Purification and characterization of a myosin heavy chain kinase from Dictyostelium discoideum.

@article{Ct1987PurificationAC,
  title={Purification and characterization of a myosin heavy chain kinase from Dictyostelium discoideum.},
  author={Graham P. C{\^o}t{\'e} and U Bukiejko},
  journal={The Journal of biological chemistry},
  year={1987},
  volume={262 3},
  pages={1065-72}
}
A Dictyostelium discoideum myosin heavy chain kinase has been purified 14,000-fold to near homogeneity. The enzyme has a Mr = 130,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and greater than 700,000 as determined by gel filtration on Bio-Gel A-1.5m. The enzyme has a specific activity of 1 mumol/min X mg when assayed at a Dictyostelium myosin concentration of 0.3 mg/ml. A maximum of 2 mol of phosphate/mol of myosin is incorporated by the kinase, and the… CONTINUE READING
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