Schiel, J.
(2012),
Glycoprotein Analysis Using Mass Spectrometry: Unraveling the Layers of Complexity, Analytical and Bioanalytical Chemistry
(Accessed February 17, 2026)
Official websites use .gov
A .gov website belongs to an official government organization in the United States.
Secure .gov websites use HTTPS
A lock (
) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.
Glycoprotein Analysis Using Mass Spectrometry: Unraveling the Layers of Complexity
Published
Author(s)
Abstract
It is generally understood that DNA serves as the direct template that eventually encodes a protein responsible for biochemical function. Alterations of a protein after synthesis (post-translational modifications, PTMs) can play a large role in a proteins form and function. Glycosylation is the most abundant PTM and arises from the addition of carbohydrates (glycans) to a protein. The inherent complexity of this PTM has resulted in glycan measurement lagging behind that of other biochemical polymers, despite the enormous impact glycosylation confers. The following review describes the various levels of glycan structure that can be measured with mass spectrometry techniques. Each stage of analysis reveals another layer of biochemical complexity, which correlates to a new level of analytical scrutiny. The recent trends toward improving glycoanalytical throughput and measurement science are highlighted.Citation
Analytical and Bioanalytical Chemistry
Volume
404
Pub Type
Journals
Keywords
Glycoprotein, Glycan, Mass Spectrometry, Standards
Citation
Issues
If you have any questions about this publication or are having problems accessing it, please contact [email protected].
Created June 12, 2012, Updated February 19, 2017