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  • Title: [Effect of solubilization by methylethyl ketone of mitochondrial monoamine oxidase of the rat liver on the kinetic properties of the enzyme].
    Author: Volkovitskaia OE, Severina IS.
    Journal: Biokhimiia; 1984 Sep; 49(9):1502-9. PubMed ID: 6518192.
    Abstract:
    The values of Km and V for serotonin, tyramine and beta-phenylethylamine deamination by solubilized and partially purified preparations of monoamine oxidase (MAO) from rat liver were determined. As a result of MAO solubilization by methylethylketone, 14% of activity localized in the mitochondria passed into solution. Subsequent chromatography on AH-Sepharose 4B resulted in 27-fold purification of the enzyme with a 9% yield. In experiments with membrane-bound and partially purified MAO, the Km and V values were shown to increase non-competitively with a rise in O2 concentration. In contrast with intact mitochondria, the use of partially purified MAO preparations led to a loss of the enzyme sensitivity to O2 depending on the nature of the amine. The dependence of kinetic properties of MAO on the lipid environment of mitochondrial membranes is discussed.
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