MAO activity measurement is generally performed following different spectroscopy methods, in most cases using peroxidase as a coupled reaction catalyst. In the presence of horseradish peroxidase (HRP), the assay follows the oxidation of the typical MAO substrate (aromatic amines) which generates hydrogen peroxide as a secondary product. There are several chromogens and fluorogens that, in the presence of hydrogen peroxide, are converted by HRP to detectable products. In the present chapter we describe the spectrophotometric 4-aminoantipyrine assay as well as the fluorogenic assay with the Amplex® Red chemical probe. These methods are applied on MAO activity and Michaelis-Menten curve determinations as well as inhibitory activity experiments.
CITATION STYLE
Reis, J., & Binda, C. (2023). The Peroxidase-Coupled Assay to Measure MAO Enzymatic Activity. In Methods in Molecular Biology (Vol. 2558, pp. 23–34). Humana Press Inc. https://doi.org/10.1007/978-1-0716-2643-6_3
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