Abstract
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 NaCl, 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 NaCl, is stimulated by this salt.
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