Calcium sensitivity of vertebrate skeletal muscle myosin.
Publication/Presentation Date
5-10-1983
Abstract
The calcium sensitivity of vertebrate skeletal muscle myosin has been investigated. Adenosinetriphosphatase (ATPase) activity was assayed in a reconstituted system composed of either purified rabbit myosin plus actin or myosin plus actin, tropomyosin, and troponin. The calcium sensitivity of actomyosin Mg-ATPase activity was found to be directly affected by the ionic strength of the assay medium. Actomyosin assayed at approximately physiological ionic strength (120 mM KCl) demonstrated calcium sensitivity which varied between 6 and 52%, depending on the myosin preparation and the age of the myosin. Mg-ATPase activity was increased when calcium was present in the assay medium at physiological ionic strength. Conversely, actomyosin Mg-ATPase activity assayed at a lower ionic strength (15 mM KCl) was inhibited by addition of calcium. Addition of tropomyosin and troponin to the assay increased the calcium sensitivity of the system at the physiological ionic strength still further (up to 99% calcium sensitivity) and conferred calcium sensitivity on the system at the lower ionic strength (greater than 90% calcium sensitivity). A correlation also existed between myosin's calcium sensitivity and the phosphorylated state of light chain 2.
Volume
22
Issue
10
First Page
2324
Last Page
2331
ISSN
0006-2960
Published In/Presented At
Pulliam, D. L., Sawyna, V., & Levine, R. J. (1983). Calcium sensitivity of vertebrate skeletal muscle myosin. Biochemistry, 22(10), 2324–2331. https://doi.org/10.1021/bi00279a004
Disciplines
Medicine and Health Sciences
PubMedID
6222760
Department(s)
Department of Surgery
Document Type
Article