Variation in the expression of Mu-class glutathione S-transferase isoenzymes from human skeletal muscle. Evidence for the existence of heterodimers.

doi:10.1042/bj2730323

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Article

Variation in the expression of Mu-class glutathione S-transferase isoenzymes from human skeletal muscle. Evidence for the existence of heterodimers.

The Biochemical journal - 15 Jan 1991

Hussey A J, Kerr L A, Cronshaw A D, Harrison D J, Hayes J D

Abstract excerpt

The cytosolic glutathione S-transferases (GST) from human skeletal muscle were purified by a combination of affinity chromatography and anion-exchange chromatography followed by either chromatofocusing or hydroxyapatite chromatography. Pi-class and Mu-class GST, but not Alpha-class GST, were isolated from muscle. In addition to a Pi-class GST subunit, which exists as a homodimer, this tissue also contains a total...

Topics

Aged
Aged, 80 and over
Amino Acid Sequence
Chromatography, Affinity
Cyanogen Bromide
Dinitrochlorobenzene
Female
Gene Expression
Genetic Variation
Glutathione Transferase
Humans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Isoenzymes

Macromolecular Substances

Molecular Sequence Data

Molecular Weight

Multigene Family

Muscles

Protein Conformation

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PMID: 1991033
DOI: 10.1042/bj2730323
PMCID: PMC1149849

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1991033-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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