Abstract
MAO activity measurement can be monitored by direct peroxidase-free assays following different spectroscopy methods. Typically, these are assays that follow the conversion of different MAO substrates into its corresponding products monitored in either absorbance or fluorescence. Herein, we describe the assays for enzyme activity assessment with MAO B and particularly the MAO A substrate kynuramine, as well as the MAO B substrate benzylamine. Moreover, we also describe MAO activity determination using the tertiary amine substrate allyl amine 1-methyl-4-(1-methyl-1 H-pyrrol-2-yl)-1,2,3,6-tetrahydropyridine (MMTP). These are very useful methods for the investigation of MAO inhibitory activity by molecules known to be HRP-interfering. In the present chapter we demonstrate the application of these methods in MAO activity and Michaelis-Menten curve determinations as well as inhibitory activity experiments.
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Reis, J., Binda, C. (2023). Measurement of MAO Enzymatic Activity by Spectrophotometric Direct Assays. In: Binda, C. (eds) Monoamine Oxidase. Methods in Molecular Biology, vol 2558. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-2643-6_4
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DOI: https://doi.org/10.1007/978-1-0716-2643-6_4
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