Catechol-O-methyl transferase in mouse liver plasma membranes

June R. Aprille, Daniel F. Malamud

    Research output: Contribution to journalArticlepeer-review


    Catechol-o-methyl transferase is usually localized predominantly in the cytosol fraction of cells, but fractionation of mouse liver showed plasma membranes contain ∼ 70% of the total enzyme activity and have a specific activity ∼ 10x greater than the cytosol fraction. Treatment of the membrane fraction with Lubrol-PX solubilized 47% of the membrane protein and 95% of the enzyme activity. A comparison of Lubrol-solubilized enzyme and [3H]norepinephrine binding activities in a variety of experimental conditions suggest binding is not related to interaction with the active site of catechol-o-methyl transferase. Isoelectric focusing of solubilized membrane proteins showed the enzyme has an isoelectric pH of 4.5-4.8.

    Original languageEnglish (US)
    Pages (from-to)1293-1302
    Number of pages10
    JournalBiochemical and Biophysical Research Communications
    Issue number4
    StatePublished - Jun 16 1975

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology


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