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Article

A novel glycosylation phenotype expressed by Lec23, a Chinese hamster ovary mutant deficient in alpha-glucosidase I.

The Journal of biological chemistry - 5 Dec 1991

Ray M K, Yang J, Sundaram S, Stanley P

Abstract excerpt

Lec23 Chinese hamster ovary (CHO) cells have been shown to possess a unique lectin resistance phenotype and genotype compared with previously isolated CHO glycosylation mutants (Stanley, P., Sallustio, S., Krag, S. S., and Dunn, B. (1990) Somatic Cell Mol. Genet. 16, 211-223). In this paper, a biochemical basis for the lec23 mutation is identified. The carbohydrates associated with the G glycoprotein of vesicular...

Topics

1-Deoxynojirimycin
Animals
CHO Cells
Carbohydrate Metabolism
Carbohydrate Sequence
Chromatography, Affinity
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Concanavalin A
Cricetinae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Glucosamine

Glucose

Glycosylation

Kinetics

Magnetic Resonance Spectroscopy

Membrane Glycoproteins

Molecular Sequence Data

Mutation

Source

Identifiers

PMID: 1660460

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1660460-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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A novel glycosylation phenotype expressed by Lec23, a Chinese hamster ovary mutant deficient in alpha-glucosidase I.PMID 1660460Read ↗

The Lec23 Chinese hamster ovary mutant is a sensitive host for detecting mutations in alpha-glucosidase I that give rise to congenital disorder of glycosylation IIb (CDG IIb).Semantic proximity Read ↗

Glycomics profiling of Chinese hamster ovary cell glycosylation mutants reveals N-glycans of a novel size and complexity.Semantic proximity Read ↗

A subclass of cell surface carbohydrates revealed by a CHO mutant with two glycosylation mutations.Semantic proximity Read ↗

LEC14, a dominant Chinese hamster ovary glycosylation mutant expresses complex N-glycans with a new N-acetylglucosamine residue in the core region.Semantic proximity Read ↗

A mutation causing a reduced level of expression of six beta4-galactosyltransferase genes is the basis of the Lec19 CHO glycosylation mutant.Semantic proximity Read ↗

LEC18, a dominant Chinese hamster ovary glycosylation mutant synthesizes N-linked carbohydrates with a novel core structure.Semantic proximity Read ↗

Expression cloning of a novel suppressor of the Lec15 and Lec35 glycosylation mutations of Chinese hamster ovary cells.Semantic proximity Read ↗

Reduced utilization of Man5GlcNAc2-P-P-lipid in a Lec9 mutant of Chinese hamster ovary cells: analysis of the steps in oligosaccharide-lipid assembly.Semantic proximity Read ↗

Five Lec1 CHO cell mutants have distinct Mgat1 gene mutations that encode truncated N-acetylglucosaminyltransferase I.Semantic proximity Read ↗

Gain-of-function Chinese hamster ovary mutants LEC18 and LEC14 each express a novel N-acetylglucosaminyltransferase activity.Semantic proximity Read ↗

Isolation of new CHO cell mutants defective in CMP-sialic acid biosynthesis and transport.Semantic proximity Read ↗

Lec3 Chinese hamster ovary mutants lack UDP-N-acetylglucosamine 2-epimerase activity because of mutations in the epimerase domain of the Gne gene.Semantic proximity Read ↗

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