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Article

Allosteric communication in mammalian muscle aldolase.

The Biochemical journal - 1 Nov 1997

Sygusch J, Beaudry D

Abstract excerpt

Mixed disulphide formation in the presence of oxidized glutathione reversibly inactivates rabbit skeletal muscle aldolase. Inactivation is allosteric, preferentially modifying Cys-72 on the surface of the aldolase homotetramer distant from active-site locations and subunit interfaces. Ion-exchange chromatography fractionates partly inactivated aldolase into three distinct enzymic species: unmodified enzyme,...

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Identifiers

PMID: 9581547
DOI: 10.1042/bj3270717
PMCID: PMC1218848

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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