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

doi:10.1016/0024-3205(89)90118-5

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

Department of Psychiatry & Behavioral Sciences

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

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 language	English (US)
Pages (from-to)	2359-2364
Number of pages	6
Journal	Life Sciences
Volume	45
Issue number	24
DOIs	https://doi.org/10.1016/0024-3205(89)90118-5
State	Published - 1989

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology
General Pharmacology, Toxicology and Pharmaceutics

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10.1016/0024-3205(89)90118-5

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title = "The effect of debrisoquin on MAO A and MAO B activities",

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.",

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T1 - The effect of debrisoquin on MAO A and MAO B activities

AU - Javors, M. A.

AU - Bembenek, M. E.

AU - Bowden, C. L.

AU - Abell, C. W.

AU - Maas, J. W.

PY - 1989

Y1 - 1989

N2 - 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.

AB - 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.

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EP - 2364

JO - Life Sciences

JF - Life Sciences

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ER -

The effect of debrisoquin on MAO A and MAO B activities

Abstract

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