Strong cation-exchange chromatography of proteins on a sulfoalkylated monolithic cryogel

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dc.authorid0000-0001-6808-2282
dc.contributor.authorPercin, Isik
dc.contributor.authorKhalaf, Rushd
dc.contributor.authorBrand, Bastian
dc.contributor.authorMorbidelli, Massimo
dc.contributor.authorGezici, Orhan
dc.date.accessioned2019-08-01T13:38:39Z
dc.date.available2019-08-01T13:38:39Z
dc.date.issued2015
dc.departmentNiğde ÖHÜ
dc.description.abstractA new strong cation exchanger (SCX) monolithic column was synthesized by at-line surface modification of a cryogel prepared by copolymerization of 2-hydroxyethylmethacrylate (HEMA) and glycidyl-methacrylate (GMA). Sodium salt of 3-Mercaptopropane sulfonic acid (3-MPS) was used as the ligand to transform the surface of the monolith into a strong cation exchanger. The obtained material was characterized in terms of elemental analysis, infrared spectroscopy (FTIR), Scanning Electron Microscopy (SEM), Brunauer-Emmett-Teller (BET) N-2 adsorption, and used as a stationary phase for strong-cation exchange chromatography of some proteins, such as a-chymotrypsinogen, cytochrome c and lysozyme. Water permeability of the column was calculated according to Darcy's law (2.66 x 10(-13) m(2)). The performance of the monolithic cryogel column was evaluated on the basis of Height Equivalent to a Theoretical Plate (HETP). Retention behavior of the studied proteins was modeled on the basis of Yamamoto model to understand the role of the ion-exchange mechanism in retention behaviors. The considered proteins were successfully separated, and the obtained chromatogram was compared with that obtained with a non-functionalized cryogel column. (c) 2015 Elsevier B.V. All rights reserved.
dc.description.sponsorshipScientific and Technological Research Council of Turkey (TUBITAK) [2219]
dc.description.sponsorship- O. Gezici would like to thank (i) Scientific and Technological Research Council of Turkey (TUBITAK) for the postdoctoral scholarship provided through 2219-program (2013-2014), and (ii) Nigde University (Turkey) for the facilities provided.
dc.identifier.doi10.1016/j.chroma.2015.01.075
dc.identifier.endpage21
dc.identifier.issn0021-9673
dc.identifier.issn1873-3778
dc.identifier.pmid25683627
dc.identifier.scopus2-s2.0-84924539995
dc.identifier.scopusqualityQ1
dc.identifier.startpage13
dc.identifier.urihttps://dx.doi.org/10.1016/j.chroma.2015.01.075
dc.identifier.urihttps://hdl.handle.net/11480/3963
dc.identifier.volume1386
dc.identifier.wosWOS:000350930200002
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.institutionauthor[0-Belirlenecek]
dc.language.isoen
dc.publisherELSEVIER SCIENCE BV
dc.relation.ispartofJOURNAL OF CHROMATOGRAPHY A
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectGradient elution
dc.subjectHPLC
dc.subjectIon-exchange
dc.subjectProtein
dc.subjectSeparation
dc.subjectYamamoto Model
dc.titleStrong cation-exchange chromatography of proteins on a sulfoalkylated monolithic cryogel
dc.typeArticle

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