Tyrosine phosphorylation of cytosolic proteins in human erythrocytes.
Some cytosolic proteins of human erythrocytes can be phosphorylated on tyrosine residues by endogenous Tyr-protein kinase(s). Their phosphorylation is enhanced by addition of Tyr-protein kinase, purified from human erythrocyte cytosol. The most phosphorylatable is a 19 kDa protein. Its phosphorylation is more activated by Mn2+ than by Mg2+. It is inhibited by NaC1, 2,3-bisphosphoglycerate and by heparin. Similar response to the above effectors is exhibited by the phosphorylation of the other protein bands. However, the phosphorylation of a 73 kDa double band, which is negligible in the absence of added NaC1, is stimulated by this salt.
Clari
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G
Dipartimento Chimica Biologica, Università Padova, Italy.
Dalla Libera
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L
Moret
V
V
D001345:Autoradiography; D001798:Blood Proteins / Q000302:isolation & purification / Q000378:metabolism*; D003600:Cytosol / Q000201:enzymology; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000097:blood*; D014443:Tyrosine
D001798:Blood Proteins; D010761:Phosphorus Radioisotopes; D014443:Tyrosine; D008345:Manganese; D011505:Protein-Tyrosine Kinases; D008274:Magnesium