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J. Biol. Chem., Vol. 268, Issue 20, 14764-14768, 07, 1993
DE Harris and DM Warshaw
Smooth muscle's stress equals that of skeletal muscle with less myosin.
Thus, under isometric conditions, smooth muscle myosin may spend a greater
fraction of its cycle time attached to actin in a high force state (i.e.
higher duty cycle). If so, then smooth muscle myosin may also have a higher
duty cycle under unloaded conditions. To test this, we used an in vitro
motility assay in which fluorescently labeled actin filaments move freely
over a sparsely coated (5-100 micrograms/ml) myosin surface. Actin filament
velocity (V) was a function of the number of cross-bridges capable of
interacting with an actin filament (N) and the duty cycle (f), V = (a x
Vmax) x (1-(1-f)N) (Uyeda et al., 1990; Harada et al., 1990). N was
estimated from the myosin density on the motility surface and the actin
filament length. Data for V versus N were fit to the above equation to
predict f. The duty cycle of smooth muscle myosin (4.0 +/- 0.7%) was not
significantly different from that of skeletal muscle myosin (3.8 +/- 0.5%)
in agreement with values estimated by Uyeda et al. (1990) for skeletal
muscle myosin under unloaded conditions. The duty cycles of smooth and
skeletal muscle myosin may still differ under isometric conditions.
Smooth and skeletal muscle myosin both exhibit low duty cycles at zero load in vitro
Department of Molecular Physiology and Biophysics, University of Vermont, Burlington 05405.
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