Myosin Isozymes and Force Velocity Relation in Fast Rat Muscle

Jaafar, A.;Beckers-Bleukx, G.;Maréchal, Georges
(1985)

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Authors
  • Jaafar, A.
    Author
  • Beckers-Bleukx, G.UCLouvain
    Author
  • Maréchal, Georgesorcid-logoUCLouvain
    Author
Abstract
(en) The force-velocity relations of 43 extensors digitorum longus (EDL) muscles of 90-day-old male (n = 24) and female (n = 19) Wistar rats were measured in vivo. The velocity constants (B) were computed using a form of Aubert's equation P= P0 exp (-1/B), (Aubert, 1956). They varied between 0.9 and 2.55 muscle length/s (37°C). The myosin isozymes were separated by electrophoresis of native myosins in a nondissociating medium. Although the individual variations of the velocity constant and the proportions of LC1f were large, we observed no correlation between them. There is no evidence that variations in power or maximum velocity of fast muscle is controlled by the relative proportion of the two alkaline light-chains, LC1f and LC3f.
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Citations

Jaafar, A., Beckers-Bleukx, G., & Maréchal, G. (1985). Myosin Isozymes and Force Velocity Relation in Fast Rat Muscle. Journal of Muscle Research and Cell Motility, 6(1), 104-105. (Original work published 1985)