Adsorption of serum albumin and γ-globulin from single and binary mixture and characterization of pHEMA-based affinity membrane surface by contact angle measurements

Basit Öğe Kaydı
dc.contributor.authorBayramoğlu, Gülay
dc.contributor.authorYalçın, Emine
dc.contributor.authorArıca, M. Yakup
dc.date.accessioned2020-06-25T17:40:19Z
dc.date.available2020-06-25T17:40:19Z
dc.date.issued2005
dc.departmentKırıkkale Üniversitesi
dc.description.abstractIn this study, an affinity membrane was synthesized using 2-hydroxyethylmethacrylate (HEMA) via UV-initiated photopolymerization. A dye-ligand (i.e., Procion Red HE-3B; Red-120) was covalently immobilized onto membrane. Human serum albumin (HSA) and human gamma-globulin (HIgG) adsorption onto pHEMA-Red-120 membrane were studied using bare poly(hydroxyethylmethacrylate) (pHEMA) membrane as a control system. The information about surface energy, hydrophobicity and chemical heterogeneity of the affinity membrane was obtained by contact angle measurements. The contact angle values of the affinity membrane were determined by sessile drop method using water, glycerol and diiodomethane as test liquids. Component and parameters of the surface free energy of all the investigated samples were calculated from measured contact angle values using the acid-base method of the van Oss. The adsorption of HSA and HIgG significantly changed both the contact angles and component of surface free energies of the affinity membrane. The reversible HSA and HIgG adsorption on the pHEMA-Red-120 followed the Freundlich and Langmuir-Freundlich isotherm models. Selectivity of the affinity membrane was tested at different pH values to HSA and HIgG and the protein concentration of in the binary system was determined by HPLC. The affinity membrane was stable when subjected to sanitization with sodium hydroxide after repeated adsorption-elution cycles. (c) 2005 Elsevier B.V. All rights reserved.en_US
dc.identifier.citationclosedAccessen_US
dc.identifier.doi10.1016/j.bej.2005.06.002
dc.identifier.endpage21en_US
dc.identifier.issn1369-703X
dc.identifier.issn1873-295X
dc.identifier.issue1en_US
dc.identifier.scopus2-s2.0-24044528574
dc.identifier.scopusqualityQ2
dc.identifier.startpage12en_US
dc.identifier.urihttps://doi.org/10.1016/j.bej.2005.06.002
dc.identifier.urihttps://hdl.handle.net/20.500.12587/3391
dc.identifier.volume26en_US
dc.identifier.wosWOS:000232041500002
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherElsevier Science Bven_US
dc.relation.ispartofBiochemical Engineering Journal
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectmicroporous membraneen_US
dc.subjectaffinity chromatographyen_US
dc.subjectdye-liganden_US
dc.subjectadsorptionen_US
dc.subjectseparationen_US
dc.subjectalbuminen_US
dc.subjectgamma-globulinsen_US
dc.subjectcontact angleen_US
dc.titleAdsorption of serum albumin and γ-globulin from single and binary mixture and characterization of pHEMA-based affinity membrane surface by contact angle measurementsen_US
dc.typeArticle

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