A cyclic AMP-dependent phosphorylation of spectrin dimer.
In contrast to the properties of spectrin obtained from [32P]phosphate-labeled red cells, purified spectrin dimer could be phosphorylated by a cAMP-dependent protein kinase from bovine heart. Both spectrin bands were phosphorylated. Spectrin band 2 contained in addition to autophosphorylated peptides several phosphopeptides that were distinct from autophosphorylated ones. The cAMP-dependent phosphorylation of spectrin band I was modulated by reducing agent and the concentration of spectrin. At high concentrations spectrin band 2 was predominantly labeled. The cAMP-dependent phosphoform of spectrin band 2 had a pI slightly higher than that of autophosphorylated spectrin band 2, but lower than that of ankyrin.
D019794:2,3-Diphosphoglycerate; D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D002417:Cattle; D004163:Diphosphoglyceric Acids / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007526:Isoelectric Point; D046911:Macromolecular Substances; D009206:Myocardium / Q000201:enzymology; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D013049:Spectrin / Q000378:metabolism*
D004163:Diphosphoglyceric Acids; D046911:Macromolecular Substances; D013049:Spectrin; D019794:2,3-Diphosphoglycerate; D011494:Protein Kinases; D000469:Alkaline Phosphatase