Human serum albumin adsorption on poly[(glycidyl methacrylate)-co-(methyl methacrylate)] beads modified with a spacer-arm-attached L-histidine ligand

dc.contributor.authorBayramoğlu, Gülay
dc.contributor.authorŞenel, Ayşegül Ülkü
dc.contributor.authorYalçın, Emine
dc.contributor.authorArıca, M. Yakup
dc.date.accessioned2020-06-25T17:41:15Z
dc.date.available2020-06-25T17:41:15Z
dc.date.issued2006
dc.departmentKırıkkale Üniversitesi
dc.description.abstractPoly(GMA/MMA) beads were synthesized from glycidyl methacrylate (GMA) and methyl methacrylate (MMA) in the presence of a cross-linker (i.e. ethyleneglycol dimethacrylate) (EGDMA) via suspension polymerization. The epoxy groups of the poly(GMA/MMA) beads were converted into amino groups with either ammonia or 1,6-diaminohexane (i.e. spacer-arm). An L-histidine ligand was then covalently immobilized on the aminated (poly(GMA/MMA)-AH) and/or the spacer-arm attached (poly(GMA/MMA)-SAH) beads using glutaric dialdehyde as a coupling agent. Both affinity adsorbents were used in human serum albumin (HSA) adsorption/desorption studies under defined pH, ionic strength or temperature conditions in a batch reactor. The spacer-arm attached affinity adsorbent resulted in an increase in the adsorption capacity to HSA when compared to the aminated counterpart (i.e. poly(GMA/MMA)-AH). The maximum adsorption capacities of the affinity adsorbents were found to be significantly high, i.e. 43.7 and 80.2 mg g(-1) (of the beads), while the affinity constants, evaluated by the Langmuir model, were 3.96 x 10(-7) and 9.53 x 10(-7) molL(-1) for poly(GMA/MMA) -AH and poly(GMA/MMA)-SAH, respectively. The adsorption capacities of the affinity adsorbents were decreased for HSA by increasing the ionic strength, adjusted with NaCl. The adsorption kinetics of HSA were analysed by using pseudo-first and pseudo-second-order equations. The second-order equation fitted well with the experimental data. (c) 2005 Society of Chemical Industry.en_US
dc.identifier.citationclosedAccessen_US
dc.identifier.doi10.1002/pi.1905
dc.identifier.endpage48en_US
dc.identifier.issn0959-8103
dc.identifier.issn1097-0126
dc.identifier.issue1en_US
dc.identifier.scopus2-s2.0-30444450438
dc.identifier.scopusqualityQ1
dc.identifier.startpage40en_US
dc.identifier.urihttps://doi.org/10.1002/pi.1905
dc.identifier.urihttps://hdl.handle.net/20.500.12587/3667
dc.identifier.volume55en_US
dc.identifier.wosWOS:000234608100007
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherWileyen_US
dc.relation.ispartofPolymer International
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectpoly(GMA/MMA) beadsen_US
dc.subjectspacer-armen_US
dc.subjecthistidineen_US
dc.subjectaffinity adsorbentsen_US
dc.subjecthuman serum albuminen_US
dc.subjectadsorptionen_US
dc.titleHuman serum albumin adsorption on poly[(glycidyl methacrylate)-co-(methyl methacrylate)] beads modified with a spacer-arm-attached L-histidine liganden_US
dc.typeArticle

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