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Chemically skinned fibre bundles were prepared from the striated adductor muscle of the sea scallop, Placopecten magellanicus. The relation between tension and calcium concentration was determined in activating solutions containing 5 mM-MgATP, ionic strength 0.2, pH 7.1 at 20 degrees C. The isometric tension rose from zero to its maximum value between pCa 6.0 and 5.2. The steepness of the relation cannot be accounted for in terms of the binding of calcium to the two known sites on myosin and suggests that there must be an additional, co-operative mechanism. The regulatory light chain content of the fibre bundles was determined by urea gel electrophoresis and was found to be approximately 2 light chains per myosin molecule. The regulatory light chains were removed completely by treatment with EDTA at 25-30 degrees C. Fibre bundles then showed a total loss of control over contraction; a high tension was generated whether or not calcium was present in the bathing solution. Complete removal of the regulatory light chains did not greatly affect the tension generated or the stiffness in the rigor state. Control of contraction could be restored completely by the addition of regulatory light chains from scallop muscle. Treatment with EDTA at 0-12 degrees C resulted in the removal of 0.76-2.0 regulatory light chains per myosin molecule. Fibre bundles for which removal was less than complete were partially sensitive to calcium, i.e. tension was higher in the presence of calcium than in its absence. The results indicate that the normal mechanism of tension generation in scallop muscle is mediated primarily through myosin and not thin filament control. This finding is consistent with previous studies of the ATPase activity of myofibrils from scallop muscle.

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