Characterization of glycosylation sites for a recombinant IgG1 monoclonal antibody and a CTLA4-Ig fusion protein by liquid chromatography-mass spectrometry peptide mapping.

@article{Bongers2011CharacterizationOG,
  title={Characterization of glycosylation sites for a recombinant IgG1 monoclonal antibody and a CTLA4-Ig fusion protein by liquid chromatography-mass spectrometry peptide mapping.},
  author={Jacob Bongers and John Devincentis and Jinmei Fu and Peiqing Huang and David H Kirkley and Kirk Leister and Peiran Liu and Richard Ludwig and Kathleen Rumney and Li Tao and Wei Wu and Reb J. Russell},
  journal={Journal of chromatography. A},
  year={2011},
  volume={1218 45},
  pages={8140-9}
}
Liquid chromatography mass spectrometry (LC-MS) peptide mapping can be a versatile technique for characterizing protein glycosylation sites without the need to remove the attached glycans as in conventional oligosaccharide mapping methods. In this way, both N-linked and O-linked sites of glycosylation can each be directly identified, characterized, and quantified by LC-MS as intact glycopeptides in a single experiment. LC-MS peptide mapping of the individual glycosylation sites avoids many of… CONTINUE READING