Novel bovine heart calmodulin-dependent protein kinase which phosphorylates a high molecular weight calmodulin-binding protein

• Published in: Biochemical and biophysical research communications Vol. 186; no. 2; pp. 819 - 826
• Main Authors: Barnes, Junor A., King, Martin J., Kalra, Jawahar, Sharma, Rajendra K.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 31.07.1992; Elsevier
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Calcium-Calmodulin-Dependent Protein Kinases; calmodulin-binding protein; Calmodulin-Binding Proteins - isolation & purification; Calmodulin-Binding Proteins - metabolism; Cattle; Chromatography, Affinity; Chromatography, Gel; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; heart; isolation; Molecular Weight; Myocardium - enzymology; Phosphorylation; protein kinase; Protein Kinases - isolation & purification; Protein Kinases - metabolism; Substrate Specificity; Transferases; PAGE; HMW; SDS; CaM; EGTA; Heart; Phosphorylation; Purification; Bovine; Calcium; Enzyme; In vitro; Binding protein; Vertebrata; Mammalia; Enzymatic activity; Substrate specificity; Artiodactyla; Ungulata; Calmodulin
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/0006-291X(92)90819-7

A novel calmodulin-dependent protein kinase has been isolated from bovine cardiac muscle by successive chromatography on DEAE-Sepharose 6B, Calmodulin-Sepharose 4B affinity and Sepharose 6B chromatography columns. The protein kinase was shown by gel filtration chromatography to have a molecular mass of 36,000 daltons. The highly purified protein kinase stoichiometrically phosphorylated the high molecular weight calmodulin-binding protein from cardiac muscle [ Sharma RK (1990) J Biol Chem 265, 1152–1157] in a Ca 2+ calmodulin -dependent manner. The phosphorylation resulted in the maximal incorporation of 1 mol of phosphate/mol of the high molecular weight calmodulin-binding protein. Other Ca 2+ calmodulin -dependent protein kinases failed to phosphorylate the high molecular weight calmodulin-binding protein. The distinct substrate specificity of this protein kinase indicates that it is not related to the known calmodulin-dependent protein kinases and therefore constitutes a novel protein kinase.