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- W2091744010 abstract "The sequential metabolic pathway leading to the arylation of proteins by the carcinogen, N-2-fiuorenylacetamide, has been studied in rat liver slices in vitro. The differential binding of 14C-labeled N-2-fluorenylacetamide, N-(1-hydroxy-2-fluorenyl) acetamide, and 2-amino-1-fluorenol to the proteins of the various liver cell fractions indicated that metabolism to the o-hydroxy derivative was required for protein binding. Comparison of the protein-labeling pattern of acetyl-14C- and 1-14C-labeled N-(1-hydroxy-2-fluorenyl) acetamide conclusively demonstrated that deacetylation preceded the protein arylation reaction. The microsomal and mitochondrial proteins were more selectively labeled than the soluble proteins, although the soluble proteins were likewise radioactive when liver slices were incubated with 1-14C-labeled N-(1-hydroxy-2-fluorenyl) acetamide. The binding to mitochondrial proteins was very likely catalyzed by mitochondrial cytochrome c-cytochrome oxidase, since, in a model system, cytochrome c-cytochrome oxidase catalyzed the oxidative arylation of 2-amino-l-fluorenol to exogenously added bovine serum albumin." @default.
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- W2091744010 date "1964-05-01" @default.
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- W2091744010 title "The biological arylation of proteins in vitro by a metabolite of the carcinogen N-2-fluorenylacetamide" @default.
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- W2091744010 doi "https://doi.org/10.1016/0006-2952(64)90007-3" @default.
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