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 | |
| State | Published - Jun 16 1975 |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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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 journal › Article
}
TY - JOUR
T1 - Catechol-O-methyl transferase in mouse liver plasma membranes
AU - Aprille, June R.
AU - Malamud, Daniel
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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UR - http://www.scopus.com/inward/citedby.url?scp=0016810686&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(75)90833-5
DO - 10.1016/0006-291X(75)90833-5
M3 - Article
VL - 64
SP - 1293
EP - 1302
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 4
ER -