Percin, IsikKhalaf, RushdBrand, BastianMorbidelli, MassimoGezici, Orhan2019-08-012019-08-0120150021-96731873-3778https://dx.doi.org/10.1016/j.chroma.2015.01.075https://hdl.handle.net/11480/3963A 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.eninfo:eu-repo/semantics/closedAccessGradient elutionHPLCIon-exchangeProteinSeparationYamamoto ModelStrong cation-exchange chromatography of proteins on a sulfoalkylated monolithic cryogelArticle1386132110.1016/j.chroma.2015.01.075256836272-s2.0-84924539995Q1WOS:000350930200002Q1