Multiple forms of cytosol and membrane-bound protein kinase activity in human erythrocytes.
Both cytosol and membranes of human erythrocytes display protein kinase activity towards exogenous protein substrates such as casein, phosvitin and histones. The histone kinase activity, unlike casein kinase, of both cytosol and membranes is increased by cyclic AMP. The protein kinase forms removed from the membranes with 0.7 M NaCl, phosphorylate only serine residues of both casein and histones through a mechanism cyclic AMP-independent. The protein kinase activity located in the cytosol (hemolysate) is due also to enzyme forms phosphorylating both serine and threonine residues of casein, in addition to forms phosphorylating only serine residues of casein and histones. Also the cytosol kinase forms, once partially purified by Sepharose 6B filtration, appear to be cyclic AMP-independent.
D002364:Caseins; D000242:Cyclic AMP / Q000494:pharmacology; D003600:Cytosol / Q000201:enzymology*; D004910:Erythrocyte Membrane / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D006656:Protamine Kinase / Q000378:metabolism; D011494:Protein Kinases / Q000097:blood*; D012694:Serine; D012965:Sodium Chloride / Q000494:pharmacology; D013912:Threonine
D002364:Caseins; D013912:Threonine; D012965:Sodium Chloride; D012694:Serine; D000242:Cyclic AMP; D011494:Protein Kinases; D006656:Protamine Kinase