The effect of debrisoquin on MAO A and MAO B activities

Life Sci. 1989;45(24):2359-64. doi: 10.1016/0024-3205(89)90118-5.

Abstract

To examine the mode of action of debrisoquin (DEB), we studied the effect of this drug in vitro on MAO A and MAO B enzyme activities. DEB was shown to be a competitive inhibitor of highly purified human MAO A and MAO B enzyme activities. DEB inhibited placental MAO A with a Ki value of 0.5 microM and liver MAO B with a Ki value of 8.8 microM, 18-fold greater effect on the A form. Kynuramine was used as substrate for both enzymes. Additional studies using a dilution technique showed that DEB was a reversible inhibitor of both forms of the enzyme. The results of this study show that DEB is a potent competitive and reversible inhibitor of both MAO A and MAO B enzymes.

MeSH terms

  • Biogenic Amines / metabolism
  • Debrisoquin / pharmacology*
  • Female
  • Humans
  • Isoquinolines / pharmacology*
  • Kinetics
  • Kynuramine / metabolism
  • Monoamine Oxidase Inhibitors / pharmacology*
  • Placenta / enzymology
  • Pregnancy

Substances

  • Biogenic Amines
  • Isoquinolines
  • Monoamine Oxidase Inhibitors
  • Kynuramine
  • Debrisoquin