An automated method for determining glycosylation and site diversity in glycoproteins

Hyun Joo An, John Tillinghast, Carlito B Lebrilla

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

The determination of glycosylation sites and oligosaccharide heterogeneity is key toward understanding the biological roles of glycoproteins. There are no previous methods that can reliably detetermine the site of glycosylation and the glycan heterogeneity at specific sites. We have developed a procedure for the determination of glycosylation sites and oligosaccharide heterogeneity in glycoproteins. The method is based on a combination of nonspecific proteolysis, deglycosylation, and high mass accuracy mass spectrometry analysis. The glycoprotein was proteolytically degraded using a nonspecific protease into glycopeptide fragments. The exact peptide mass was calculated by subtracting the glycan mass from the observed glycopeptide mass. The amino acid sequence of a matched peptide mass was identified from the protein database. A computer program, GlycoX, was developed in MATLAB to aid in the determination of the glycosylation sites and oligosaccharide heterogeneity in glycoproteins.

Original languageEnglish (US)
Title of host publicationACS Symposium Series
PublisherAmerican Chemical Society
Pages241-250
Number of pages10
Volume990
ISBN (Print)9780841274402
DOIs
StatePublished - Sep 1 2008

Publication series

NameACS Symposium Series
Volume990
ISSN (Print)00976156
ISSN (Electronic)19475918

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

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  • Cite this

    An, H. J., Tillinghast, J., & Lebrilla, C. B. (2008). An automated method for determining glycosylation and site diversity in glycoproteins. In ACS Symposium Series (Vol. 990, pp. 241-250). (ACS Symposium Series; Vol. 990). American Chemical Society. https://doi.org/10.1021/bk-2008-0990.ch011