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

doi:10.1074/jbc.271.13.7484

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Article

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

The Journal of biological chemistry - 29 Mar 1996

Raju T S, Stanley P

Abstract excerpt

The Chinese hamster ovary cell (CHO) glycosylation mutant, LEC14, was previously selected for resistance to pea lectin (Pisum sativum agglutinin) and shown to behave dominantly. The lectin resistance properties of LEC14 cells are related to, but distinct from, those of LEC18, a dominant Chinese h...

Topics

Acetylglucosamine
Animals
CHO Cells
Carbohydrate Conformation
Carbohydrate Sequence
Cell Membrane
Chromatography, Affinity
Cricetinae
Glycopeptides
Glycosylation
Lectins
Magnetic Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Methylation

Molecular Sequence Data

Monosaccharides

Mutation

Plant Lectins

Polysaccharides

Source

Open in PubMed

Identifiers

PMID: 8631778
DOI: 10.1074/jbc.271.13.7484

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8631778-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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LEC14, a dominant Chinese hamster ovary glycosylation mutant expresses complex N-glycans with a new N-acetylglucosamine residue in the core region.PMID 8631778Read ↗

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

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

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 ↗

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

Independent Lec1A CHO glycosylation mutants arise from point mutations in N-acetylglucosaminyltransferase I that reduce affinity for both substrates. Molecular consequences based on the crystal structure of GlcNAc-TI.Semantic proximity Read ↗

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

CHO cells provide access to novel N-glycans and developmentally regulated glycosyltransferases.Semantic proximity Read ↗

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

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