Proteolytic separation of the actin-activatable ATPase site from the phosphorylation site on the heavy chain of Acanthamoeba myosin IA.
Open Access
- 1 January 1981
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 256 (1) , 503-506
- https://doi.org/10.1016/s0021-9258(19)70166-5
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- Direct photoaffinity labeling by nucleotides of the apparent catalytic site on the heavy chains of smooth muscle and Acanthamoeba myosins.Journal of Biological Chemistry, 1981
- Regulation and Kinetics of the Actin-Myosin-ATP InteractionAnnual Review of Biochemistry, 1980
- Fragmentation of gizzard myosin by alpha-chymotrypsin and papain, the effects on ATPase activity, and the interaction with actin.Journal of Biological Chemistry, 1980
- Calcium‐Sensitivity of Pig‐Carotid‐Actomyosin ATPase in Relation to Phosphorylation of the Regulatory Light ChainEuropean Journal of Biochemistry, 1980
- Chymotryptic heavy meromyosin from gizzard myosin: A proteolytic fragment with the regulatory properties of the intact myosinBiochemical and Biophysical Research Communications, 1978
- The isolated heavy chain of an Acanthamoeba myosin contains full enzymatic activity.Journal of Biological Chemistry, 1978
- Myosin-linked calcium regulation in vertebrate smooth muscleJournal of Molecular Biology, 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
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951