1 Ocak 2015 Dergi makalesi Açık Erişim

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

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        "name": "Percin, Isik"
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        "affiliation": "ETH, Inst Chem & Bioengn, CH-8093 Zurich, Switzerland", 
        "name": "Khalaf, Rushd"
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      {
        "affiliation": "ETH, Inst Chem & Bioengn, CH-8093 Zurich, Switzerland", 
        "name": "Brand, Bastian"
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      {
        "affiliation": "ETH, Inst Chem & Bioengn, CH-8093 Zurich, Switzerland", 
        "name": "Morbidelli, Massimo"
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        "name": "Gezici, Orhan"
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    "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.", 
    "doi": "10.1016/j.chroma.2015.01.075", 
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    "journal": {
      "pages": "13-21", 
      "title": "JOURNAL OF CHROMATOGRAPHY A", 
      "volume": "1386"
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    "title": "Strong cation-exchange chromatography of proteins on a sulfoalkylated monolithic cryogel"
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