Potassium contractures were induced in lobster muscle bundles under conditions which produced varying KCl fluxes into the fibers. The presence or absence of chloride fluxes during depolarization by high concentrations of potassium, had no effect on the tensions developed. The curve relating tension to the membrane potential had a typical sigmoid shape with an apparent "threshold" for tension at -60 mv. Soaking the muscles in low (0.1 mM) calcium salines for 30 min completely eliminated the potassium contractures but the caffeine contractures were only slightly reduced under these conditions. The potassium contracture could be completely restored in less than 2 min by return of the calcium ions to the saline. Evidence is presented for independent, superficial, and deep calcium sites; the superficial sites appear to be involved in the coupling mechanisms associated with potassium contractures. These sites are highly selective for Ca++, and attempts to substitute either Cd++, Co++, Mg++, Ba++, or Sr++ for Ca++ were unsuccessful. However, K+ appeared to compete with Ca++ for these sites, and the evoked tension could be reduced by prestimulation of the muscle fibers with high K+ salines. The results of studies on the influx of 45Ca during potassium contractures were compatible with the view of muscle activation by the entry of extracellular calcium.
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1 July 1968
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July 01 1968
The Role of Calcium in Excitation-Contraction Coupling of Lobster Muscle
Harold Gainer
Harold Gainer
From the Department of Zoology, University of Maryland, College Park, Maryland 20742
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Harold Gainer
From the Department of Zoology, University of Maryland, College Park, Maryland 20742
Received:
December 04 1967
Online ISSN: 1540-7748
Print ISSN: 0022-1295
Copyright © 1968 by The Rockefeller University Press
1968
J Gen Physiol (1968) 52 (1): 88–110.
Article history
Received:
December 04 1967
Citation
Harold Gainer; The Role of Calcium in Excitation-Contraction Coupling of Lobster Muscle . J Gen Physiol 1 July 1968; 52 (1): 88–110. doi: https://doi.org/10.1085/jgp.52.1.88
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