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dc.contributor.authorElexpuru, Ana-
dc.contributor.authorSoriano, Montserrat-
dc.contributor.authorVillalobo, Antonio-
dc.identifierdoi: 10.1515/bchm3.1994.375.4.293-
dc.identifierissn: 0177-3593-
dc.identifiere-issn: 1437-4315-
dc.identifier.citationBiological Chemistry Hoppe-Seyler 375(4): 293-298 (1993)-
dc.description.abstractWe have identified the 170 kDa epidermal growth factor (EGF) receptor in crude membrane fractions isolated from Ehrlich ascites tumor cells by its EGF-dependent phosphorylation with [γ-32Ρ]ΑΤΡ. An apparent affinity constant for the ligand of 40-50 ΠΜ, based on the extent of its EGF-dependent phosphorylation, was calculated. [125I]EGF binds to the 170 kDa receptor and Scatchard plot analysis shows high affinity and low affinity KC,S of 1.7 ΠΜ and 24 ΠΜ, respectively, in whole cells, and 0.2-0.8ΠΜ and 39-116nM, respectively, in isolated non-phosphorylated membrane fractions. We have estimated the presence of 48 χ 103 high affinity and 275 x103 low affinity EGF binding sites per tumor cell. Phosphoamino acid analysis shows EGFdependent phosphorylation of tyrosine and serine residues. A polyclonal antibody to a human EGF receptor/c-eroB-2 product common cytoplasmic domain epitope immunoprecipitates a 45 kDa phosphopolypeptide from the tumor membrane fractions and from whole cell lysates. Phosphoamino acid analysis of the immunoprecipitated 45 kDa phosphopolypeptide shows the presence of phosphoserine. The immunoprecipitated 45 kDa polypeptide is able to undergo EGF-independent phosphorylation, although no significant protein kinase activity towards exogenous substrates is detected.-
dc.description.sponsorshipThis work was supported by grants to A.V. from the Comisión Interministerial de Ciencia y Tecnología (SAF392/93), and from the Secretaria de Educación de la Comunidad de Madrid (C174/90 and 366/92).-
dc.publisherWalter de Gruyter-
dc.titleCharacterization of the epidermal growth factor receptor from Ehrlich ascites tumor cells-
dc.description.versionPeer Reviewed-
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