Acanthamoeba myosin IA, IB, and II heavy chains are synthesized in vitro from Acanthamoeba messenger RNA.
Open Access
- 1 September 1984
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 259 (18) , 11157-11159
- https://doi.org/10.1016/s0021-9258(18)90836-7
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Purification and characterization of a myosin I heavy chain kinase from Acanthamoeba castellanii.Published by Elsevier ,2021
- The interaction of F-actin with phosphorylated and unphosphorylated myosins IA and IB from Acanthamoeba castellanii.Journal of Biological Chemistry, 1983
- Supramolecular regulation of the actin-activated ATPase activity of filaments of Acanthamoeba Myosin II.Journal of Biological Chemistry, 1983
- Identification of three phosphorylation sites on each heavy chain of Acanthamoeba myosin II.Journal of Biological Chemistry, 1981
- Proteolytic separation of the actin-activatable ATPase site from the phosphorylation site on the heavy chain of Acanthamoeba myosin IA.Journal of Biological Chemistry, 1981
- [31] Use of protein A—bearing staphylococci for the immunoprecipitation and isolation of antigens from cellsPublished by Elsevier ,1981
- Evidence for differential intracellular localization of the Acanthamoeba myosin isoenzymesNature, 1980
- An Efficient mRNA‐Dependent Translation System from Reticulocyte LysatesEuropean Journal of Biochemistry, 1976
- Electrophoretic analysis of the major polypeptides of the human erythrocyte membraneBiochemistry, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970