We tested the hypothesis that age-associated decline in muscle function is related to a change in myosin ATPase activity. Single, glycerinated semimembranosus fibers from young (8-12 mo) and aged (32-37 mo) Fischer 344 × Brown Norway male rats were analyzed simultaneously for force and myosin ATPase activity over a range of Ca2+ concentrations. Maximal force generation was ∼20% lower in fibers from aged animals (P = 0.02), but myosin ATPase activity was not different between fibers from young and aged rats: 686 ± 46 (n = 30) and 697 ± 46 μM/s (n = 33) (P = 0.89). The apparent rate constant for the dissociation of strong-binding myosin from actin was calculated to be ∼30% greater in fibers from aged animals (P = 0.03), indicating that the lower force produced by fibers from aged animals is due to a greater flux of myosin heads from the strong-binding state to the weak-binding state during contraction. This is in agreement with our previous electron paramagnetic resonance experiments that showed a reduced fraction of myosin heads in the strong-binding state during a maximal isometric contraction in fibers from older rats.
- Actomyosin adenosinetriphosphate
- Specific tension
- Type II fibers