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- W2430607462 abstract "Synthesis of microsomal cytochrome P- 450 in rat liver requires synthesis of apoprotein in rough endoplasmic reticulum and of heme in mitochondria. Dissociation of apoprotein and heme synthesis by con- comitant treatment of rats with inducers of cytochrome P- 450 (i.e., phenobarbital) and inhibitors of heme synthesis (i.e., cobalt) resulted in a relative excess of apocytochrome P-450. Under these circumstances, it was possible to re- constitute the holocytochrome by addition of hemin in vitro. The holocytochrome was detected spectrophoto- metrically by its CO-binding properties and functionally by its increased oxidative activity. Heme-mediated recon- stitution was most efficient in cell fractions rich in mito- chondria-rough endoplasmic reticulum complexes (640 X g fraction), suggesting that the structural association of these two organelles may represent a functional unit es- sential for the synthesis of holocytochrome P-450. These findings indicate that phenobarbital-mediated induction of apocytochrome P-450 is independent of heme syn- thesis. It is suggested that synthesis of the apocytochrome may be the primary and rate-limiting event in the forma- tion of cytochrome P-450." @default.
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- W2430607462 date "2016-01-01" @default.
- W2430607462 modified "2023-09-26" @default.
- W2430607462 title "Apocytochrome P-450: Reconstitution of" @default.
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