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- W249326039 abstract "ABSTRACT The metabolism of Procarbazine ( N -isopropyl- p -[ N' -methylhydrazino methyl]-benzamide) and other hydrazine derivatives has been studied using purified pig liver microsomal amine oxidase and rat liver microsomal fractions. The substrate specificity of the purified amine oxidase for hydrazines was studied; 1,1-dimethyl- and 1-methyl-1-phenylhydrazine were two of the best substrates. The metabolism of 1,1-dimethylhydrazine by liver microsomes has been shown to be dependent on the amine oxidase present in these fractions. Conversely, several other hydrazine derivatives, including Procarbazine, are metabolized exclusively by the cytochrome P-450-dependent monooxygenase of liver microsomal fractions. These results further support the observation that two major monooxygenases, the liver microsomal amine oxidase and the cytochrome P-450-dependent enzyme system, are involved in the metabolism of many nitrogenous compounds, including hydrazine derivatives." @default.
- W249326039 created "2016-06-24" @default.
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- W249326039 date "1977-01-01" @default.
- W249326039 modified "2023-10-05" @default.
- W249326039 title "THE MICROSOMAL METABOLISM OF CARCINOGENIC AND/OR THERAPEUTIC HYDRAZINES" @default.
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- W249326039 doi "https://doi.org/10.1016/b978-0-08-021523-5.50070-5" @default.
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