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. 1977 Nov 1;167(2):333–343. doi: 10.1042/bj1670333

The sites of phosphorylation of rabbit cardiac troponin I by adenosine 3':5'-cyclic monophosphate-dependent protein kinase. Effect of interaction with troponin C.

A J Moir, S V Perry
PMCID: PMC1183663  PMID: 202250

Abstract

1. Troponin I prepared from rabbit hearts contains 1.0-1.5 mol of P/mol when isolated by affinity chromatography. Most of the covalently bound phosphate is located in residues 1-48 of the molecule. 2. 3':5'-Cyclic AMP-dependent protein kinase catalyses phosphorylation at serine-20 and serine-146. Serine-20 is more rapidly phosphorylated than serine-146. 3. In troponin I prepared from frozen hearts by affinity chromatography about 0.3-0.5 mol of P/mol is associated with serine-20 and 0.8-1.0 mol of P/mol with other site(s) in residues 1-48 of the molecule. 4. Phosphorylation at serine-20 and servine-146 is not significantly inhibited by troponin C. 5. The mechansim of the interaction of troponin C with cardiac troponin I is discussed in the light of these results.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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