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Review
. 2009 Oct;13(4):421-6.
doi: 10.1016/j.cbpa.2009.07.022. Epub 2009 Aug 21.

Determination of glycosylation sites and site-specific heterogeneity in glycoproteins

Affiliations
Review

Determination of glycosylation sites and site-specific heterogeneity in glycoproteins

Hyun Joo An et al. Curr Opin Chem Biol. 2009 Oct.

Abstract

Glycosylation is one of the most common post-translational modifications (PTMs) of proteins. At least 50% of human proteins are glycosylated with some estimates being as high as 70%. Glycoprotein analysis requires determining both the sites of glycosylation as well as the glycan structures associated with each site. Recent advances have led to the development of new analytical methods that employ mass spectrometry extensively making it possible to obtain the glycosylation site and the site microheterogeneity. These tools will be important for the eventual development of glycoproteomics.

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Figures

Figure 1
Figure 1
The standard approaches to determine site-specific glycosylation employing the specific enzymatic proteolysis. Depending on the nature of the samples used, some of the steps were not always needed (marked with an asterisk (*)). The order of procedures had some variability as well.
Figure 2
Figure 2
The experimental strategy for the determination of glycosylation sites and site-specific heterogeneity using non-specific proteolysis. Glycan information (on the right) is often used to eliminate false positive assignment of specific glycopeptides.

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