On the inhibitory action of mersalyl on microsomal drug oxidation: A rigid organization of the electron transport chain

The organic mercurial, mersalyl, causes a 50% inhibition of TPNH-cytochrome c reductase activity, TPNH-cytochrome P-450 reductase activity, and ethylmorphine N-demethylation in rat liver microsomes at concentrations of about 25 mμmoles/mg microsomal protein. The K"i (mersalyl) proved to be independ... Ausführliche Beschreibung

1. Person: Franklin, M.R.
Weitere Personen: Estabrook, R.W.
Quelle: in Archives of Biochemistry and Biophysics Vol. 143, No. 1 (1971), p. 318-329
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Format: Online-Artikel
Sprache: English
Veröffentlicht: 1971
Beschreibung: Online-Ressource
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Anmerkung: Copyright: Copyright (c) 2005 Elsevier (USA)
Zusammenfassung: The organic mercurial, mersalyl, causes a 50% inhibition of TPNH-cytochrome c reductase activity, TPNH-cytochrome P-450 reductase activity, and ethylmorphine N-demethylation in rat liver microsomes at concentrations of about 25 mμmoles/mg microsomal protein. The K"i (mersalyl) proved to be independent of whether the overall hydroxylation activity was enhanced by the addition of DPNH, or an increased ionic strength; or was inhibited by carbon monoxide. Mersalyl, at a concentration of 25 mμmoles/mg protein, caused no extensive conversion of cytochrome P-450 to P-420. Studies on the pattern of inhibition suggest a rigid electron-transport system linking a single molecule of TPNH-cytochrome c reductase to a number of molecules of cytochrome P-450 contained within a multicomponent complex and that reducing equivalents can be transferred only within a single enzyme complex with no demonstrable electron transfer interactions between the components of different complexes.
ISSN: 0003-9861

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