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Identification of isoenzymes using matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry
Author(s) -
Hardouin Julie,
HubertRoux Marie,
Delmas Agnès F.,
Lange Catherine
Publication year - 2006
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.2355
Subject(s) - chemistry , mass spectrometry , reflectron , matrix assisted laser desorption/ionization , proteomics , time of flight mass spectrometry , chromatography , protein mass spectrometry , ionization , sample preparation in mass spectrometry , top down proteomics , electrospray ionization , ion , desorption , biochemistry , organic chemistry , adsorption , gene
The identification of isoforms is one of the great challenges in proteomics due to the large number of identical amino acids preventing their separations by two‐dimensional electrophoresis. Matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry (MALDI‐TOFMS) has become a rapid and sensitive tool in proteomics, notably with the new instrumental improvements. In this study, we used several acquisition modes of MALDI‐TOFMS to identify isoforms of porcine glutathiones S‐transferase. The use of multiple proteases coupled to the different acquisition modes of MALDI‐TOFMS (linear, reflectron, post‐source decay (PSD) and in‐source decay, positive and negative modes) allowed the identification of two sequences. Moreover, a third sequence is pointed out from a PSD study of a tryptic ion revealing the modification of the amino acid tyrosine 146 to phenylalanine. Copyright © 2006 John Wiley & Sons, Ltd.