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Issue 4, 2015
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PNGase F-mediated incorporation of 18O into glycans for relative glycan quantitation

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Abstract

PNGase F-catalyzed glycosylation site 18O-labeling is a widely used method for glycoprotein quantitation owing to its efficiency and simplicity. However, PNGase F-catalyzed glycan 18O-labeling, which offers advantages for glycomics, has not yet been developed. In this study, PNGase F-mediated incorporation of 18O into glycans during the N-glycan release from glycoproteins by PNGase F was finally realized, named as PCGOL (PNGase F-catalyzed glycan 18O-labeling), which offers a potential strategy for relative glycan quantitation. This new method showed good linearity and high reproducibility within at least 2 orders of magnitude in the dynamic range. Furthermore, PCGOL combined with our previously developed TOSIL method (tandem 18O stable isotope labeling for N-glycoproteome quantitation) can be used for comprehensive N-glycosylation quantification, achieving simultaneous quantification of glycans, glycopeptides and glycoproteins in a single workflow, which was also used to analyze glycosylation changes in immunoglobulin G (IgG) associated with hepatocellular carcinoma in the present work.

Graphical abstract: PNGase F-mediated incorporation of 18O into glycans for relative glycan quantitation

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Supplementary files

Article information


Submitted
11 Nov 2014
Accepted
03 Dec 2014
First published
03 Dec 2014

Analyst, 2015,140, 1082-1089
Article type
Paper
Author version available

PNGase F-mediated incorporation of 18O into glycans for relative glycan quantitation

W. Zhang, W. Cao, J. Huang, H. Wang, J. Wang, C. Xie and P. Yang, Analyst, 2015, 140, 1082
DOI: 10.1039/C4AN02073A

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