Purified tyrosine kinases, the EGF receptor kinase and the src kinase, can catalyze the phosphorylation of the band 3 protein from human erythrocytes.
The band 3 glycoprotein from human erythrocytes was found to be phosphorylated on tyrosine residues by the purified EGF receptor kinase and the purified src kinase in vitro. Kinetic analysis revealed that Km of the band 3 protein phosphorylation by the EGF receptor kinase was 0.17 microM and 0.65 microM in the absence and presence of EGF (3 X 10(-7)M), respectively, and that in the case of the src kinase it was 0.4 microM. From these data the band 3 protein can be regarded as one of the best substrates common for the EGF receptor kinase and the src kinase in vitro.
D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism*; D004815:Epidermal Growth Factor / Q000378:metabolism; D066246:ErbB Receptors; D004912:Erythrocytes / Q000378:metabolism; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D015688:Oncogene Protein pp60(v-src); D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism*; D012191:Retroviridae Proteins / Q000378:metabolism*; D013379:Substrate Specificity
D001457:Anion Exchange Protein 1, Erythrocyte; D011956:Receptors, Cell Surface; D012191:Retroviridae Proteins; D004815:Epidermal Growth Factor; D066246:ErbB Receptors; D011505:Protein-Tyrosine Kinases; D015688:Oncogene Protein pp60(v-src)