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    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. © 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

    Citation

    Dale E Edmondson. Purification of MAO A and MAO B from Mammalian Tissue Sources. Methods in molecular biology (Clifton, N.J.). 2023;2558:1-10

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    PMID: 36169851

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