Membrane-bound phosphotyrosyl-protein phosphatase activity in human erythrocytes. Dephosphorylation of membrane band 3 protein.
Human erythrocyte membranes exhibit, in addition to "acid" p-nitrophenyl-phosphatase activity, remarkable phosphotyrosyl-protein phosphatase activity, assayed on synthetic polymer poly (Glu-Tyr) 4:1, previously phosphorylated on Tyr residues by rat spleen tyrosine-protein kinase. The results reported here indicate that such a 32P-Tyr-phosphatase activity, rather than p-nitrophenyl-phosphatase, is involved in the dephosphorylation of transmembrane band 3 protein on 32P-tyrosine residues.
D009597:4-Nitrophenylphosphatase / Q000032:analysis; D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000032:analysis*; D006801:Humans; D010749:Phosphoprotein Phosphatases / Q000032:analysis*; D010766:Phosphorylation; D017027:Protein Tyrosine Phosphatases; D014443:Tyrosine / Q000378:metabolism
D001457:Anion Exchange Protein 1, Erythrocyte; D014443:Tyrosine; D010749:Phosphoprotein Phosphatases; D009597:4-Nitrophenylphosphatase; D017027:Protein Tyrosine Phosphatases