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Time of flight versus ion trap MS coupled to CE to analyse intact proteins
Author(s) -
Erny Guillaume L.,
León Carlos,
Marina Maria Luisa,
Cifuentes Alejandro
Publication year - 2008
Publication title -
journal of separation science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.72
H-Index - 102
eISSN - 1615-9314
pISSN - 1615-9306
DOI - 10.1002/jssc.200700651
Subject(s) - repeatability , chemistry , mass spectrometry , chromatography , ion trap , analytical chemistry (journal) , time of flight mass spectrometry , reproducibility , electrospray , ion , ionization , organic chemistry
In this work, two different CE‐MS instruments, namely, CE‐ESI‐IT‐MS and CE‐ESI‐TOF‐MS, applied to analyse intact proteins from complex samples are investigated. The aim of this work was to compare both instruments in terms of LOD, number of proteins detected, and precision and repeatability in the determination of the protein relative molecular mass. Results show that although CE‐ESI‐IT‐MS provides cleaner MS spectra of intact proteins, CE‐ESI‐TOF‐MS allows the identification of a higher number of proteins from complex matrices in an easier way. Performance in terms of peak area reproducibility, LOD and precision in the determination of the molecular mass were similar for both instruments. The usefulness of the optimised CE‐ESI‐IT‐MS and CE‐ESI‐TOF‐MS conditions was demonstrated by studying the zein‐proteins composition of three natural maize lines and their corresponding transgenic lines, showing no significant differences.