1 Ocak 2015 Dergi makalesi Açık Erişim

Percin, Isik; Khalaf, Rushd; Brand, Bastian; Morbidelli, Massimo; Gezici, Orhan

Dublin Core

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  <dc:creator>Percin, Isik</dc:creator>
  <dc:creator>Khalaf, Rushd</dc:creator>
  <dc:creator>Brand, Bastian</dc:creator>
  <dc:creator>Morbidelli, Massimo</dc:creator>
  <dc:creator>Gezici, Orhan</dc:creator>
  <dc:date>2015-01-01</dc:date>
  <dc:description>A 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>
  <dc:identifier>https://aperta.ulakbim.gov.trrecord/78327</dc:identifier>
  <dc:identifier>oai:zenodo.org:78327</dc:identifier>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:rights>http://www.opendefinition.org/licenses/cc-by</dc:rights>
  <dc:source>JOURNAL OF CHROMATOGRAPHY A 1386 13-21</dc:source>
  <dc:title>Strong cation-exchange chromatography of proteins on a sulfoalkylated monolithic cryogel</dc:title>
  <dc:type>info:eu-repo/semantics/article</dc:type>
  <dc:type>publication-article</dc:type>
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