The myosin content from red and white muscles of three marine fish species, saithe (Pollachius virens. L.), haddock (Melanogrammus aeglefinus, L.), both members of the family Gadidae, and capeline (Mallotus villosus, M.) of the family Osmeridae, was analyzed electrophoretically. Analysis of the native myosin by electrophoresis under non-dissociating conditions revealed two isoforms in red muscles, and three or four in white muscles. The white muscles of the two closely related species had a similar pattern of isoforms. Myosin from the slow red muscles had two types of light chain, LC1S and LC2S, and myosin from the fast white muscles three, LC1F, LC2F, and LC3F. The pattern of light chains in both types of muscles was species-dependent. All the light chains from fish myosins were more acidic than those of the rat diaphragm used as standard. One main type of heavy chain was detected in each kind of muscle. In white muscles of saithe there was an extra band, present in minor amounts. The heavy chains from white muscle myosin had lower electrophoretic mobilities than those from red muscle, and the mobilities of all of them were intermediate between those of the heavy chains type IIa and I of rat diaphragm myosin. In our opinion, there are probably more isomyosins in fish muscles than those detected in the present work and their presence is obscured by comigration with the main types.