title: Microassay analyses of protein glycosylation.
abstract: To accurately characterize the carbohydrate moieties of oligosaccharide chains in glycosylated proteins, it is necessary to distinguish exactly which types of oligosaccharides are present at which site. We describe lectin overlay assays, which take advantage of the ability of lectins to distinguish between different types of glycoproteins via recognition of terminal sugars, thus allowing the chain type and peripheral antigenic components to be determined. Three microassays involving lectins are reported in this paper: non-protease-treated intact glycoproteins; glycopeptides released by prior digestion of the glycoprotein and then separated by HPLC; and release of sugars from glycoproteins by hydrazinolysis and then coupling them to a multivalent support.
authors.affiliation: School of Biological & Chemical Sciences, Birkbeck College, University of London, UK.
authors.forename: N K
authors.initials: NK
authors.lastname: Wong
authors.forename: N
authors.initials: N
authors.lastname: Kanu
authors.forename: N
authors.initials: N
authors.lastname: Thandrayen
authors.forename: G J
authors.initials: GJ
authors.lastname: Rademaker
authors.forename: C I
authors.initials: CI
authors.lastname: Baldwin
authors.forename: D V
authors.initials: DV
authors.lastname: Renouf
authors.forename: E F
authors.initials: EF
authors.lastname: Hounsell
mesh_terms: D000595:Amino Acid Sequence; D006031:Glycosylation; D006801:Humans; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
chemical_list: D011506:Proteins; D014357:Trypsin