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- W2005958892 abstract "Abstract Investigation of site‐specific protein O ‐glycosylation remains a formidable task in post‐translational modification‐centred proteomics. In particular, the determination of O ‐glycosylated amino acids in mucin‐like glycopeptides lags far behind the techniques for phosphorylation site and N ‐glycosylation site identification, for which well‐established enrichment techniques are available. The present work investigated β‐elimination of mucin‐like O ‐glycopeptides with a mild alkylamine base and concomitant Michael‐type addition using 2‐mercaptoethanol as nucleophile applied to synthetic GalNAcylated O ‐glycopeptides as well as exoglycosidase‐treated endogenous peptides isolated from human blood plasma. This strategy permits O ‐glycosylated sites to be unambiguously localized, even in multiple‐glycosylated peptides. Peptides covalently modified with the glycan surrogate exhibit excellent backbone fragmentation in MS/MS due to their stability during CID." @default.
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- W2005958892 date "2011-12-01" @default.
- W2005958892 modified "2023-10-18" @default.
- W2005958892 title "Evaluation of non‐reductive β‐elimination/Michael addition for glycosylation site determination in mucin‐like <i>O</i>‐glycopeptides" @default.
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- W2005958892 doi "https://doi.org/10.1002/elps.201100393" @default.
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