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The effect of C-protein on the assembly reaction of myosin was studied by flow birefringence, electron microscopy, and ultracentrifugation. Myosin filaments were formed by dilution to a lower ionic strength. Thinner filaments of 70-110 A in diameter were formed in the presence of C-protein. When dilution was effected by moderately slow dilution (dilution time of 0.5-2 min) or by stepwise dilution, C-protein favored the formation of longer filaments. When dilution was effected by even slower dilution (dilution time above 2 min), C-protein favored the formation of shorter filaments. Longer filaments formed by slow dilution incorporated more C-protein than shorter ones formed by faster dilution. Addition of C-protein to a solution of myosin filaments caused association of the filaments into longer filaments. The elongation effect was slower and stronger for longer filaments.

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