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- W2021452018 abstract "Energy balance studies indicate that ATP splitting by myosin motors during rapid shortening of skeletal muscle is not sufficient to account for the energy (mostly heat) output (Rall et al., J Gen Physiol 68(1), 13, 1976; Homsher et al., J Physiol 321, 423, 1981). We investigated the kinetic step of the myosin ATP-ase cycle related to this phenomenon in single muscle fibers from Rana esculenta (∼2.15 μm sarcomere length, 4°C), by recording the isotonic velocity transient following a force step from zero to the isometric tetanic value (T0). Once the isometric tetanus had developed, the force was first clamped to zero for a range of times from 10 ms to 18 ms (during which the fiber shortened at the maximum velocity by 30 nm hs−1 to 50 nm hs−1) and then raised again to T0 in a stepwise manner (∼120 μs). The elastic lengthening induced by the force step was followed by a transient isotonic lengthening, the size of which ranged from 40 to 60 nm hs−1 depending on the size of the preceding shortening. The lengthening velocity was larger for larger shortening size and progressively decreased to approach the isometric condition with a half-time of 2-3 ms. Similarly, the half-sarcomere stiffness recovered the isometric value e0 from the unloaded shortening value of 0.4 e0 with an exponential time course with τ ∼3 ms. We conclude that during rapid shortening a ∼3 ms-transition between detached states of the myosin motor, likely related to the ATP hydrolysis, becomes rate limiting. Accumulation of motors in the state preceding the hydrolysis step can account for the unexplained energy during rapid shortening. Supported by MIUR (Italy)." @default.
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- W2021452018 date "2010-01-01" @default.
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- W2021452018 title "The Isotonic Velocity Transient Following a Sudden Rise in Force Imposed on the Muscle Sarcomere During Unloaded Shortening Reveals a Rate Limiting Step in Detached Myosin Motors" @default.
- W2021452018 doi "https://doi.org/10.1016/j.bpj.2009.12.1882" @default.
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