Procedures are described for the purification of the mitochondrial-bound enzymes human and bovine monoamine oxidases A and B (MAO A and B) from placental and liver tissue sources, respectively. Enzyme purification follows isolation of the mitochondria and preparation of outer membrane particles. The membrane-bound enzymes are solubilized by treatment of membranes with phospholipases and detergent extraction. Functional bovine MAO B is purified by polymer fractionation and differential centrifugation. Functional human MAO A is purified by ion-exchange DEAE-Sepharose chromatography.
CITATION STYLE
Edmondson, D. E. (2023). Purification of MAO A and MAO B from Mammalian Tissue Sources. In Methods in Molecular Biology (Vol. 2558, pp. 1–10). Humana Press Inc. https://doi.org/10.1007/978-1-0716-2643-6_1
Mendeley helps you to discover research relevant for your work.