Methyl linoleate ozonide: a substrate for rat glutathione S-transferases.

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.