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Article

Characterization of iduronate sulphatase mutants affecting N-glycosylation sites and the cysteine-84 residue.

The Biochemical journal - 15 Aug 1997

Millat G, Froissart R, Maire I, Bozon D

Abstract excerpt

Iduronate sulphatase (IDS) is responsible for mucopolysaccharidosis type II, a rare recessive X-linked lysosomal storage disease. The aim of this work was to evaluate the functional importance of each N-glycosylation site, and of the cysteine-84 residue. IDS mutant cDNAs, lacking one of the eight potential N-glycosylation sites, were expressed in COS cells. Although each of the potential sites was used, none of...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 9337875
DOI: 10.1042/bj3260243
PMCID: PMC1218661

Genes

IDS

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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