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

Barwell, C.J. and Ebrahimi, S.A. (1994) Some problems associated with measuring monoamine oxidase activity in the presence of sodium azide. Journal of Neural Transmission, Supplement (41). pp. 35-39.

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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- 1,2,4-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.

Item Type: Article
Additional Information: cited By 2
Uncontrolled Keywords: amine oxidase (flavin containing) benzylamine; amitrole; catalase; hydrogen peroxide; sodium azide; unclassified drug; amine oxidase (flavin containing); azide; benzaldehyde; benzaldehyde derivative; benzylamine; benzylamine derivative, animal tissue; colorimetry; conference paper; controlled study; enzyme activity; liver; male; nonhuman; priority journal; rat; animal; article; deamination; drug effect; enzymology; liver mitochondrion; metabolism; rat strain, Amitrole; Animal; Azides; Benzaldehydes; Benzylamines; Catalase; Colorimetry; Deamination; Hydrogen Peroxide; Male; Mitochondria, Liver; Monoamine Oxidase; Rats; Rats, Wistar; Sodium Azide; Support, Non-U.S. Gov't
Depositing User: EPrints System Admin
Date Deposited: 19 Jul 2017 10:13
Last Modified: 19 Jul 2017 10:13

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