Structural change of crossbridges of rabbit skeletal muscle during isometric contraction.
Structural changes of crossbridges during isometric contraction have been studied by electron microscopy. Chemically skinned rabbit fibres were rapidly frozen either in activating solution or in ATP-free (rigor) solution, freeze-substituted and embedded. Longitudinal sections of muscle fibres show that the number of crossbridges in active fibres (isometric contraction) is approximately the same as in rigor fibres. Crossbridges of the active and rigor states differ in their shapes, angles and manner of arrangement on the thin filaments. In rigor many crossbridges are wide near the thin filaments and narrow near the thick filament shafts; in active fibres they have more uniform width along their length. The angle of the crossbridges in active fibres is somewhat variable. The average angle is approximately 90 degrees to the filament axis. The crossbridges are arranged on the thin filament retaining the 14.3 nm thick filament periodicity. The crossbridges in rigor are tilted and their arrangement near the thin filament reveals the 36 nm actin periodicity. The variability in the shapes of the crossbridges in active fibres is still higher when we look at them in cross-sections of muscle fibres. The crossbridge shapes in the cross-sections were classified and the relative frequency of different shapes was determined. The shapes that are commonly observed in active fibres are similar in that the majority of the mass of the crossbridges is farther away from the thin filament than the crossbridges in rigor fibres.
Hirose
K
K
Department of Physics, Faculty of Science, University of Tokyo, Japan.
Wakabayashi
T
T
D000199:Actins / Q000648:ultrastructure*; D000818:Animals; D005615:Freezing; D007537:Isometric Contraction; D008854:Microscopy, Electron; D008954:Models, Biological; D009132:Muscles / Q000648:ultrastructure*; D009218:Myosins / Q000648:ultrastructure*; D011817:Rabbits
D000199:Actins; D009218:Myosins