Tension and ATPase rate in steady-state contractions of rabbit soleus fiber segments.

Steady-state isometric tension and ATPase were studied in hyperpermeable segments of single muscle fibers from rabbit soleus muscle at 22 degrees C. The ATPase activity was due to actomyosin. The ratio of fiber ATPase to tension was used as an index of steady-state cross-bridge kinetics. Increasing the calcium ion concentration from pCa 8 to pCa 5 activated both tension and ATPase. The maximal tension was 1.35 +/- 0.07 kg/cm2. The maximal ATPase was 1.05 +/- 0.13 mumol X g-1. s-1 at pCa 5.2. ATPase activity increased with tension, such that the ratio of ATPase to tension remained constant at all calcium concentrations. In the absence of calcium, increasing the concentration of MgATP from 1 to 7 X 10(-7) M increased tension from zero to a maximum of 0.46 +/- 0.03 kg/cm2. Increasing MgATP concentration further to 1 X 10(-6) M inhibited tension. In the phase of rising tension, ATPase increased proportionally to tension, to 0.11 +/- 0.01 mumol X g-1 X s-1 at maximum tension. However, the ratio of ATPase to tension on the rising phase had a value only one-third of that seen with calcium-activated tension. Thus, low substrate concentrations, but not low calcium ion concentrations, influence cross-bridge kinetics under steady-state isometric conditions, possibly by an increase in the tension-time product during a cross-bridge cycle.