Key result
Myosin filament length does not affect sliding velocity along F-actin bundles.
Why the study?
The mechanism of unidirectional sliding of myosin filaments along actin bundles and the role of ATP in this process required experimental investigation.
Should not change clinical practice; leaves open whether myosin length modulates cardiac contractility in vivo.
Unidirectional sliding of myosin filaments along F‐actin bundles was produced with purified muscle actin and myosin in the presence of ATP. The velocity of myosin filament sliding was independent of myosin filament length. This result supports a recent hypothesis that long distance movement of myosin cross‐bridge can be induced by splitting of one ATP molecule [Yanagida, Arata, and Oosawa, 1985. Nature. 316:366–369; Higashi‐Fujime. 1985. J. Cell Biol., 101:2335–2344].
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Sugie Higashi‐Fujime (1986) studied this question. ATP was evaluated on Velocity of myosin filament sliding. The velocity of unidirectional sliding of myosin filaments along F-actin bundles in the presence of ATP was independent of myosin filament length.
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