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Article Dans Une Revue Proteomics Année : 2012

An innovative strategy for sulfopeptides analysis using MALDI-TOF MS reflectron positive ion mode

Résumé

Sulfation of tyrosine residues is a key posttranslationalmodification in the regulation of various cellular processes. As such, the detection and localization of tyrosine sulfation is an essential step toward the elucidation of the physiological and pathological roles of this process. Despite substantial advances, intact sulfated peptides are still difficult to detect by MALDI-MS due to the extreme lability of the sulfo-moiety. The present report demonstrates for the first time how intact sulfated peptides can be directly and specifically detected by MALDI-MS in positive reflectronmode by using pyrenemethylguanidine (pmg) as a noncovalent derivatizing agent and an ionization enhancer. This new method allows the determination of the degree of sulfation of sulfopeptides pure or in mixtures. Moreover, the observation of specific peaks in the mass spectra enables a rapid and unambiguous discrimination between phospho- and sulfopeptides.

Dates et versions

hal-00726729 , version 1 (31-08-2012)

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Sonia Cantel, Luc Brunel, Ohara Keiichiro, Christine Enjalbal, Jean Martinez, et al.. An innovative strategy for sulfopeptides analysis using MALDI-TOF MS reflectron positive ion mode. Proteomics, 2012, 12, pp.2247-2257. ⟨10.1002/pmic.201100525⟩. ⟨hal-00726729⟩
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