1. The troponin complex from skeletal muscle contains approximately 1 mol of phosphate/80000g of complex, covalently bound to the troponin T component. 2. On prolonged incubation of the troponin complex or troponin T with phosphorylase kinase the phosphate content of troponin T was increased to approx. 3mol/mol. 3. On prolonged incubation of troponin I with phosphorylase kinase up to 1.6mol of phosphate/mol were incorporated. 4. Phosphorylation of troponin I was greatly inhibited by troponin C owing to the strong interaction between these proteins. Thus in the troponin complex troponin T was the main substrate for phosphorylase kinase. The phosphorylation of isolated troponin T was also inhibited by troponin C. 5. Troponin I was phosphorylated when the troponin complex was incubated with a bovine cardiac 3′:5′-cyclic AMP-dependent protein kinase. Troponin T either in its isolated form or in the troponin complex was not phosphorylated by bovine protein kinase to any significant extent under the conditions used. 6. If the troponin complex was dephosphorylated to 0.2mol/mol, or phosphorylated up to 2.5mol/mol there was no significant effect on the ability of normal concentrations to confer Ca2+sensitivity on the adenosine triphosphatase of densensitized actomyosin.
Research Article| September 01 1974
Phosphorylation of troponin and the effects of interactions between the components of the complex
Samuel V. Perry;
Biochem J (1974) 141 (3): 733–743.
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Samuel V. Perry, Heather A. Cole; Phosphorylation of troponin and the effects of interactions between the components of the complex. Biochem J 1 September 1974; 141 (3): 733–743. doi: https://doi.org/10.1042/bj1410733
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