Catechol-O-methyl transferase in mouse liver plasma membranes

June R. Aprille; Daniel F. Malamud

doi:10.1016/0006-291X(75)90833-5

Catechol-O-methyl transferase in mouse liver plasma membranes

June R. Aprille, Daniel F. Malamud

Research output: Contribution to journal › Article › peer-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 language	English (US)
Pages (from-to)	1293-1302
Number of pages	10
Journal	Biochemical and Biophysical Research Communications
Volume	64
Issue number	4
DOIs	https://doi.org/10.1016/0006-291X(75)90833-5
State	Published - Jun 16 1975

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(75)90833-5

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title = "Catechol-O-methyl transferase in mouse liver plasma membranes",

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.",

author = "Aprille, {June R.} and Malamud, {Daniel F.}",

note = "Funding Information: ACKNOWLEDGEMENT: This study was supported grant from the Damon Runyon Foundation. Development Award.",

year = "1975",

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doi = "10.1016/0006-291X(75)90833-5",

language = "English (US)",

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T1 - Catechol-O-methyl transferase in mouse liver plasma membranes

AU - Aprille, June R.

AU - Malamud, Daniel F.

N1 - Funding Information: ACKNOWLEDGEMENT: This study was supported grant from the Damon Runyon Foundation. Development Award.

PY - 1975/6/16

Y1 - 1975/6/16

N2 - 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.

AB - 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.

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JO - Biochemical and Biophysical Research Communications

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Catechol-O-methyl transferase in mouse liver plasma membranes

Abstract

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