Complex formation with heavy meromyosin of the isolated actin-like component of thrombosthenin, the contractile protein from blood platelets

Abstract Heavy meromyosin from rabbit skeletal muscle myosin was added on grids to the filamentous polymer of highly purified thrombosthenin A, tho actin-like protein in blood platelets. This resulted in an arrowhead complex formation between heavy meromyosin and the polymer, providing evidence that the polymer has a helical tertiary structure similar to muscle actin. The complex formation was inhibited by ATP.