The effect of debrisoquin on MAO A and MAO B activities

M. A. Javors, M. E. Bembenek, C. L. Bowden, C. W. Abell, J. W. Maas

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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 μM and liver MAO B with a Ki value of 8.8 μM, 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.

Original languageEnglish (US)
Pages (from-to)2359-2364
Number of pages6
JournalLife Sciences
Volume45
Issue number24
DOIs
StatePublished - 1989

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ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

Cite this

Javors, M. A., Bembenek, M. E., Bowden, C. L., Abell, C. W., & Maas, J. W. (1989). The effect of debrisoquin on MAO A and MAO B activities. Life Sciences, 45(24), 2359-2364. https://doi.org/10.1016/0024-3205(89)90118-5