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High‐sensitive protein analysis by FESI‐CE‐MALDI‐MS
Author(s) -
Pourhaghighi Mohammad Reza,
Busnel JeanMarc,
Girault Hubert H.
Publication year - 2011
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201100024
Subject(s) - capillary electrophoresis , chromatography , mass spectrometry , chemistry , capillary electrophoresis–mass spectrometry , electrokinetic phenomena , analytical chemistry (journal) , matrix assisted laser desorption/ionization , desorption , matrix (chemical analysis) , electrophoresis , bioanalysis , electrospray ionization , adsorption , organic chemistry
Capillary zone electrophoresis (CZE) and matrix‐assisted laser desorption ionization mass spectrometry (MALDI‐MS) are two techniques highly suitable for the separation and detection of intact proteins. Herein, based on the use of a recently introduced iontophoretic fraction collection interface for the coupling of CE and MALDI‐MS, the potential of the combination of both techniques for the analysis of intact proteins is assessed. To further provide a bioanalytical platform with high‐sensitivity capabilities, field‐enhanced sample injection is integrated as on online preconcentration strategy upstream from the electrokinetic separation. Under optimized conditions, more than 3200‐ and 4800‐fold improvement, respectively in terms of peak height and peak area, as well as LODs ranging from 5 to 10 nM, has been achieved.