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analysis of protein glycosylation by mass spectrometry
(2016)
  • Susan Rey
Abstract
analysis of protein glycosylation by mass spectrometry, the attachment of sugar moieties to proteins, is a post-translational modification (PTM) that provides greater proteomic diversity than other PTMs. Glycosylation is critical for a wide range of biological processes, including cell attachment to the extracellular matrix and protein-ligand interactions in the cell. This PTM is characterized by various glycosidic linkages, including N-, O- and C-linked glycosylation, glypiation (GPI anchor attachment) and phosphoglycosylation. Glycoproteins can be detected, purified and analyzed by different strategies, including glycan staining and visualization, glycan cross-linking to agarose or magnetic resin for labeling or purification, or proteomic analysis by mass spectrometry, respectively., the attachment of sugar moieties to proteins, is a post-translational modification (PTM) that provides greater proteomic diversity than other PTMs. Glycosylation is critical for a wide range of biological processes, including cell attachment to the extracellular matrix and protein-ligand interactions in the cell. This PTM is characterized by various glycosidic linkages, including N-, O- and C-linked glycosylation, glypiation (GPI anchor attachment) and phosphoglycosylation. Glycoproteins can be detected, purified and analyzed by different strategies, including glycan staining and visualization, glycan cross-linking to agarose or magnetic resin for labeling or purification, or proteomic analysis by mass spectrometry, respectively.
Disciplines
Publication Date
2016
Citation Information
Susan Rey. "analysis of protein glycosylation by mass spectrometry" (2016)
Available at: http://works.bepress.com/susan_rey/21/