Disproportionate accumulation of myosin and tropomyosin in cultured muscle cells.

Accumulation of two major myofibrillar proteins, myosin and tropomyosin, was monitored in differentiating skeletal muscle cultures. The tropomyosin subunit to myosin heavy chain accumulation rate ratio was more than twice the stoichiometric ratio of tropomyosin subunit to myosin heavy chain in mature skeletal muscle myofibrils and crude myofibrils from cultured muscle cells. Electron microscopy revealed normal patterns of myofibril assembly in these muscle cultures. Therefore, the observed disproportionate accumulation of tropomyosin and myosin heavy chain may be reflecting normal cellular conditions for de novo myofbril assembly.