Identification of Myosin in Nitella flexilis1
- 1 September 1977
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 82 (3), 777-782
- https://doi.org/10.1093/oxfordjournals.jbchem.a131754
Abstract
A myosin B-like protein was extracted from the alga Nitella flexilis. SDS-polyacrylamide gel electrophoresis revealed the presence of myosin heavy chain and actin as the main components. At high ionic strength, its ATPase [EC 3.6.1.3] reaction was activated by EDTA or Ca2+ and inhibited by Mg2+ At low ionic strength, superprecipitation was induced by the addition of ATP. Myosin was purified from Nitella myosin B. The molecular weight of the heavy chain of Nitella myosin, estimated by SDS-gel electrophoresis, was slightly higher than that of skeletal muscle myosin. At low ionic strength, Nitella myosin aggregated to form bipolar filaments about 0.2 μm long. At high ionic strength, its ATPase reaction was activated by EDTA or Ca2+ and inhibited by Mg2+ The Mg2+ reaction of Nitella myosin was activated by skeletal muscle F-actin.Keywords
This publication has 5 references indexed in Scilit:
- Influence of inorganic phosphate in the formation of phosphatases by Escherichia coliBiochimica et Biophysica Acta, 1959
- Velocity Distribution of the Protoplasmic Streaming in Nitella CellsJournal of Plant Research, 1956
- THE MOLECULAR TRANSFORMATIONS OF ACTIN .1. GLOBULAR ACTIN1952
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- Determination of Inorganic PhosphateAnalytical Chemistry, 1949