Metabolism of aromatic amines by prostaglandin H synthase.

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Metabolism of aromatic amines by prostaglandin H synthase.

The metabolism of aromatic amines by the peroxidase activity of prostaglandin H synthase (PHS) has been studied in this laboratory by use of two model compounds, the carcinogenic primary amine 2-aminofluorene (2-AF) and the substituted amine aminopyrine (AP). 2-AF is oxidized by PHS to 2, 2-azobisfluorene, 2-aminodifluorenylamine, 2-nitrofluorene, polymeric material, and products covalently bou...

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Bladder and Kidney Prostaglandin H Synthase Metabolic Activation of Carcinogenic Aromatic Amines by Dog

Microsomal enzyme preparations from dog liver, kidney, and bladder were used to assess the prostaglandin H synthasecatalyzed activation of carcinogenic aromatic amines to bind covalently to proteins and nucleic acids. Benzidine, a urinary bladder carcinogen, bound to protein of bladder transitional epithelial and renal inner and outer medullary microsomes and was dependent upon addition of arac...

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Metabolic activation of carcinogenic aromatic amines by dog bladder and kidney prostaglandin H synthase.

Microsomal enzyme preparations from dog liver, kidney, and bladder were used to assess the prostaglandin H synthase-catalyzed activation of carcinogenic aromatic amines to bind covalently to proteins and nucleic acids. Benzidine, a urinary bladder carcinogen, bound to protein of bladder transitional epithelial and renal inner and outer medullary microsomes and was dependent upon addition of ara...

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Prostaglandin H synthase-dependent mutagenic activation of heterocyclic aromatic amines of the IQ-type.

Microsomes from ram seminal vesicles known as a rich source of prostaglandin H synthase (PHS) activate the food mutagen IQ (2-amino-3-methylimidazo[4,5-f]quinoline) to (a) product(s) mutagenic in Salmonella typhimurium TA98. The activation is dependent on the PHS cofactor arachidonic acid and is strongly inhibited by the PHS inhibitor indomethacin. In this system, the mutagenic potency of IQ is...

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Metabolic Activation of Carcinogenic Aromatic Amines by Dog Bladder and Kidney Prostaglandin H Synthase1

Microsomal enzyme preparations from dog liver, kidney, and bladder were used to assess the prostaglandin H synthasecatalyzed activation of carcinogenic aromatic amines to bind covalently to proteins and nucleic acids. Benzidine, a urinary bladder carcinogen, bound to protein of bladder transitional epithelial and renal inner and outer medullary microsomes and was dependent upon addition of arac...

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ژورنال

عنوان ژورنال: Environmental Health Perspectives

سال: 1985

ISSN: 0091-6765,1552-9924

DOI: 10.1289/ehp.856445