Chapter title |
Ethyl Esterification for MALDI-MS Analysis of Protein Glycosylation.
|
---|---|
Chapter number | 11 |
Book title |
Proteomics in Systems Biology
|
Published in |
Methods in molecular biology, January 2016
|
DOI | 10.1007/978-1-4939-3341-9_11 |
Pubmed ID | |
Book ISBNs |
978-1-4939-3339-6, 978-1-4939-3341-9
|
Authors |
Karli R. Reiding, Emanuela Lonardi, Agnes L. Hipgrave Ederveen, Manfred Wuhrer |
Editors |
Jörg Reinders |
Abstract |
Ethyl esterification is a technique for the chemical modification of sialylated glycans, leading to enhanced stability when performing matrix-assisted laser desorption/ionization (MALDI)-mass spectrometry (MS), as well as allowing the efficient detection of both sialylated and non-sialylated glycans in positive ion mode. In addition, the method shows specific reaction products for α2,3- and α2,6-linked sialic acids, leading to an MS distinguishable mass difference. Here, we describe the ethyl esterification protocol for 96 glycan samples, including enzymatic N-glycan release, the aforementioned ethyl esterification, glycan enrichment, MALDI target preparation, and the MS(/MS) measurement. |
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