Author index to volume 154 |
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Authors: | Peter Moldéus,Peter J. O Brien,Hj?rdis Thor,Margareta Berggren,Sten Orrenius |
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Affiliation: | Department of Forensic Medicine, Karolinska Institutet, Box 60400, S-104 01 Stockholm, Sweden |
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Abstract: | Horseradish peroxidase-catalyzed N-demethylation of aminopyrine and dimethylaniline results in generation of free radical intermediates which can interact with glutathione (GSH) to form a glutathione radical. This can either dimerize to yield glutathione disulfide or react with O2 to form oxygenated products of glutathione. Ethylmorphine is not a substrate in the peroxidase-mediated reaction, and free radical intermediates which react with GSH, are not formed from aminopyrine and dimethylaniline when the horseradish peroxidase/H2O2 system is replaced by liver microsomes and NADPH. Therefore, it appears unlikely that formation of free radical intermediates can be responsible for the depletion of GSH observed during N-demethylation of several drugs in isolated liver cells. |
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Keywords: | Glutathione Thiol oxidase γ-Glutamyl transferase Tubular epithelium Renal cell Plasma membrane |
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