Issue 6, 2008
From the journal:

Analyst

Glycopeptide analysis by mass spectrometry

Dilusha S. Dalpathadoa  and  Heather Desaire*a  

* Corresponding authors

a Department of Chemistry, University of Kansas, Lawrence, KS 66045, USA
E-mail: hdesaire@ku.edu
Fax: +1 785-864-5396
Tel: +1 785-864-3015

Abstract

Glycosylation is one of the most important post-translational modifications found in nature. Identifying and characterizing glycans is an important step in correlating glycosylation structure to the glycan's function, both in normal glycoproteins and those that are modified in a disease state. Glycans on a protein can be characterized by a variety of methods. This review focuses on the mass spectral analysis of glycopeptides, after subjecting the glycoprotein to proteolysis. This analytical approach is useful in characterizing glycan heterogeneity and correlating glycan compositions to their attachment sites on the protein. The information obtained from this approach can serve as the foundation for understanding how glycan compositions affect protein function, in both normal and aberrant glycoproteins.

Graphical abstract: Glycopeptide analysis by mass spectrometry

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Article information

DOI
https://doi.org/10.1039/B713816D
Article type
Tutorial Review
First published
19 Mar 2008

Analyst, 2008,133, 731-738

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Glycopeptide analysis by mass spectrometry

D. S. Dalpathado and H. Desaire, Analyst, 2008, 133, 731 DOI: 10.1039/B713816D

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