J. Kuroki, N. Koga, H. Yoshimura
1986
Citations
1
Influential Citations
52
Citations
Journal
Chemosphere
Abstract
The interaction of 2,3,4,7,8-pentachlorodibenzofuran (PenCDF) with cytochrome P-450 isozymes was studied in male Wistar rats using 14C-labeled PenCDF. Three forms of cytochrome P-450 isozymes, P-448 H, P-448 L and P-452, were purified to homogeneity from 14C-PenCDF-treated rat liver microsomes. The purified P-448 H contained 0.847 mole of PenCDF per mole of the hemoprotein, whereas the amounts of PenCDF bound to P-448 L and P-452 were far less than that to P-448 H. These results suggest that cytochrome P-450, particularly P-448 H, functions as the storage site of PenCDF in the rat liver.