Abstract
In the presence of 20 mM PC a strong contraction is produced in glycerol-extracted muscle fibers by ATP and AMP in concentrations as low as 10(-6)M per liter. At low concentrations of nucleotide tension rises very slowly. This rise is interpreted as being due to absorption of nucleotide by the contractile elements. AMP gives an S-shaped tension curve, indicating that the conversion of AMP into ATP is an autocatalytic process. Tension is maintained in a contracted muscle even in PC solutions free of ATP. PC alone produces a contraction if applied within 5 minutes after ATP has been washed out from a contracting muscle. It is concluded from these results that PC is the substrate for the enzymatic activity of the contractile elements and that this activity depends on the presence of bound nucleotide which acts as an energy transfer mechanism. PC accelerates relaxation which is caused by ATP under certain conditions. In the presence of PC even very low concentrations of ATP can produce relaxation. A strong contraction can be produced under these conditions by the addition of Ca ions. These observations support the conclusion that relaxation depends on the rephosphorylation of nucleotide bound by the contractile elements.
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