Methyl linoleate ozonide: a substrate for rat glutathione S-transferases |
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| Authors: | R M Vos I M Rietjens G M Alink P J van Bladeren |
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| Affiliation: | Department of Toxicology, Agricultural University, Wageningen, The Netherlands. |
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| 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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