Assigning glycosylation sites and microheterogeneities in glycoproteins by liquid chromatography/tandem mass spectrometry

• Published in: Methods in molecular biology (Clifton, N.J.) Vol. 492; p. 161
• Main Authors: Mechref, Yehia, Madera, Milan, Novotny, Milos V
• Format: Journal Article
• Language: English
• Published: United States 2009
• Subjects: alpha-Fetoproteins - analysis; alpha-Fetoproteins - chemistry; alpha-Fetoproteins - metabolism; Amino Acid Sequence; Animals; Binding Sites; Cattle; Chromatography, Affinity; Chromatography, Liquid - methods; Glycopeptides - analysis; Glycopeptides - chemistry; Glycopeptides - metabolism; Glycoproteins - analysis; Glycoproteins - chemistry; Glycoproteins - metabolism; Glycosylation; Lectins - chemistry; Molecular Sequence Data; Silicon Dioxide - chemistry; Tandem Mass Spectrometry - methods; Trypsin - metabolism

Glycosylation of proteins is one of the most common posttranslational modifications which has its bearing on function and biological activity. Assigning the glycosylation sites and their inherent microheterogeneities are key structural issues addressing various glycoprotein functions. This chapter d...