Epidermal growth factor-stimulated phosphorylation of tyrosine residues on a 120 000 dalton protein in mouse liver plasma membrane subfractions

The addition of Epidermal growth factor (EGF) to mouse liver sinusoidal plasma membrane subfractions, isolated from the blood face of hepatocytes, resulted in a two to threefold increase of 32P incorporation from [γ- 32P ]ATP into a 120 000 dalton protein component. The EGF-stimulation of the phosph...

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Veröffentlicht in:Biochemical and biophysical research communications 1981-09, Vol.102 (2), p.602-609
Hauptverfasser: Ehrhart, Jean-Claude, Creuzet, Claudine, Rollet, Emmanuelle, Loeb, Jacques
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container_title Biochemical and biophysical research communications
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creator Ehrhart, Jean-Claude
Creuzet, Claudine
Rollet, Emmanuelle
Loeb, Jacques
description The addition of Epidermal growth factor (EGF) to mouse liver sinusoidal plasma membrane subfractions, isolated from the blood face of hepatocytes, resulted in a two to threefold increase of 32P incorporation from [γ- 32P ]ATP into a 120 000 dalton protein component. The EGF-stimulation of the phosphorylation of this component was also evidenced in plasma membranes derived from the lateral and biliary faces of hepatocytes. A major phosphoamino acid residue after EGF stimulation was identified as tyrosine. An EGF-enhancement of the phosphorylation of threonine and serine residues also appears to be detectable.
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subjects Animals
Cell Membrane - metabolism
Electrophoresis, Polyacrylamide Gel
Epidermal Growth Factor - pharmacology
Female
Liver - metabolism
Membrane Proteins - metabolism
Mice
Molecular Weight
Phosphorylation
Tyrosine
title Epidermal growth factor-stimulated phosphorylation of tyrosine residues on a 120 000 dalton protein in mouse liver plasma membrane subfractions
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