[Effect of the innervation on the structural state of F-actin in rat fast muscles]

Effect of denervation and damage of the spinal cord on the structural state of F-actin in muscle extensor digitorum longus of a rat was studied by polarized microfluorimetry in the ultraviolet light region. The ability of F-actin to change its conformation at ATP binding was used as a test. The character of the changes in tryptophan polarized fluorescence induced by ATP binding was different at muscle denervation and at the damage of the spinal cord. A suggestion is made that the structural state of F-action in muscle fibres may depend on muscle innervation.