title: Identification of GlcNAcylation sites of peptides and alpha-crystallin using Q-TOF mass spectrometry.
abstract: The addition of a single N-acetylglucosamine residue O-linked to serine and threonine residues of nuclear and cytoplasmic proteins is a widespread modification throughout all eukaryotes. The conventional method for detecting and locating sites of modification is a multi-step radioactivity-based protocol. In this paper we show that using quadrupole time-of-flight (Q-TOF) mass spectrometry, modification sites can be identified at a significantly higher sensitivity than previous approaches. This is the first demonstration that sites of O-GlcNAcylation can be identified directly using mass spectrometry.
authors.affiliation: Ludwig Institute for Cancer Research, University College Branch of Cell and Molecular Biology, Royal Free and University College Medical School, London, UK.
authors.forename: R J
authors.initials: RJ
authors.lastname: Chalkley
authors.forename: A L
authors.initials: AL
authors.lastname: Burlingame
mesh_terms: D000215:Acylation; D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D003459:Crystallins / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D005690:Galactose / Q000737:chemistry; D006868:Hydrolysis; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D021241:Spectrometry, Mass, Electrospray Ionization
chemical_list: D003459:Crystallins; D010455:Peptides; D005690:Galactose