Catechol-O-methyl transferase in mouse liver plasma membranes

June R. Aprille, Daniel F. Malamud

Research output: Contribution to journalArticlepeer-review

Abstract

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
Volume64
Issue number4
DOIs
StatePublished - Jun 16 1975

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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