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Some problems associated with measuring monoamine oxidase activity in the presence of sodium azide

  • C. J. Barwell
  • S. A. Ebrahimi
Part of the Journal of Neural Transmission book series (NEURAL SUPPL, volume 41)

Summary

The colourimetric assay of monoamine oxidase activity, as hydrogen peroxide production, normally requires the use of sodium azide to inhibit breakdown of hydrogen peroxide by catalase. Sodium azide was shown to act as an uncompetitive inhibitor of benzylamine deamination with an inhibitor constant of 1.5 mM. Catalase activity of isolated rat liver mitochondria could be eliminated with the irreversible inhibitor of catalase, 3-amino-l,2,4-triazole. The treatment did not affect benzylamine deaminating activity. The catalase-free preparation could be used to assay monoamine oxidase activity colourimetrically, as hydrogen peroxide production, in the absence of sodium azide.

Keywords

Catalase Activity Sodium Azide Inhibitor Constant Monoamine Oxidase Activity Uncompetitive Inhibitor 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Margoliash E, Novogrodsky A, Schejter A (1960) Irreversible reaction of 3-amino-l:2:4-triazole and related inhibitors with the protein of catalase. Biochem J 74: 339–348.PubMedGoogle Scholar
  2. Szutowicz A, Kobes RD, Orsulak PJ (1983) Colorimetric assay for monoamine oxidase in tissues using peroxidase and 2,2′-azinodi(3-ethylbenzthiazoline-6-sulphonic acid) as chromogen. Anal Biochem 138: 86–94.CrossRefGoogle Scholar
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  4. Tipton KF, Youdim MBH (1983) Methods in biogenic amine research, 1st edn. Elsevier, Amsterdam, p 441.Google Scholar

Copyright information

© Springer-Verlag 1994

Authors and Affiliations

  • C. J. Barwell
    • 1
  • S. A. Ebrahimi
    • 1
  1. 1.School of Pharmacy and Biomedical SciencesUniversity of PortsmouthPortsmouthUK

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