Catechol-O-methyl transferase in mouse liver plasma membranes

June R. Aprille, Daniel Malamud

Research output: Contribution to journalArticle

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

Fingerprint

Guaiacol
Enzyme activity
Cell membranes
Transferases
Liver
Membrane Proteins
Cell Membrane
Enzymes
Fractionation
Cytosol
Norepinephrine
Membranes
Cell Fractionation
Isoelectric Focusing
Catalytic Domain
catechol
polidocanol
lubrol

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Catechol-O-methyl transferase in mouse liver plasma membranes. / Aprille, June R.; Malamud, Daniel.

In: Biochemical and Biophysical Research Communications, Vol. 64, No. 4, 16.06.1975, p. 1293-1302.

Research output: Contribution to journalArticle

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