Phosphorylation of troponin T by Ca-phospholipid-dependent protein kinase.

Phosphorylation of skeletal and cardiac troponin T by Ca-phospholipid-dependent protein kinase/protein kinase C/was investigated. Under conditions used, the rate of troponin T phosphorylation was only 3-4 times lower than that of histone H-1, and after long term incubation the enzyme incorporated about 1 mol of phosphate per mol of skeletal and cardiac troponin T. The sites phosphorylated by protein kinase C are mainly located in the C-terminal part/residues 159-259/of skeletal troponin T. The less effectively phosphorylated sites are located in between residues 42-158 of troponin T. Reverse phase HPLC revealed four groups of tryptic phosphopeptides of troponin T. The phosphopeptides weakly adsorbed on a RP-18 column were identified as a mixture of two peptides/GKKQTAR and QTAR/both containing Thr-171 of troponin T phosphorylated by protein kinase C.