The role of porcine thyroid peroxidase and FAD-containing monooxygenase in the metabolism of 1-methyl-2-thioimidazole (methimazole) |
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| Authors: | J R Paterson H T Hood G G Skellern |
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| Institution: | Drug Metabolism Research Unit, Department of Pharmacy, University of Strathclyde, Glasgow G1 1XW, U.K. |
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| Abstract: | The peroxidase and FAD-containing monooxygenase activities of porcine thyroid subcellular preparations were measured and it was observed that FAD-containing monooxygenase activity was considerably lower than that of peroxidase. The end product of 1-methyl-214C]thioimidazole oxidation catalysed by thyroid peroxidase was confirmed to be 1-methylimidazole by mass spectrometry. In the presence of thyroid peroxidase 1-methyl-2-thioimidazole would appear initially to be oxidised to bis(1-methylimidazole)-2,2'-disulphide. The extent of oxidation was dependent on the iodide concentration in the reaction mixture. |
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| Keywords: | αTPI α thiol proteinase inhibitor Bz α-N-benzoyl Z α-N-benzyloxycarbonyl N-Nap 2 naphtylamide L-trans-epoxysuc-cinylleucylamido (4-guanidino) butane |
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