Identification of isoenzymes using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

Abstract : 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.
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Submitted on : Monday, August 7, 2006 - 2:23:51 PM
Last modification on : Tuesday, June 4, 2019 - 4:30:11 PM

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J. Hardouin, M. Hubert-Roux, A.F. Delmas, C. Lange. Identification of isoenzymes using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Rapid Communications in Mass Spectrometry, Wiley, 2006, 20, pp.725-732. ⟨10.1002/rcm.2355⟩. ⟨hal-00088855⟩

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