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

Gary R. Hayes, Caroline Enns, John J. Lucas

Research output: Contribution to journalArticle

41 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)355-359
Number of pages5
JournalGlycobiology
Volume2
Issue number4
DOIs
StatePublished - Aug 1992
Externally publishedYes

Fingerprint

Glycosylation
Transferrin Receptors
Receptor
Amino acids
Amino Acids
Glycoproteins
Glycoprotein
Glycopeptides
High-performance Liquid Chromatography
Protein Sequence Analysis
Sequence Analysis
N-Acetylneuraminic Acid
Amino Acid Sequence
Chromatography
Spectral Analysis
Spectrum analysis
Reverse
Digestion
High Pressure Liquid Chromatography
Acids

Keywords

  • Human placenta
  • O-glycosylation
  • Threonine
  • Transferrin receptor

ASJC Scopus subject areas

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Public Health, Environmental and Occupational Health
  • Neuropsychology and Physiological Psychology
  • Hematology
  • Biochemistry

Cite this

Identification of the O-linked glycosylation site of the human transferrin receptor. / Hayes, Gary R.; Enns, Caroline; Lucas, John J.

In: Glycobiology, Vol. 2, No. 4, 08.1992, p. 355-359.

Research output: Contribution to journalArticle

Hayes, Gary R. ; Enns, Caroline ; Lucas, John J. / Identification of the O-linked glycosylation site of the human transferrin receptor. In: Glycobiology. 1992 ; Vol. 2, No. 4. pp. 355-359.
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