GLUTATHIONE DEPLETION BY ANILINE ANALOGS <I>IN VITRO</I> ASSOCIATED WITH LIVER MICROSOMAL CYTOCHROME P-450
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概要
- 論文の詳細を見る
Enzymic depletion of glutathione (GSH) <I>in vitro</I> by aniline analogs was mostly dependent on the cytochrome P-450 level in liver microsomes. In a case of acetaminophen (AAP), active metabolite of AAP formed through liver microsomal drug metabolizing enzymes consumed GSH. The active metabolite formed binds, at least in part, covalently to liver microsomal proteins. In addition, species differences in the extent of GSH depletion by AAP <I>in vitro</I> was related to the amounts of the active metabolite of AAP bound covalently to liver microsomal protein(s) by experiments using <SUP>14</SUP>C-AAP. Similar depletion of GSH was also seen with other aniline analogs such as aniline itself and p-chloroaniline, but not with acetanilide, in four animal species. These <I>in vitro</I> results obtained here strongly support the well-known findings concerning both GSH depletion and covalent binding in vivo of the active metabolite after AAP treatment.
- 社団法人 日本薬理学会の論文
著者
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Kitagawa Haruo
Department Of Biochemical Pharmacology Faculty Of Pharmaceutical Sciences Chiba University
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Kobayashi Keiko
Department Of Biochemical Pharmacology Faculty Of Pharmaceutical Sciences Chiba University
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Aikawa Kazuo
Department Of Biochemical Pharmacology Faculty Of Pharmaceutical Sciences Chiba University
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Satoh Tetsuo
Department Of Anesthesiology National Defense Medical College
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KITAGAWA Haruo
Department of Biochemical Pharmacology and Biotoxicology, Faculty of Pharmaceutical Sciences, Chiba University
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