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Article

Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase.

Proceedings of the National Academy of Sciences of the United States of America - 1 Apr 1991

Mononen I, Heisterkamp N, Kaartinen V, Williams J C, Yates J R, Griffin P R, Hood L E, Groffen J

Abstract excerpt

Aspartylglycosaminuria is an inherited lysosomal storage disease caused by deficiency of glycoasparaginase (EC 3.5.1.26) and occurs with higher frequency among Finns than other populations. We have purified human glycoasparaginase and determined about 90% of the amino acid sequence of its light subunit and greater than 70% of that of its heavy subunit by Edman degradation and mass spectrometry. Additional...

Topics

Amino Acid Sequence
Aspartylglucosylaminase
Base Sequence
Codon
Finland
Humans
Leukocytes
Macromolecular Substances
Metabolism, Inborn Errors
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Nucleic Acid Hybridization

Oligonucleotide Probes

Polymerase Chain Reaction

Source

Open in PubMed Open full text

Identifiers

PMID: 2011603
DOI: 10.1073/pnas.88.7.2941
PMCID: PMC51356

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2011603-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase.PMID 2011603Read ↗

Aspartylglycosaminuria in a non-Finnish patient caused by a donor splice mutation in the glycoasparaginase gene.Semantic proximity Read ↗

Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163----Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits.Semantic proximity Read ↗

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