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

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

Research output: Contribution to journalArticle

44 Scopus citations

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 1 1992

Keywords

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

ASJC Scopus subject areas

  • Biochemistry

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