Identification of the O-linked glycosylation site of the human transferrin receptor

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 se...

Full description

Saved in:
Bibliographic Details
Published inGlycobiology (Oxford) Vol. 2; no. 4; p. 355
Main Authors Hayes, G R, Enns, C A, Lucas, J J
Format Journal Article
LanguageEnglish
Published England 01.08.1992
Subjects
Amino Acid Sequence
Binding Sites
Carbohydrate Conformation
Female
Glycoproteins - chemistry
Glycosylation
Humans
Mass Spectrometry
Molecular Sequence Data
Peptide Fragments - chemistry
Placenta - chemistry
Receptors, Transferrin - chemistry
Threonine - metabolism
Trypsin
Online AccessGet more information

Cover

More Information
Summary: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.
ISSN:0959-6658
DOI:10.1093/glycob/2.4.355