Myosin isozymes and force-velocity relation in fast rat muscle

Jaafar, A.F.;Beckers-Bleukx, G.;Maréchal, Georges
(1986) First Scientific Medical Congress — Location: Al-Mustansiriya University, Bagdad (25.March.1986)

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Authors
  • Jaafar, A.F.
    Author
  • Beckers-Bleukx, G.UCLouvain
    Author
  • Maréchal, Georgesorcid-logoUCLouvain
    Author
Abstract
The force-velocity relations of 43 extensor digitorum longus (EDL) muscles of 90 day old male (n=24) and female (n=19) rats were measured in vivo at 8 different velocities under the control of an ergometer and the tension was recorded on a fast U.V. recorder. The velocity constants (B) varied between 0.9 and 2.55 muscle length/s. The myosin isozymes of the muscles were separated by electrophoresis of native myosin in a non-dissociating media. Into 3 zones: HC-LC1f-LC1f (FM3); HC-LC1f-LC3f; FM2); HC-LC3f-LC3f (FM1) the concentration of LC1f relative to the total concentration of the alkaline light chains varied between 0.43 and 0.71. They had no correlation with the velocity constants, although the individual variations were large. There is no support for the hypothesis that the variations in power or maximum velocity of fast muscles is controlled by the relative proportion of the alkaline light chains.

Citations

Jaafar, A. F., Beckers-Bleukx, G., & Maréchal, G. (1986). Myosin isozymes and force-velocity relation in fast rat muscle. First Scientific Medical Congress, p. 70. https://hdl.handle.net/2078.5/214426