Modulation of smooth muscle calponin by protein kinase C and calmodulin.

@article{Naka1990ModulationOS,
  title={Modulation of smooth muscle calponin by protein kinase C and calmodulin.},
  author={Michiko Naka and Yasuko Kureishi and Yoshio Muroga and Koichi Takahashi and Masaaki Ito and Toshiki Tanaka},
  journal={Biochemical and biophysical research communications},
  year={1990},
  volume={171 3},
  pages={933-7}
}
When smooth muscle calponin was incubated with protein kinase C, 1 mole of phosphate was incorporated per mole of calponin. The apparent Km value for calponin of the protein kinase was about 0.4 microM. The phosphorylation of calponin by protein kinase C was inhibited markedly by calmodulin in a calcium-dependent manner. Kinetic analysis of calmodulin-induced inhibition of calponin phosphorylation by protein kinase C revealed that calmodulin inhibited the phosphorylation in a noncompetitive… CONTINUE READING