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Glycomics

Mass spectrometry based glycomics methods seek to identify the role of protein glycosylation, a ubiquitous class of PTMs in higher organisms. Glycomics methods are applied at the protein level to establish the range of N- and O-linked glycosylation sites and structures present, or alternatively, the glycans may be released from proteins to gain an overview or quantitative profile of all glycans present in a sample. A secondary goal of released glycan analysis is to structurally characterize the branched structures using tandem (MS/MS) or multi-stage (MSn) mass spectrometry. Our lab is particularly interested in O-linked glycosylation and O-glycoproteomics by working with NEB’s new O-glycoprotease IMPa, an enzyme uniquely enabling the characterization of complex O-glycosylated proteins for site-specific O-glycosylation analyses. The lab is additionally working on Mass Spectrometry Imaging (MSI) by applying NEB glycosidases to various tissue types and substrates.

Graph of relative abundance vs. time with peaks marked by yellow and purple symbols, showing a major peak at 15 minutes.

The chromatogram shows released O-glycan separation from Bovine Fetuin after reductive beta-elimination, permethylation, reversed phase LC-MS/MS.