Strong cation-exchange chromatography of proteins on a sulfoalkylated monolithic cryogel
Küçük Resim Yok
Tarih
2015
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
ELSEVIER SCIENCE BV
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
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.
Açıklama
Anahtar Kelimeler
Gradient elution, HPLC, Ion-exchange, Protein, Separation, Yamamoto Model
Kaynak
JOURNAL OF CHROMATOGRAPHY A
WoS Q Değeri
Q1
Scopus Q Değeri
Q1
Cilt
1386
