Purification of the epidermal growth factor receptor by tyrosine-Sepharose affinity chromatography.
The EGF receptor has been purified from human epidermoid carcinoma A431 cells by affinity chromatography on wheat germ agglutinin-agarose and tyrosine-Sepharose. The purified EGF receptor was shown to be homogeneous by SDS-polyacrylamide gel electrophoresis and possessed EGF-sensitive tyrosine kinase activity. Kinetic analysis of the autophosphorylation indicated that approximately 1.4 mol of phosphate was incorporated per mol of the EGF receptor. When a synthetic tyrosine-containing peptide was used as a phosphorylatable substrate, the specific activity of the EGF-stimulated kinase was 66 nmol/min/mg.
D002294:Carcinoma, Squamous Cell / Q000032:analysis*; D002460:Cell Line; D002462:Cell Membrane / Q000032:analysis; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D066246:ErbB Receptors; D006801:Humans; D007700:Kinetics; D010766:Phosphorylation; D011956:Receptors, Cell Surface / Q000302:isolation & purification* / Q000378:metabolism; D012685:Sepharose; D014443:Tyrosine
D011956:Receptors, Cell Surface; D014443:Tyrosine; D012685:Sepharose; D066246:ErbB Receptors