Contraction of rabbit skinned skeletal muscle fibers at low levels of magnesium adenosine triphosphate.

The contractile properties of skinned single fibers from rabbit psoas muscle were investigated under conditions of low MgATP and no Ca2+ (i.e., less than 10(-8) M). At 1 microM MgATP, fibers shortened at a maximum velocity of 660 +/- 420 A/half sarcomere/s (n = 9), compared with 34,000 A/half sarcomere/s measured during maximum Ca2+-activation at 1 mM MgATP (Moss, R. L., 1982. J. Muscle Res. Cell. Motil ., 3:295-311). The observed dependence of Vmax on pMgATP between 7.0 and 5.3 was similar to that of actomyosin ATPase measured previously by Weber, A., R. Herz , and I. Reiss (1969, Biochemistry, 8:2266-2270). Isometric tension was found to vary with pMgATP in a manner much like that reported by Reuben , J. P., P. W. Brandt, M. Berman , and H. Grundfest (J. Gen. Physiol. 1971. 57:385-407). A simple cross-bridge model was developed to simulate contractile behaviour at both high and low levels of MgATP. It was found that the pMgATP dependence of Vmax and ATPase could be successfully modeled if the rate of detachment of the cross-bridge was made proportional to the concentration of MgATP. In the model, the similar dependence of Vmax and ATPase on pMgATP was derived from the fact that in this range of pMgATP every pass of a cross-bridge by an actin site resulted in an attachment-detachment cycle, and every such cycle caused hydrolysis of one molecule of ATP.