Summary
Incubation of rat cytochrome b5 (D-b5) with rat liver microsomes resulted in specific binding of the hemoprotein. The bound hemoprotein was rapidly reduced by NADH. The NADH cytochrome c reductase activity in these preparations increased in proportion to the amount of cytochrome. In contrast to D-b5, which inhibited N-demethylation and the NADH synergism, the binding of cytochrome b5 preparations, reconstituted from heme and apocyto-chrome b5 had no effect on either the NADPH-dependent N-demethylation of aminopyrine or ethylmorphine or the NADH synergism observed with rat liver microsomes. In addition, manganese protoporphyrin-apocytochrome complex, when bound to microsomes in amounts equivalent to D-b5, showed no effect on N-demethylation activity. These results suggest that homogeneous cytochrome b5 contains contaminating amounts of tightly bound detergent which presumably is removed during the extraction of the heme from the apocytochrome.
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© 1975 Plenum Press, New York
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Cinti, D.L., Ozols, J. (1975). The Role of Cytochrome b5 in Mixed Function Oxidations: Effect of Microsomal Binding of the Hemoprotein on Hepatic N-Demethylations. In: Cooper, D.Y., Rosenthal, O., Snyder, R., Witmer, C. (eds) Cytochromes P-450 and b5 . Advances in Experimental Medicine and Biology, vol 58. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9026-2_32
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DOI: https://doi.org/10.1007/978-1-4615-9026-2_32
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