Maximizing coverage of glycosylation heterogeneity in MALDI-MS analysis of glycoproteins with up to 27 glycosylation sites.

@article{Zhang2008MaximizingCO,
  title={Maximizing coverage of glycosylation heterogeneity in MALDI-MS analysis of glycoproteins with up to 27 glycosylation sites.},
  author={Ying Zhang and Eden P. Go and Heather Desaire},
  journal={Analytical chemistry},
  year={2008},
  volume={80 9},
  pages={3144-58}
}
Glycosylation affects various biological functions of proteins (e.g., protein binding, inter- or intracell signaling, etc.), and it can serve as an indicator of disease. Therefore, characterization of the glycosylation in proteins is one important step in developing a comprehensive understanding of the biological significance of glycosylation and in facilitating disease diagnosis. Glycopeptide-based MS analysis has proven to be a viable tool for glycopeptide analysis. However, when… CONTINUE READING

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