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Methyl linoleate ozonide: a substrate for rat glutathione S-transferases
R M Vos1, I M Rietjens, G M Alink
1Department of Toxicology, Agricultural University, Wageningen, The Netherlands.
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.
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