| Literature DB >> 3449385 |
R M Vos1, I M Rietjens, G M Alink, P J van Bladeren.
Abstract
Glutathione S-transferases (GST) were shown to be capable of reducing the toxicity of the ozonide of methyl linoleate (MLO) by catalyzing its reaction with reduced glutathione (GSH). MLO was a substrate for both cytosolic and microsomal GST. Isoenzyme 2-2 demonstrated the highest specific activity. Oxidised glutathione and aldehydes were identified as products of the reaction, with unstable glutathione-conjugates being formed as intermediates only. It was concluded that the GST-activity toward MLO may be similar to the GST-peroxidase activity with lipid hydroperoxides as substrates.Entities:
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Year: 1987 PMID： 3449385 DOI： 10.1007/BF03189912
Source DB: PubMed Journal: Eur J Drug Metab Pharmacokinet ISSN： 0378-7966 Impact factor: 2.441