Phosphorylation of a second site for myosin light chain kinase on platelet myosin.

@article{Ikebe1989PhosphorylationOA,
  title={Phosphorylation of a second site for myosin light chain kinase on platelet myosin.},
  author={M. Ikebe},
  journal={Biochemistry},
  year={1989},
  volume={28 22},
  pages={
          8750-5
        }
}
  • M. Ikebe
  • Published 1989
  • Biology, Medicine
  • Biochemistry
The 20,000-dalton light chain of bovine platelet myosin is phosphorylated at two sites by myosin light chain kinase. The first and second phosphorylation sites are at a serine and a threonine residue, respectively. The location of the phosphorylation sites was determined by using limited proteolysis. The N-terminal sequence of the 17,000-dalton tryptic fragment of platelet myosin 20,000-dalton light chain was found to be identical with that of gizzard 20,000-dalton light chain from Ala-17 to… Expand
Phosphorylation of vertebrate nonmuscle and smooth muscle myosin heavy chains and light chains
Diphosphorylation of platelet myosin by myosin light chain kinase.
Molecular cloning and sequencing of myosin light chains in human megakaryoblastic leukemia cells.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 37 REFERENCES
Phosphorylation of smooth muscle myosin at two distinct sites by myosin light chain kinase.
Regulation in vitro of brush border myosin by light chain phosphorylation.
Myosin phosphorylation in intact platelets.
...
1
2
3
4
...