The literature contains several reports on the fine structure of isolated myofibrils (1)(2)(3)(4)(5). From these it is clear that the extended fibril is composed, in part, of longitudinally arranged filaments which in the dry state are about 200/~. thick and which show nodosities and densities arranged at regular intervals of about 400/~. In the intact fibril these densities are likely to be in perfect phase or register and thus give to the fibril a fine cross-banding quite distinct from the relatively macroscopic striations. There is some evidence (3, 4) that these filaments are arranged along the periphery of the fibril, thus making of it a tubular structure. From electron microscopy the major striations, the A and Z bands, seem to result from concentrations of a non-fibrous, amorphous material. The association, if any, between this and the filaments has not been clarified. In contraction, the major part of the amorphous material within the A band moves into the I and Z band regions. That more attention has not been given the phenomenon is doubtless due to difficulty in controlling contraction of small muscle units and obtaining intermediate stages in the process.Schick and Hass (6) have described the isolation of fibrils from frozen sections of muscle with the aid of tryptic digestion at 0 ° C. When the isolated fibrils were treated with adenosinetriphosphate, the fibrils progressively shortened to approximately 25 per cent of their original lengths. During this shortening, the cross-striations became indistinct and the fibrils broadened. After a time no further contraction was observed. The action was not reversible.More recent studies (7) have indicated that the contraction could be slowed