The modification of actomyosin ATPase activity by tropomyosin-troponin and its 
dependence on ionic strength, ATP-concentration, and actin-myosin ratio

Dancker, Peter

doi:10.1515/znc-1974-9-1008

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The modification of actomyosin ATPase activity by tropomyosin-troponin and its dependence on ionic strength, ATP-concentration, and actin-myosin ratio

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Dancker, Peter
Max Planck Institute for Medical Research, Max Planck Society;

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https://doi.org/10.1515/znc-1974-9-1008
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Citation

Dancker, P. (1974). The modification of actomyosin ATPase activity by tropomyosin-troponin and its dependence on ionic strength, ATP-concentration, and actin-myosin ratio. Zeitschrift für Naturforschung, C: Journal of Biosciences, 29, 496-505. doi:10.1515/znc-1974-9-1008.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-F3E6-E

Abstract

At millimolar concentrations of ATP the ATPase activity of regulated actomyosin (which consisted of myosin and of actin containing the regulatory proteins tropomyosin and troponin) was lower than that of unregulated actomyosin (containing actin devoid of the regulatory proteins) when the ionic strength was high (> 0 .0 3 ᴍ KCl). At low ionic strength (0.03 ᴍ KCl) the ATPase activity of regulated actomyosin was similar to or even higher than that of unregulated acto myosin. Besides increasing ionic strength an increasing actin-myosin ratio tended to depress the ATPase activity of regulated actomyosin below that of unregulated one. At lower ATP concen trations (0.1 mᴍ or lower) the ATPase activity of regulated actomyosin was higher than that of unregulated actomyosin at any ionic strength and at any actin-myosin ratio. EGTA inhibited the ATPase of regulated actomyosin under any conditions at high ATP concentrations. At lower ATP concentrations EGTA inhibited either at higher ionic strength or at a higher actin-myosin ratio. The inhibition of the ATPase activity of acto-HMM by increasing ionic strength was not in fluenced by the regulatory proteins. - For the interpretation of these results it has been assumed that in actomyosin regulated actin can adopt three states: A low-affinity state which activates the ATPase of myosin only slightly (occurring at high ATP concentrations and in the absence of Ca2+), a high affinity state which activates the ATPase of myosin better than does unregulated actin (occurring at low concentrations of ATP and in the presence of Ca2+), and an intermediate state. This latter state (occurring at high concentrations of ATP and in the presence of Ca2+ or at low concentrations of ATP and in the absence of Ca2+) activates the ATPase of myosin less than does unregulated actin when the actin-myosin ratio is high (wide spacing of myosin on the actin filaments) but activates more (or at least not less) when the actin-myosin ratio is low (dense spacing of myosin on the actin filaments)