Adsorption and separation of immunoglobulins by novel affinity core-shell beads decorated with protein L and L-histidine

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dc.contributor.authorBayramoğlu, Gülay
dc.contributor.authorÖzalp, V. Cengiz
dc.contributor.authorArıca, M. Yakup
dc.date.accessioned2021-05-15T12:40:58Z
dc.date.available2021-05-15T12:40:58Z
dc.date.issued2013
dc.departmentTıp Fakültesien_US
dc.descriptionOzalp, Veli Cengiz/0000-0002-7659-5990
dc.description.abstractA novel core shell beaded chromatographic materials was prepared by grafting of glycidyl methacrylate (GMA) on to the surface of poly(hydoxypropyl methacrylate/ethyleneglycol dimethacrylate), p(HPMA/EGDMA) beads via surface-initiated atom transfer radical polymerization (SI-ATRP). For grafting GMA, p(HPMA/EGDMA) beads were first modified with an ATRP initiator. A reaction with 2-bromo-2-methylpropionyl bromide of the hydroxyl groups of the beads led to ATRP initiator-covered surfaces. The grafted p(GMA) fibrous chains on the beads were decorated with two different ligands (i.e., Protein L and L-histidine) for separation of Immunoglobulin's (Igs) from aqueous solution in batch system. The maximum Igs adsorptions on the p(HPMA/EGDMA)-g-p(GMA)-Protein L and p(HPMA/EGDMA)-g-p(GMA)-L-histidine affinity beads were found to be 81.8 and 112.3 mg/g at pH 7.5 and 5.5, respectively. The purity of Igs from human serum was analyzed by HPLC. The Protein L immobilized affinity beads provided purity about 98%. The novel core shell polymeric beads decorated with Protein L showed a good selectivity for Igs molecules from diluted human serum. Adsorption studies of Igs onto Protein L and L-histidine immobilized affinity beads were also carried out in a continuous system. (C) 2013 Elsevier B.V. All rights reserved.en_US
dc.identifier.doi10.1016/j.jchromb.2013.07.025
dc.identifier.endpage9en_US
dc.identifier.issn1570-0232
dc.identifier.issn1873-376X
dc.identifier.pmid23959148
dc.identifier.scopus2-s2.0-84882741693
dc.identifier.scopusqualityQ2
dc.identifier.startpage1en_US
dc.identifier.urihttps://doi.org/10.1016/j.jchromb.2013.07.025
dc.identifier.urihttps://hdl.handle.net/20.500.12939/719
dc.identifier.volume936en_US
dc.identifier.wosWOS:000324564400001
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.institutionauthorArıca, M. Yakup
dc.language.isoen
dc.publisherElsevier Science Bven_US
dc.relation.ispartofJournal of Chromatography B-Analytical Technologies in the Biomedical and Life Sciences
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectAffinity Beadsen_US
dc.subjectProtein Len_US
dc.subjectL-Histidineen_US
dc.subjectAdsorptionen_US
dc.subjectSeparationen_US
dc.subjectImmunoglobulinsen_US
dc.titleAdsorption and separation of immunoglobulins by novel affinity core-shell beads decorated with protein L and L-histidine
dc.typeArticle

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