Phosphorylation of rabbit and human erythrocyte membranes by soluble adenosine 3':5'-monophosphate-dependent and -independent protein kinases.

摘要: Abstract Previous reports from this laboratory and others have established that both the rabbit human erythrocyte membranes contain multiple protein kinase phosphate acceptor activities. We now report these also phosphoryl sites for soluble cyclic AMP-dependent -independent kinases erythrocytes. The membrane, which does not a kinase, has at least four polypeptides (Bands 2.1, 2.3, 4.5, 4.8) are phosphorylated in presence of I, IIa, IIb isolated lysates. resulting phosphoprotein profile is very similar to obtained AMP-mediated autophosphorylation membranes. activities toward been studied several pH values. Although substrate specificity three similar, polypeptide 2.3 appears be greater extent by IIa than I or IIb. This occurs all values studied. Also apparent membrane phosphorylation different histone phosphorylation. proteins can catalyzed casein kinases. These enzymes regulated nucleotides use either ATP GTP as their donor. Polypeptides 2.9, 4.1, 4.8, 5 reaction optimal 7.5. Experiments were performed determine whether membrane-bound additive exclusive. Our results indicate after maximal membranes, available Furthermore, with one type further 32P incorporation occur result exposure other kinase.