O-Acetylation is one of the major modifications of sialic acids that significantly alters biological properties of the parent molecule. These O-acetylated forms are components of the cellular membrane and can affect physiological and pathological responses. Understanding the role of N-glycans in physiology is of increasing relevance to cellular biologists in various disciplines who study glycoproteomics yet lack information regarding the function of the attached glycans. However, permethylation, the most common mass spectrometric analytical means, leads to the loss of O-linked acetyl groups in sialic acids. In this chapter, we demonstrated that O-acetylation of sialic acid in Atlantic salmon serum N-glycan can be well investigated by capillary electrophoresis-mass spectrometry.
CITATION STYLE
Liu, X., & Afonso, L. (2010). Is permethylation strategy always applicable to protein N-glycosylation study?: A case study on the O-acetylation of sialic acid in fish serum glycans. Methods in Molecular Biology (Clifton, N.J.), 600, 259–268. https://doi.org/10.1007/978-1-60761-454-8_18
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