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Published on: April 1, 2019
Methods for analysis of O-linked modifications on epidermal growth factor-like and thrombospondin type 1 repeats
Aleksandra Nita-Lazar1, Robert S Haltiwanger
1Department of Biochemistry and Cell Biology, SUNY at Stony Brook, Stony Brook, New York, USA.
Abstract:
The identification of novel forms of O-linked glycosylation on epidermal growth factor and thrombospondin type 1 repeats, and their emerging functional significance, require the development of new methods for their analysis. This chapter describes detailed methods to analyze both the structure and the site of modification of O-fucose and O-glucose glycans on proteins. These methods use both traditional biochemical methods of carbohydrate composition analysis and electrospray ionization-mass spectrometry of glycopeptides.
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Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
