Table of Contents

Purification of MAO A and of MAO B from Mammalian Tissue Sources.- Purification of Recombinant Eukaryotic MAO A and MAO B Utilizing the Pichia pastoris Expression System.- The Peroxidase-Coupled Assay to Measure MAO Enzymatic Activity.- Measurement of MAO Enzymatic Activity by Spectrophotometric Direct Assays.- Radiochemical Assay of Monoamine Oxidase Activity.- MAO Visible Spectroscopy for Ligand Interactions, Redox Chemistry, and Kinetics of Irreversible Inhibition.- Conventional Receptor Radioligand Binding Techniques Applied to the Study of Monoamine Oxidase.- Assay of MAO Inhibition by Chromatographic Techniques (HPLC/HPLC-MS).- Crystallization of Human Monoamine Oxidase B.- Detecting Monoamine Oxidase A and B Proteins: A Western Blotting Protocol and Some Practical Considerations.- An (Immune)Fluorescence Protocol for Monitoring Monoamine Oxidase A/B Protein Distribution within the Cell.- Expression and Function of MAO A in Cardiac Cells by Means of Adenovirus-Mediated Gene-Transfer.- In Vitro and In Vivo Assays Characterizing MAO A Function in Cancers.- In Vivo Study of Monoamine Oxidases Using Multisite Intracerebral Microdialysis.- Informed Use of 3D-QSAR for the Rational Design of Coumarin Derivatives as Potent and Selective MAO B Inhibitors.- Hansch-Type QSAR Models for the Rational Design of MAO Inhibitors: Basic Principles and Methodology.- Computational Chemistry and Molecular Modeling of Reversible MAO Inhibitors.