title: Identification of the O-linked glycosylation site of the human transferrin receptor.
abstract: The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites. Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site. Amino acid sequence analysis reveals that the site of O-glycosylation is Thr-104. Mass spectral analysis is consistent with the presence of a Gal-GalNAc core with predominantly two sialic acid residues.
authors.affiliation: Department of Biochemistry and Molecular Biology, SUNY Health Science Center, Syracuse 13210.
authors.forename: G R
authors.initials: GR
authors.lastname: Hayes
authors.forename: C A
authors.initials: CA
authors.lastname: Enns
authors.forename: J J
authors.initials: JJ
authors.lastname: Lucas
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D002236:Carbohydrate Conformation; D005260:Female; D006023:Glycoproteins / Q000737:chemistry*; D006031:Glycosylation; D006801:Humans; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010920:Placenta / Q000737:chemistry; D011990:Receptors, Transferrin / Q000737:chemistry*; D013912:Threonine / Q000378:metabolism; D014357:Trypsin
chemical_list: D006023:Glycoproteins; D010446:Peptide Fragments; D011990:Receptors, Transferrin; D013912:Threonine; D014357:Trypsin