2-Aminobenzoyl誘導体の水酸化反応に関与するタンパク性因子と薬物代謝酵素活性

概要

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2-Aminobenzamide is hardly hydroxylated with the microsome-NADPH system and was found to require the protein factor contained in the soluble fraction. The action of this protein factor on the microsome enzyme system has hardly any effect on the demethylation of aminopyrine or hydroxylation of aniline, but showed a marked acceleration on hydroxylation of 3- or 5-position in compounds possessing a 2-aminobenzoyl skeleton. This protein factor also inhibited the lipid peroxidation of microsomes in the NADPH-added system or NADPH-Fe^<2+> added system. On the other hand, this protein factor showed almost no effect on the reduction of oxidized type cytochrome c, dichlorophenol-indophenol, and potassium ferricyanide by the NADPH-cytochrome c reductase, but showed a marked inhibition on the formation of red neotetrazolium formazan in the Triton X-100 added system and the reduction of cytochrome c by xanthine oxidase, indicating that this protein factor possessed the superoxide dismutase activity.
社団法人日本薬学会の論文
1974-10-25