Soluble Cyclic AMP-Dependent Protein Kinases: Review of the Enzyme Isolated from Bovine Cardiac Muscle* *Supported in part by grants from the National Institute of Health, National Science Foundation, and The American Cancer Society.

Author(s):  
ORA MENDELSOHN ROSENT ◽  
RAFAEL RANGEL-ALDAO ◽  
JACK ERLICHMAN
1975 ◽  
Vol 149 (3) ◽  
pp. 525-533 ◽  
Author(s):  
H A Cole ◽  
S V Perry

1. Troponin I isolated from fresh cardiac muscle by affinity chromatography contains about 1.9 mol of covalently bound phosphate/mol. Similar preparations of white-skeletal-muscle troponin I contain about 0.5 mol of phosphate/mol. 2. A 3':5'-cyclic AMP-dependent protein kinase and a protein phosphatase are associated with troponin isolated from cardiac muscle. 3. Bovine cardiac 3':5'-cyclic AMP-dependent protein kinase catalyses the phosphorylation of cardiac troponin I 30 times faster than white-skeletal-muscle troponin I. 4. Troponin I is the only component of cardiac troponin phosphorylated at a significant rate by the endogenous or a bovine cardiac 3':5'-cyclic AMP-dependent protein kinase. 5. Phosphorylase kinase catalyses the phosphorylation of cardiac troponin I at similar or slightly faster rates than white-skeletal-muscle troponin I. 6. Troponin C inhibits the phosphorylation of cardiac and skeletal troponin I catalysed by phosphorylase kinase and the phosphorylation of white skeletal troponin I catalysed by 3':5'-cyclic AMP-dependent protein kinase; the phosphorylation of cardiac troponin I catalysed by the latter enzyme is not inhibited.


FEBS Letters ◽  
1980 ◽  
Vol 114 (1) ◽  
pp. 83-88 ◽  
Author(s):  
Koji Takio ◽  
Kenneth A. Walsh ◽  
Hans Neurath ◽  
Stephen B. Smith ◽  
Edwin G. Krebs ◽  
...  

1986 ◽  
Vol 83 (14) ◽  
pp. 5272-5276 ◽  
Author(s):  
D. E. Brion ◽  
F. Raynaud ◽  
A. Plet ◽  
P. Laurent ◽  
B. Leduc ◽  
...  

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