|
pubmed:abstractText |
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.
|
