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- W2025846504 abstract "In this report, we have examined the origin of the electrophilic chlorine formed during the microsomal metabolism of carbon tetrachloride and the possibility that liver microsomal proteins catalyze chloroperoxidase or myeloperoxidase halogenation reactions. Studies with stable isotopes of chlorine show that at least 99% of the trapped chlorine originated from carbon tetrachloride. When hydrogen peroxide or cumene hydroperoxide was added to liver microsomes in the presence of chloride ion, no trapped chlorine was observed. Thus, cytochrome P-450 does not catalyze chloroperoxidase type chloride ion oxidation but instead catalyzes a reaction leading to cleavage of a carbon-chlorine bond with concomitant chlorine atom oxidation." @default.
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- W2025846504 date "1982-07-01" @default.
- W2025846504 modified "2023-09-28" @default.
- W2025846504 title "Metabolism of carbon tetrachloride to electrophilic chlorine by liver microsomes: Exclusion of cytochrome P-450 catalyzed chloroperoxidase reaction" @default.
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- W2025846504 doi "https://doi.org/10.1016/0006-291x(82)91664-3" @default.
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