Human platelet myosin light chain kinase requires the calcium-binding protein calmodulin for activity.

@article{Hathaway1979HumanPM,
  title={Human platelet myosin light chain kinase requires the calcium-binding protein calmodulin for activity.},
  author={David R. Hathaway and Robert S Adelstein},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1979},
  volume={76 4},
  pages={
          1653-7
        }
}
In an actomyosin fraction isolated from human platelets, phosphorylation of the 20,000-dalton light chain of myosin is stimulated by calcium and the calcium-binding protein calmodulin. The enzyme catalyzing this phosphorylation has been isolated by using calmodulin-affinity chromatography. Platelet myosin light chain kinase activity was monitored throughout the isolation procedures by using the 20,000-dalton smooth muscle myosin light chain purified from turkey gizzards as substrate. The… CONTINUE READING

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