Abstract
The Ca2+-regulation of scallop striated muscle contraction, a Ca2+-regulation mechanism that is linked to myosin, was first discovered by A. G. Szent-Györgyi and his colleagues. 1,2 In myosin-linked Ca2+-regulation, the Ca2+ -receptive site is the essential light chain of myosin, and the ATPase of the scallop myofibrils has been found to be desensitized to Ca2+ by removal of the regulatory light chain (RLC) of myosin in response to treatment with a divalent cation chelator (EDTA). At the same time, three components of troponin and tropomyosin have also been isolated from scallop striated muscle, and several of their biochemical properties have been investigated.3–5 In this troponin-linked Ca2+-regulation, the concurrent presence of all three components of troponin (troponins C, I, and T; TnC, TnI, and TnT) and tropomyosin are necessary for the regulation of actomyosin ATPase activity.6–10 The action of Ca2+ on TnC ultimately induces actomyosin ATPase activity. Troponin-linked Ca2+ -regulation is also desensitized by the removal of TnC in response to treatment with divalent cation chelators such as EDTA or CDTA. The mutual relation of these two types of Ca2+-regulations in scallop myofibrils was then investigated as follows.11 Desensitized scallop myofibrils were prepared by removing both RLC and TnC by treatment with a divalent cation chelator, CDTA, and the effects of reconstitution with RLC and/or TnC on the ATPase activity of the desensitized myofibrils were examined.
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Yumoto, F., Tanokura, M. (2007). Structural and Functional Analysis of Troponins from Scallop Striated and Human Cardiac Muscles. In: Ebashi, S., Ohtsuki, I. (eds) Regulatory Mechanisms of Striated Muscle Contraction. Advances in Experimental Medicine and Biology, vol 592. Springer, Tokyo. https://doi.org/10.1007/978-4-431-38453-3_15
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DOI: https://doi.org/10.1007/978-4-431-38453-3_15
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