In vitro movement of actin filaments on gizzard smooth muscle myosin: requirement of phosphorylation of myosin light chain and effects of tropomyosin and caldesmon.

@article{Okagaki1991InVM,
  title={In vitro movement of actin filaments on gizzard smooth muscle myosin: requirement of phosphorylation of myosin light chain and effects of tropomyosin and caldesmon.},
  author={Tsuyoshi Okagaki and Sugie Higashi-Fujime and Ryoki Ishikawa and Hiromi Takano-Ohmuro and Kazuyuki Kohama},
  journal={Journal of biochemistry},
  year={1991},
  volume={109 6},
  pages={
          858-66
        }
}
ATP-dependent movement of actin filaments on smooth muscle myosin was investigated by using the in vitro motility assay method in which myosin was fixed on the surface of a coverslip in a phosphorylated or an unphosphorylated state. Actin filaments slid on gizzard myosin phosphorylated with myosin light chain kinase (MLCK) at a rate of 0.35 micron/s, but did not slide at all on unphosphorylated myosin. The movement of actin filaments on phosphorylated myosin was stopped by perfusion of… CONTINUE READING
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