Poster de conférence
Résumé : Carbohydrates of glycoproteins, such as myleoperoxidase (MPO), play an important role in biosynthesis and influence properties of the mature protein such as solubility, stability, immunogenicity, or molecular recognition. In the case of MPO, five N-glycans sites were described in the literature (P. Van Antwerpen, J. Biol. Chem., 2010) and the activity of deglycosylated enzyme was decreased significantly by comparison with native enzyme. Indeed, at least 3 of the five glycosylation sites were able to interact with receptors or others membranes proteins; the others ones, localized at interface, contributes to dimer stabilization. Moreover, N-glycosylation of MPO could modulate the enzyme activity and could change in some pathologies. For example, a high mannose and a complex glycan structures were presented on residue N485 of MPO in samples from a leukemia patient (T. Ravnsborg, Bioch. Biophys. Acta, 2010). In this context, the development of mass spectrometry coupled to liquid chromatography that could quantify modifications sustained by the carbohydrate moiety of MPO, is of interest. After digestion by PNGase F from glycoproteins and a eventual permethylation, glycans analysis using liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) was carried out with different sources (ESI and APCI) and chromatographic systems.

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