RELEASE OF BOUND SODIUM IN SINGLE MUSCLE FIBERS
Authors:
- J. A. M. HinkeJHJ. A. M. Hinke
- S. G. A. McLaughlinSMS. G. A. McLaughlin
- 1 July 1967
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Physiology and Pharmacology
- Vol. 45 (4) , 655-667
Abstract
The activities of sodium, potassium, and hydrogen in the myoplasm of single muscle fibers from the giant barnacle were measured by cation-sensitive microelectrodes as the temperature of the bathing solution was increased from 7 to 40 °C. An irreversible shortening occurred in all fibers between 37 and 40 °C. When the fibers shortened in a sodium-free Ringer solution, the mean activity of sodium increased by 130%, the mean activity of potassium remained relatively constant, and the pH decreased from 7.17 to 6.77. The results have been interpreted as meaning that at 37–40 °C there was a disruption of the myofilaments and a release of associated sodium ions.Keywords
This publication has 1 reference indexed in Scilit:
- The Binding of Ions to the Muscle Proteins. Measurements on the Binding of Potassium and Sodium Ions to Myosin A, Myosin B and Actin1,2Journal of the American Chemical Society, 1957