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

J Am Soc Mass Spectrom. 2001 Oct;12(10):1106-13. doi: 10.1016/s1044-0305(01)00295-1.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acylation
  • Amino Acid Sequence
  • Chromatography, High Pressure Liquid
  • Crystallins / chemistry*
  • Electrophoresis, Polyacrylamide Gel
  • Galactose / chemistry
  • Hydrolysis
  • Mass Spectrometry
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Spectrometry, Mass, Electrospray Ionization


  • Crystallins
  • Peptides
  • Galactose