Abstract
Myosin was separated from Physarum myxoamoeba myosin B by ultracentrifugation, then purified by potassium iodide treatment followed by gel filtration.
The purified myxoamoeba myosin was similar to the myosin isolated from Physarum plasmodium. Myxoamoeba myosin was soluble at low ionic strength, but it formed bipolar filaments on the addition of 10 mM MgCl2. ATPase activity was activated by Ca++, but was inhibited by Mg++ and EDTA.
