wosqualityQ3
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherElsevier Science Bven_US
dc.relation.ispartofColloids And Surfaces A-Physicochemical And Engineering Aspects
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectmembraneen_US
dc.subjectaffinity chromatographyen_US
dc.subjectmetal chelateen_US
dc.subjectIgGen_US
dc.subjectadsorptionen_US
dc.subjectcontact angleen_US
dc.subjectsurface interactionen_US
dc.titleImmunoglobulin G adsorption behavior of L-histidine ligand attached and Lewis metal ions chelated affinity membranesen_US
dc.typeArticle

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