Methods for analysis of O-linked modifications on epidermal growth factor-like and thrombospondin type 1 repeats.
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.
Nita-Lazar
Aleksandra
A
Department of Biochemistry and Cell Biology, SUNY at Stony Brook, Stony Brook, New York, USA.
Haltiwanger
Robert S
RS
D000818:Animals; D001671:Biochemistry / Q000379:methods*; D004815:Epidermal Growth Factor / Q000032:analysis / Q000737:chemistry*; D010100:Oxygen / Q000737:chemistry*; D019700:Thrombospondin 1 / Q000032:analysis / Q000737:chemistry*
D019700:Thrombospondin 1; D004815:Epidermal Growth Factor; D010100:Oxygen