Insulin stimulates phosphorylation of serine residues in soluble insulin receptors

Using lectin affinity-purified receptor preparations from human hepatoma cells, insulin (10 −7M) specifically stimulated phosphorylation of the 95,000 dalton (beta) subunit of its own receptor. Phospho-amino acid analysis of the receptor subunit revealed that insulin increased at least 2.5-fold the...

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Veröffentlicht in:	Biochemical and biophysical research communications 1983-11, Vol.116 (3), p.1129-1135
Hauptverfasser:	Zick, Yehiel, Grunberger, George, Podskalny, Judith M., Moncada, Victoria, Taylor, Simeon I., Gorden, Phillip, Roth, Jesse
Format:	Artikel
Sprache:	eng
Schlagworte:	Carcinoma, Hepatocellular - metabolism Cell Line Humans Insulin - pharmacology Kinetics Liver Neoplasms - metabolism Molecular Weight Phosphorylation Receptor, Insulin - drug effects Receptor, Insulin - isolation & purification Receptor, Insulin - metabolism Serine
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