Lipoprotein lipaseBethesda: a single amino acid substitution (Ala-176----Thr) leads to abnormal heparin binding and loss of enzymic activity.

doi:10.1073/pnas.87.9.3474

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Article

Lipoprotein lipaseBethesda: a single amino acid substitution (Ala-176----Thr) leads to abnormal heparin binding and loss of enzymic activity.

Proceedings of the National Academy of Sciences of the United States of America - 1 May 1990

Beg O U, Meng M S, Skarlatos S I, Previato L, Brunzell J D, Brewer H B, Fojo S S

Abstract excerpt

The molecular defect that leads to a deficiency of lipoprotein lipase (LPL) activity in the proband from a Bethesda kindred has been identified. The pre- and post-heparin plasma LPL mass in the proband was elevated when compared to controls; however, there was no detectable LPL activity, indicating the presence of a defective enzyme (termed LPLBethesda). Analysis of the patient's post-heparin plasma by...

Topics

Adult
Alanine
Amino Acid Sequence
Base Sequence
Chromatography, Affinity
DNA
Heparin
Humans
Leukocytes
Lipoprotein Lipase
Macrophages

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Male

Molecular Sequence Data

Mutation

Plasmids

Polymerase Chain Reaction

Protein Binding

Reference Values

Source

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Identifiers

PMID: 2110364
DOI: 10.1073/pnas.87.9.3474
PMCID: PMC53923

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2110364-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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