Myosin specific phosphatases isolated from Dictyostelium discoideum

Edward R. Kuczmarski*, Jennifer Pagone

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Scopus citations


Using native myosin phosphorylated on either the heavy chain or the light chain, we have isolated myosin phosphatases from extracts of vegetative Dictyostelium amoeba. Two phosphatases were resolved by DEAE-cellulose chromatography. One of these phosphatases removed phosphate from heavy chain or light chain at approximately the same rate. The other phosphatase appeared to be much more specific for phosphorylated myosin heavy chain. Although these enzymes removed phosphate from other phosphoprotein substrates such as histone or casein, they did so at a much lower rate. Both enzymes required magnesium for activity, but appeared to be independent of calcium.

Original languageEnglish (US)
Pages (from-to)510-516
Number of pages7
JournalJournal of Muscle Research and Cell Motility
Issue number6
StatePublished - Dec 1986

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Cell Biology


Dive into the research topics of 'Myosin specific phosphatases isolated from Dictyostelium discoideum'. Together they form a unique fingerprint.

Cite this