By means of polarized UV fluorescent microscopy, the state of F-actin was studied in single glycerinized muscle fibers from intact, locally damaged and denervated m. semi-tendinosus of the frog. It was shown that F-actin of denervated muscle fiber lost the ability to reply by increasing tryptophan fluorescence anisotropy during the fiber relaxation and its stretching in the rigor solution by 1--4 per cent compared to the original length. Zenker's necrosis retains this ability only slightly. It is supposed that both the denervation atrophy and Zenker's necrosis change the structure of F-actin.

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