High affinity of 2,3,4,7,8-pentachlorodibenzofuran to cytochrome P-450 in the hepatic microsomes of rats |
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| Affiliation: | 1. Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok, Thailand;2. Department of Biochemistry, Faculty of Science, Burapha University, Chonburi, Thailand;3. Department of Chemistry, Faculty of Science, Burapha University, Chonburi, Thailand;4. Center for Innovation in Chemistry, Burapha University, Chonburi, Thailand |
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| 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. |
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