Abstract
Abstract It is known that F-actin, one of the main structural proteins of myofibrils, forms a network structure in solution, resulting in complicated behavior under hydrodynamic force. The present study demonstrates that a factor of protein nature, isolated from myofibrils, inhibits the network formation of F-actin. Under a field of sonic vibration or high shearing force in the presence of this “actin-factor”, F-actin is dispersed with a dimension of about 1 μ in particle length, which is close to the unit length of F-actin in situ (1 filaments in sarcomeres).
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