Calcium-dependent phosphorylation of bovine cardiac C-protein by phosphorylase kinase.
Phosphorylase kinase catalyzed the calcium-dependent phosphorylation of bovine cardiac C-protein. Phosphorylation of C-protein by phosphorylase kinase reached nearly 2 mol [32P]/mol C-protein. Tryptic phosphopeptide mapping and phosphoamino acid analysis indicated that phosphorylase kinase maybe phosphorylating some of the same seryl residues that undergo phosphorylation by cAMP-dependent protein kinase and that C-protein from bovine and chicken heart are structurally different. Bovine cardiac C-protein was not a substrate for a number of calcium and cyclic nucleotide-independent protein kinases, suggesting that phosphorylation of cardiac C-protein is restricted to protein kinases which are modulated by calcium and cAMP.
Department of Pharmacology, Medical College of Ohio, Toledo 43699.
K K
KK
Schlender
T J
TJ
Thysseril
M G
MG
Hegazy
D000818:Animals; D002118:Calcium / Q000502:physiology*; D002352:Carrier Proteins; D002384:Catalysis; D002417:Cattle; D009124:Muscle Proteins / Q000378:metabolism*; D009206:Myocardium / Q000378:metabolism*; D010449:Peptide Mapping; D010764:Phosphorylase Kinase / Q000502:physiology*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000502:physiology; D000099163:Myosin Binding Protein C
D002118:Calcium; D002352:Carrier Proteins; D009124:Muscle Proteins; D010764:Phosphorylase Kinase; D011493:Protein Kinase C; D000099163:Myosin Binding Protein C