PARTIAL PURIFICATION OF PULMONARY CYTOCHROME P-448 FROM 3-METHYLCHOLANTHRENE-TREATED RATS
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概要
- 論文の詳細を見る
Pulmonary cytochrome P-448 from 3-methylcholanthrene-pretreated rats was partially purified approximately 20-fold. The purified preparations containing 1.74 nmol per mg protein were essentially free of NADH-cytochrome b_5 reductase and NADPH-cytochrome c reductase, and included a small amount of cytochrome b_5 spectrophotometrically. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of the partially purified cytochrome P-448 gave one major band and several minor bands when stained with Coomassie blue. The major band on which the presence of peroxidase activity could be determined had the apparent molecular weight of 57,000. In the presence of NADPH-cytochrome c reductase, lipid and NADPH, the pulmonary cytochrome P-448 was active in hydroxylation of benzo-[a] pyrene, but catalyzed N-demethylation of benzphetamine in a slow rate.
- 日本トキシコロジー学会の論文
- 1981-05-25
著者
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ABE Tatsuya
Department of Neurosurgery, Oita Medical University
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Abe Tatsuya
Department Of Neurosurgery Oita University School Of Medicine
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Tamura Yoshiko
Department Of Food Science And Technology School Of Agriculture Nagoya University
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Tamura Yoshiko
Department Of Cancer Chemotherapy And Prevention The Research Institute For Tuberculosis And Cancer
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Watanabe Minro
Department Of Cancer Chemotherapy Research Institute For Tuberculosis And Cancer Tohoku University
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Watanabe Minro
Department Of Cancer Chemotherapy And Prevention The Research Institute For Tuberculosis And Cancer
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Abe Tatsuya
Department Of Biochemistry Kyushu University School Of Medicine
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