Mechanical properties and myosin light chain composition of skinned muscle fibres from adult and new‐born rabbits.
- 1 February 1981
- journal article
- research article
- Published by Wiley in The Journal of Physiology
- Vol. 311 (1) , 201-218
- https://doi.org/10.1113/jphysiol.1981.sp013581
Abstract
The maximum velocity of shortening, Vmax, and stiffness were measured in skinned single fiber segments from psoas and soleus muscles of adult rabbits and psoas muscles of newborn rabbits, and the myosin light chain composition was determined in the same segments used in the mechanical studies. Vmax was obtained at 15.degree. C during maximal activation at pCa (-log[Ca]) 5.49 using a method involving measurement of the time required to take up various amounts of slack imposed on the segments. Stiffness was measured during activation at 10.degree. C by application of length steps complete in 0.6 ms. The myosin light chain composition of the segments was then determined by SDS(sodium dodecyl sulfate)-polyacrylamide gel electrophoresis. Only fast type light chains were present in the psoas fiber segments, although the relative amounts of myosin LC1f, LC2f and LC3f in these segments was somewhat variable. In most instances, the sum of the amounts of LC1f and LC3f present was equivalent to the amount of LC2f. Only slow type light chains were found in the soleus segments, and the sum of the amounts of LC1as and LC1bs was about equal to the amount of LC2s. The results indicate that there are no consistent relationships between Vmax, tension development or stiffness and LC1f/LC2f in the segments from adult and newborn psoas muscles or between these mechanical parameters and LC1as/LC2s or LC1bs/LC2s in the adult soleus segments. The psoas segments, which had light chains of the fast type, had Vmax values that were consistently higher than those of the soleus segments, which had light chains of the slow type. The stiffness values obtained in each of the 3 kinds of muscle were similar, suggesting that cross-bridge stiffness is similar in rabbit skeletal muscles of different type and age. Apparently, the amount of end compliance introduced by the connections to the fiber segments has a marked influence on the stiffness that is measured.This publication has 43 references indexed in Scilit:
- Changes in tropomyosin subunits and myosin light chains during development of chicken and rabbit straited musclesDevelopmental Biology, 1979
- Active and rigor muscle stiffness [proceedings].1977
- Tension responses to sudden length change in stimulated frog muscle fibres near slack lengthThe Journal of Physiology, 1977
- Temperature and amplitude dependence of tension transients in glycerinated skeletal and insect fibrillar muscle.The Journal of Physiology, 1977
- Force-velocity characteristics for calcium-activated mammalian slow-twitch and fast-twitch skeletal fibers from the guinea pig.Proceedings of the National Academy of Sciences, 1976
- Dynamic properties of mammalian skeletal muscles.Physiological Reviews, 1972
- Substructure of the myosin moleculeJournal of Molecular Biology, 1971
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Subunit structure of myosin. 3. A proposed model for rabbit skeletal myosin.1969
- The variation in isometric tension with sarcomere length in vertebrate muscle fibresThe Journal of Physiology, 1966