ArticleThe Biochemical journal2001
Purification and characterization of a glutathione S-transferase Omega in pig: evidence for two distinct organ-specific transcripts.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 23 citations in OpenAlex.
- Clonorchis sinensis omega-class glutathione transferases play major roles in the protection of the reproductive system during maturation and the response to oxidative stress.Parasites & vectors · 2016Article
- A novel Omega-class glutathione S-transferase gene in Apis cerana cerana: molecular characterisation of GSTO2 and its protective effects in oxidative stress.Cell stress & chaperones · 2013Article
- A peroxisomal glutathione transferase of Saccharomyces cerevisiae is functionally related to sulfur amino acid metabolism.Eukaryotic cell · 2006Article
- Saccharomyces cerevisiae cells have three Omega class glutathione S-transferases acting as 1-Cys thiol transferases.The Biochemical journal · 2006Article
- Reduction of anti-leishmanial pentavalent antimonial drugs by a parasite-specific thiol-dependent reductase, TDR1.The Biochemical journal · 2004Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
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Abstract
A cytosolic glutathione S-transferase (GST, EC 2.5.1.18) from the recently characterized Omega class [GSTO; Board et al. 2000, J. Biol. Chem. 275, 24798-24806] has been identified in pig organs. It was found widely distributed in the different tissues investigated and especially abundant in liver and muscle. The hepatic enzyme has been purified to homogeneity by using its selective affinity for S-hexylglutathione over GSH, thus providing a simple method to isolate mammalian GSTO. The dimeric protein has a subunit molecular mass of 27328 Da as measured by electrospray ionization MS. Internal peptide sequencing and complete cDNA sequencing revealed strong similarities with its human recombinant orthologue and two rodent GST-like proteins with the ability to catalyse the GSH-dependent reduction of dehydroascorbate. Additional similarities, including the presence of a specific N-terminal extension and of immunological cross-reactivity, support the results. Moreover, this gene encoding GSTO generates two organ-specific transcripts, suggesting transcriptional mechanisms with a significance that is as yet uncharacterized.
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