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- W2066646621 abstract "We have investigated the ability of calmodulin to replace troponin-C in the troponin complex. Unlike troponin-C, calmodulin is able to confer Ca2+-sensitivity on the actin-activated myosin subfragment-1 ATPase of filaments containing actin, tropomyosin and troponin-I in the absence of troponin-T. Gel electrophoresis of the supernatants and the sedimented filaments shows that the Ca2+-sensitive reversible dissociation of calmodulin from the troponin-I causes this regulation. At high Ca2+ concentration troponin-I and calmodulin are associated, and they do not interact with filaments of actin and tropomyosin. At low Ca2+ concentration calmodulin dissociates from troponin-I, which is then able to bind to actin and tropomyosin filaments and inhibit the actin-activated myosin subfragment-1 ATPase. At no stage is calmodulin associated with the filaments. We conclude that although calmodulin seems to regulate the actin-activated myosin subfragment-1 ATPase similarly to the troponin-C plus troponin-T complex, it acts by a different mechanism. Our observations are consistent with a model in which there are two sites of interaction between troponin-I and troponin-C." @default.
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- W2066646621 date "1980-09-01" @default.
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- W2066646621 title "Calmodulin as a model for troponin C" @default.
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- W2066646621 doi "https://doi.org/10.1016/0006-291x(80)91392-3" @default.
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