Determination of site-specific glycan heterogeneity on glycoproteins View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2012-06-07

AUTHORS

Daniel Kolarich, Pia H Jensen, Friedrich Altmann, Nicolle H Packer

ABSTRACT

The comprehensive analysis of protein glycosylation is a major requirement for understanding glycoprotein function in biological systems, and is a prerequisite for producing recombinant glycoprotein therapeutics. This protocol describes workflows for the characterization of glycopeptides and their site-specific heterogeneity, showing examples of the analysis of recombinant human erythropoietin (rHuEPO), α1-proteinase inhibitor (A1PI) and immunoglobulin (IgG). Glycoproteins of interest can be proteolytically digested either in solution or in-gel after electrophoretic separation, and the (glyco)peptides are analyzed by capillary/nano-liquid chromatography–electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS). If required, specific glycopeptide enrichment steps, such as hydrophilic interaction liquid chromatography (HILIC), can also be performed. Particular emphasis is placed on data interpretation and the determination of site-specific glycan heterogeneity. The described workflow takes approximately 3–5 d, including sample preparation and data analysis. The data obtained from analyzing released glycans of rHuEPO and IgG, described in the second protocol of this series (10.1038/nprot.2012.063), provide complementary detailed glycan structural information that facilitates characterization of the glycopeptides. More... »

PAGES

1285-1298

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nprot.2012.062

DOI

http://dx.doi.org/10.1038/nprot.2012.062

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1015648284

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/22678432


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