Studies on monoamine oxidase; Report 8, Solubilization and purification of mitochondrial monoamine oxidase

Abstract

Monoamine oxidase (MAO) in hog kidney was found mainly in mitochondrial fraction and about 60 % of the enzyme in mitochondria was solubilized by a treatment of 1 % sodium cholate and ammonium sulfate fractionation. The specific activity of purified MAO was about 10-fold than that of the homogenate. PS maximum of the purified MAO was found at 2.0 and pH optimum was found at 8.0 in case of tyramine used as substrate. The administration of Fe⁺⁺ and Cu⁺⁺ in the system caused inhibition, however, NaN₃ caused marked activation of the enzymic activity.