A single fibre bundle from rat soleus muscle was chemically skinned wi
th saponin and the transfer of myosin heads from the thick filaments t
o the thin filaments at a sarcomere length of 2.4 mu m was measured as
a function of Ca2+ concentration using an x-ray diffraction method at
4-7 degrees C. In the relaxed state, the 1,0 spacing was 42.08 nm. Th
e spacing showed no significant decrease when the Ca2+ concentration w
as below the threshold (-log(10) [Ca2+] or pCa 5.8). No significant tr
ansfer of the myosin heads occurred when the Ca2+ concentration was be
low the threshold (pCa 5.8). When the muscle was maximally activated a
t pca 4.4, the spacing decreased to 40.35 nm. During the maximum isome
tric contraction at pCa 4.4, 54.9 +/- 6.5% (+/- SE of the mean) of the
myosin heads were transferred to the thin filaments. The transfer of
the myosin heads was approximately proportional to relative tension. T
hese results suggest that myosin heads of both fast-twitch and slow-tw
itch skeletal muscles transferred on the common movement as a function
of Ca2+ concentration.