Abstract
Measurements of the mass ratio of myosin to paramyosin of myofibrils of honey bee flight muscles on sodium dodecyl sulphate-polyacrylamide gels yielded a paramyosin content of 24% of the myosin filament mass. Based on the myosin to actin mass ratio of 2.3, and 3 actin filaments per myosin filament and per half sarcomere, it could be calculated that there were 3.8 myosin molecules repeating regularly at intervals of 14.4 nm along the myosin filament. In spite of the high paramyosin content the diameter of the myosin filaments is 19–20 nm, as in other insect flight muscles.
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