Altered glycosylation of human chorionic gonadotropin decreases its hormonal activity as determined by cyclic-adenosine 3',5'-monophosphate production in MA-10 cells.

doi:10.1093/glycob/1.1.45

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Article

Altered glycosylation of human chorionic gonadotropin decreases its hormonal activity as determined by cyclic-adenosine 3',5'-monophosphate production in MA-10 cells.

Glycobiology - 1 Sept 1990

Amano J, Nishimura R, Sato S, Kobata A

Abstract excerpt

Human chorionic gonadotropin (hCG) purified from pooled urine of normal pregnant women contains four asparagine-linked sugar chains and four mucin-type sugar chains. The structures of asparagine-linked sugar chains of this hormone are constant and site-specific. hCGs obtained from the urine of patients with invasive mole or choriocarcinoma have quite different sets of oligosaccharides although the primary...

Topics

Animals
Carbohydrate Sequence
Cell Line
Choriocarcinoma
Chorionic Gonadotropin
Cyclic AMP
Enzyme-Linked Immunosorbent Assay
Female
Genetic Variation
Glycosylation
Humans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Hydatidiform Mole

Leydig Cell Tumor

Mice

Molecular Sequence Data

Neoplasm Invasiveness

Nucleic Acid Conformation

Oligosaccharides

Source

Open in PubMed

Identifiers

PMID: 1967025
DOI: 10.1093/glycob/1.1.45

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1967025-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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