Alteration of N-linked oligosaccharide structures of human chorionic gonadotropin beta-subunit by disruption of disulfide bonds.

doi:10.1023/a:1018593805890

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Article

Alteration of N-linked oligosaccharide structures of human chorionic gonadotropin beta-subunit by disruption of disulfide bonds.

Glycoconjugate journal - 1 Feb 1997

Moriwaki T, Suganuma N, Furuhashi M, Kikkawa F, Tomoda Y, Boime I, Nakata M, Mizuochi T

Abstract excerpt

The human chorionic gonadotropin beta-subunit (hCGbeta) is a glycoprotein in which 12 cysteine residues pair to form six intramolecular disulfide bonds. In order to elucidate the effect of each disulfide bond on glycosylation of the molecule, we analysed structures of asparagine-linked oligosacch...

Topics

Acetylglucosamine
Alanine
Animals
CHO Cells
Chorionic Gonadotropin, beta Subunit, Human
Chromatography, High Pressure Liquid
Cricetinae
Cysteine
Disulfides
Electrophoresis, Polyacrylamide Gel
Galactose
Glycosylation
Humans
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase

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PMID: 9111139
DOI: 10.1023/a:1018593805890

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9111139-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Mutation

Neuraminidase

Oligosaccharides

Protein Conformation