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Rapid Separation of Proteins by Capillary HPLC on a Short Polymethacrylate‐based Strong Cation‐exchange Monolithic Column
Author(s) -
Ding Mingyu,
Wang Zonghua,
Zheng Rui
Publication year - 2010
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.201090113
Subject(s) - chemistry , monolithic hplc column , monolith , glycidyl methacrylate , monomer , polymerization , chromatography , copolymer , solvent , propanol , capillary action , chemical engineering , polymer chemistry , high performance liquid chromatography , polymer , organic chemistry , ethanol , materials science , engineering , composite material , catalysis
A polymethacrylate‐based strong cation‐exchange capillary monolithic column was prepared by in‐situ copolymerization for the fast separation of proteins. Glycidyl methacrylate (GMA) was used as monomer, ethylenedimethacrylate (EDMA) as cross link agent and the mixture of 1‐propanol, 1,4‐butanediol and water as porogen solvent. The monolith was sulfonated using 1 mol/L Na 2 SO 3 based on a ring opening of epoxides. The influences of the contents of the porogen solvent and GMA and the various concentration ratios of 1‐propanol to 1,4‐butanediol in the polymerization mixture on the morphology, porosity, globule size, stability and column efficiency were investigated. The morphology and pore size distribution of the monolith were characterized by SEM and mercury intrusion porosimetry, respectively. Using only 1.5 cm length of this monolithic capillary column, four kinds of proteins, trypsin, cytochrome C, lysozyme (egg white) and egg albumin, were successfully separated from each other in 5 min at a high flow rate of 110 mm/s.