Free radicals and carcinogenesis. Some properties of the nitroxyl free radicals produced by covalent binding of 2-nitrosofluorene to unsaturated lipids of membranes.
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Biomedical subjects
Publications and source records attributed to D L Reigh.
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A peroxidase preparation from rat mammary gland parenchymal cells, a target tissue of arylamine carcinogens, was shown to activate the carcinogen N-hydroxy-2-acetylaminofluorene via a nitroxyl free radical intermediate to the more active carcinogens nitrosofluorene and N-acetoxy-2-acetylaminofluorene. Hydrogen peroxide, cumene hydroperoxide, and linoleic acid hydroperoxide were effective as substrates. The antioxidants ascorbate, propyl gallate and reduced glutathione prevented the free radical activation route.
The kinetics of horseradish peroxidase catalyzed of scopoletin oxidation were observed to be sigmoidal. The apparent KmS for scopoletin is 0.9 mM. Inhibition of scopoletin oxidation by indole-3-acetic acid (IAA) appears to be non competitive. Non competitive inhibition by IAA suggests a more significant role of the peroxidase protein matrix in regulating the activity of the heme moiety.
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