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- W109025034 abstract "Oxidative metabolism of bilirubin (BR), a breakdown product of haem with cytoprotective and toxic properties, is an important route of detoxification in addition to glucuronidation. Bilirubin oxidases in this alternative disposal mechanism have been suggested and were shown to exist in the hepatic microsomal fractions of rats and mice. Previously, we have demonstrated that the mouse hepatic cytochrome P450 2a5 (Cyp2a5) is predominantly responsible for microsomal oxidation of bilirubin (Abu-Bakar et. al., 2005). In the present study we explore the potential of CYP2A6 (the human orthologue of the mouse Cyp2a5) to catalyse the oxidation of bilirubin in vitro. To achieve the aim we used microsomal fractions from the wild type-yeast and recombinant yeast expressing the human CYP2A6. Western blot analysis and coumarin hydroxylase activity assay showed that CYP2A6 is present in the microsomal fractions of the recombinant yeast but not the wild-type yeast. We also observed moderate difference in bilirubin oxidation rates between the wild type and recombinant yeast microsomes. The rates of bilirubin oxidation for wild type yeast were slower at 59 pmol bilirubin/min/nmol cytochrome P450 compared to that of the recombinant yeast expressing the human CYP2A6 protein at 84.6 pmol bilirubin/min/nmol cytochrome P450. The result suggests that cytochrome P450 isozyme(s) other than the CYP2A6 may contribute to the bilirubin oxidation in vitro. Currently, identification of the oxidative products formed from this reaction is being explored." @default.
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- W109025034 date "2007-01-01" @default.
- W109025034 modified "2023-09-27" @default.
- W109025034 title "Bilirubin Degradation system in Yeast Microsomes: Role of Cytochrome 2A6" @default.
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