Specificity of hepatic cytochrome P-450 isoenzymes from PCB-treated rats and participation of cytochrome b5 in the activation of aflatoxin B1

Carcinogenesis
Y UenoR Kato

Abstract

Employing six forms of cytochrome P-450s fractionated from the hepatic microsomes of PCB-treated rats, the activation of aflatoxin B1 (AFB1) was examined in the reconstituted cytochrome P-450 system. AFB1 was specifically activated into DNA-binding form by cytochrome P-450 I-a, which is one of P-450 type cytochromes and possesses an absorption peak at 450.0 nm in its carbon monoxide difference spectrum. This activation was enhanced by cytochrome b5 and the maximal enhancement (1.6-fold of the control) was observed with the molar ratio of 0.25 cytochrome b5:1.0 cytochrome P-450.

Citations

Aug 1, 1993·Food and Chemical Toxicology : an International Journal Published for the British Industrial Biological Research Association·T YabeY Ueno
Nov 4, 1986·Biochimica Et Biophysica Acta·A Aström, J W DePierre
Jan 1, 1990·Food Additives and Contaminants·J F NarbonneF Leveque
Jan 1, 1992·Natural Toxins·M SakaiY Ueno
Apr 30, 1985·Biochemical and Biophysical Research Communications·G J DeMarco, G D McCoy
Jun 14, 1985·Biochemical and Biophysical Research Communications·Y Omata, Y Ueno
Nov 30, 1983·Biochemical and Biophysical Research Communications·S YamamotoR Kato
Jan 1, 1985·Critical Reviews in Toxicology·Y Ueno

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