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Glycobiology vol 2 no 4 pp. 355-359, 1992
© 1992

research-article

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

Gary R. Hayes, Caroline A. Enns1 and John J. Lucas2

Department of Biochemistry and Molecular Biology, SUNY Health Science Center at Syracuse Syracuse, NY 13210, USA
1Department of Cell Biology and Anatomy L2l5, Oregon Health Sciences University Portland, OR 97201, USA

2To whom correspondence should be addressed

Received on April 13, 1992; accepted on May 13, 1992

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.

human placenta O-glycosylation threonine transferrin receptor


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