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Purification of MAO A and MAO B from Mammalian Tissue Sources
1Department of Biochemistry, Emory University, Atlanta, GA, USA. deedmon@emory.edu.
Abstract:
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.
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