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

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

doi:10.1093/glycob/2.4.355

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 journal › Article › peer-review

49 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 language	English (US)
Pages (from-to)	355-359
Number of pages	5
Journal	Glycobiology
Volume	2
Issue number	4
DOIs	https://doi.org/10.1093/glycob/2.4.355
State	Published - Aug 1992
Externally published	Yes

Keywords

Human placenta
O-glycosylation
Threonine
Transferrin receptor

ASJC Scopus subject areas

Biochemistry

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10.1093/glycob/2.4.355

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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.",

keywords = "Human placenta, O-glycosylation, Threonine, Transferrin receptor",

author = "Hayes, {Gary R.} and Enns, {Caroline A.} and Lucas, {John J.}",

note = "Funding Information: We express our gratitude to Barbara Root for peptide sequencing and Nick Garigliano for technical assistance. We thank Dr C.E.Costelloof the MIT Mass Spectrometry Facility for performing the mass spectra] analyses. The MIT Mass Spectrometry Facility is supported by the NIH Center for Research Resources Grant No. RR0317, to K.Biemann. This work was supported by NIH Grant GM 43111.",

year = "1992",

month = aug,

doi = "10.1093/glycob/2.4.355",

language = "English (US)",

volume = "2",

pages = "355--359",

journal = "Glycobiology",

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TY - JOUR

T1 - Identification of the O-linked glycosylation site of the human transferrin receptor

AU - Hayes, Gary R.

AU - Enns, Caroline A.

AU - Lucas, John J.

N1 - Funding Information: We express our gratitude to Barbara Root for peptide sequencing and Nick Garigliano for technical assistance. We thank Dr C.E.Costelloof the MIT Mass Spectrometry Facility for performing the mass spectra] analyses. The MIT Mass Spectrometry Facility is supported by the NIH Center for Research Resources Grant No. RR0317, to K.Biemann. This work was supported by NIH Grant GM 43111.

PY - 1992/8

Y1 - 1992/8

N2 - 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.

AB - 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.

KW - Human placenta

KW - O-glycosylation

KW - Threonine

KW - Transferrin receptor

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

Abstract

Keywords

ASJC Scopus subject areas

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