Myosin from the Myxoamoebae of Physarum polycephalum
- 1 January 1980
- journal article
- research article
- Published by Japan Society for Cell Biology in Cell Structure and Function
- Vol. 5 (4) , 379-382
- https://doi.org/10.1247/csf.5.379
Abstract
Myosin was separated from Physarum myxoamoeba myosin B by ultracentrifugation and 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 Ca2+ but was inhibited by Mg2+ and EDTA.This publication has 4 references indexed in Scilit:
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- Biochemistry of actomyosin-dependent cell motility (a review).Proceedings of the National Academy of Sciences, 1978
- Extraction of Contractile Protein from Myxoamoebae of Physarum polycephalumCell Structure and Function, 1978
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951