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Modulation of rabbit and human hepatic cytochrome P-450-catalyzed steroid hydroxylations by alpha-naphthoflavone

Academic Article
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Overview

authors

  • Schwab, G. E.
  • Raucy, J. L.
  • Johnson, Eric

publication date

  • May 1988

journal

  • Molecular Pharmacology  Journal

abstract

  • Rifampicin induces cytochrome P-450 3c, progesterone 16 alpha- and 6 beta-hydroxylation, 17 beta-estradiol 2-hydroxylation, benzo[a] pyrene hydroxylation, and erythromycin N-demethylation in rabbit liver microsomes. Kinetic analysis of the 6 beta-hydroxylation of progesterone as catalyzed by liver microsomes prepared from rifampicin-treated B/J rabbits exhibits a curvilinear double-reciprocal plot, suggestive of substrate activation. Further experimentation demonstrated that alpha-naphthoflavone could augment the catalytic efficiency [Vmax/Km] observed for the 16 alpha- and 6 beta-hydroxylation of progesterone and the 2-hydroxylation of 17 beta-estradiol, whereas erythromycin N-demethylase activity was partially inhibited. Allosteric activation of these steroid hydroxylases by alpha-naphthoflavone is also found for human liver microsomes, indicating that the activation of these enzymes is conserved in man and rabbit.

subject areas

  • Allosteric Regulation
  • Animals
  • Benzoflavones
  • Cytochrome P-450 Enzyme System
  • Enzyme Activation
  • Estradiol
  • Flavonoids
  • Humans
  • In Vitro Techniques
  • Kinetics
  • Microsomes, Liver
  • Progesterone
  • Rabbits
  • Rifampin
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Identity

International Standard Serial Number (ISSN)

  • 0026-895X

PubMed ID

  • 3367901
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Additional Document Info

start page

  • 493

end page

  • 499

volume

  • 33

issue

  • 5

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