Differences in the charge distribution of glycerol-extracted muscle fibers in rigor, relaxation, and contraction

• Published in: The Journal of general physiology Vol. 64; no. 5; pp. 551 - 567
• Main Authors: Pemrick, S M, Edwards, C
• Format: Journal Article
• Language: English
• Published: United States The Rockefeller University Press 01-11-1974
• Subjects: Animals; Calcium - pharmacology; Electrophysiology; Glycerol - pharmacology; In Vitro Techniques; Magnesium - pharmacology; Microelectrodes; Muscle Contraction; Muscle Proteins; Muscles - physiology; Protein Conformation; Rabbits; Space life sciences
• ISSN: 0022-1295; 1540-7748
• DOI: 10.1085/jgp.64.5.551

Glycerol-extracted rabbit psoas muscle fibers were impaled with KCl-filled glass microelectrodes. For fibers at rest-length, the potentials were significantly more negative in solutions producing relaxation than in solutions producing either rigor or contraction; further the potentials in the latter two cases were not significantly different. For stretched fibers, with no overlap between thick and thin filaments, the potentials did not differ in the rigor, the relaxation, or the contraction solutions. The potentials measured from fibers in rigor did not vary significantly with the sarcomere length. For relaxed fibers, however, the potential magnitude decreased with increasing sarcomere length. The difference between the potentials measured for rigor and relaxed fibers exhibited a nonlinear relationship with sarcomere length. The potentials from calcium-insensitive fibers were less negative in both the rigor and the relaxation solutions than those from normal fibers. When calcium-insensitive fibers had been incubated in Hasselbach and Schneider's solution plus MgCl(2) or Guba-Straub's solution plus MgATP the potentials recorded upon impalement were similar in the rigor and the relaxation solution to those obtained from normal fibers in the relaxed state. It is concluded that the increase in the negative potential as the glycerinated fiber goes from rigor to relaxation may be due to an alteration in the conformation of the contractile proteins in the relaxed state.