Direct determination of glycosylation sites in O-fucosylated glycopeptides using nano-electrospray quadrupole time-of-flight mass spectrometry
Article first published online: 26 APR 2001
Copyright © 2001 John Wiley & Sons, Ltd.
Rapid Communications in Mass Spectrometry
Volume 15, Issue 10, pages 771–777, 30 May 2001
How to Cite
Maček, B., Hofsteenge, J., Peter-Katalinić, J. (2001), Direct determination of glycosylation sites in O-fucosylated glycopeptides using nano-electrospray quadrupole time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom., 15: 771–777. doi: 10.1002/rcm.298
- Issue published online: 26 APR 2001
- Article first published online: 26 APR 2001
- Manuscript Accepted: 26 MAR 2001
- Manuscript Received: 22 MAR 2001
O-Fucosylation is an unusual posttranslational modification present in several proteins that play important roles in physiological processes such as coagulation, cell signaling and metastasis. Although the exact function of the modification is still unclear, the number of proteins found to be modified is increasing, and there is a need for further structural and functional analyses. Here we report on a rapid and straightforward approach in the analysis of glycosylation status and determination of glycosylation sites in O-fucosylated glycopeptides using nano-electrospray quadrupole time-of-flight (nano-ESI Q-TOF) mass spectrometry. In a single measurement of previously chemically untreated O-fucosylated peptides originating from the thrombospondin-1 repeats, we were able to determine the glycosylation status of the analyzed peptide, the glycosylation site, and the glycan structure. The abundance of glycosylated peptide fragment ions in MS2 spectra suggests that nano-ESI Q-TOF mass spectrometry can be used as a general approach in structural studies of O-fucosylation in proteins. Copyright © 2001 John Wiley & Sons, Ltd.