Abstract
The purified inhibitory subunit of rabbit skeletal muscle troponin, TN-I (M.W. 24,000) was phosphorylated by phosphorylase kinase in the presence of Mg− ATP2− and Ca2+, and by protein kinase in the presence of Mg−ATP2− and cyclic AMP2. Phosphorylase phosphatase removed all the phosphate incorporated by either kinase. The primary site of phosphorylation of TN-I by phosphorylase kinase was a threonine residue, as compared to a serine residue in phosphorylase a. Comparison of kinetic parameters for both kinases and the phosphatase with TN-I and other protein substrates showed it to be a favorable substrate. The tropomyosin binding subunit of troponin, TN-T (M.W. 38,000) was also phosphorylated by phosphorylase kinase, but not protein kinase, and dephosphorylated by phosphorylase phosphatase. Incubation of troponin with Mg−ATP2− and either phosphorylase kinase or protein kinase resulted in incorporation of phosphate into both TN-I and TN-T with both kinases. All of the phosphate incorporated was removed by phosphorylase phosphatase.
Supported by Grant AM 12842 from the National Institutes of Health, and grants from the American Heart Association and the Muscular Dystrophy Association of America, Inc. J.T.S. holds a Damon Runyon Cancer Research Fellowship.
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Abbreviations
- cyclic AMP:
-
cyclic adenosine 3′,5′-monophosphate
- ATPase:
-
adenosine triphosphatase
- SDS:
-
sodium dodecyl sulfate
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England, P.J., Stull, J.T., Huang, T.S., Krebs, E.G. (1974). Phosphorylation and Dephosphorylation of Skeletal Muscle Troponin. In: Metabolic Interconversion of Enzymes 1973. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-80817-3_17
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DOI: https://doi.org/10.1007/978-3-642-80817-3_17
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