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Identification of GlcNAcylation sites of peptides and α-crystallin using Q-TOF mass spectrometry

  • Robert J. Chalkley
  • A. L. BurlingameEmail author
Article

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.

Keywords

GlcNAc Glycopeptide Cone Voltage GlcNAc Residue Optimal Collision Energy 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© American Society for Mass Spectrometry 2001

Authors and Affiliations

  1. 1.Ludwig Institute for Cancer Research, University College Branch of Cell and Molecular BiologyRoyal Free and University College Medical SchoolLondonUK
  2. 2.Department of Pharmaceutical Chemistry, Mass Spectrometry FacilityUniversity of California San FranciscoSan FranciscoUSA
  3. 3.Department of Pharmaceutical ChemistryUniversity of California San FranciscoSan FranciscoUSA

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