Rabbit skeletal muscle preparations (actin, heavy meromyosin, Subfragment 1, tropomyosin-troponin)
Addition of tropomyosin-troponin complex and manipulation of Ca2+ levels
Absence of tropomyosin-troponin complex or presence of Ca2+
ATPase activity of acto-heavy meromyosin and acto-Subfragment 1surrogate
The tropomyosin-troponin complex regulates muscle contraction by binding to actin and inhibiting ATPase activity in the absence of calcium.
Actin purified by a new, simple, and rapid purification procedure activated the ATPase activity of both heavy meromyosin and Subfragment 1 of heavy meromyosin, and this activation was not inhibited by the removal of Ca2+. Preparations of tropomyosin-troponin inhibited (by 85%) both the acto-heavy meromyosin and acto-Subfragment 1 ATPases in the absence of, but not in the presence of, Ca2+. This inhibition was shown to result from binding of the tropomyosin-troponin complex solely to actin and in a ratio of about 1 mole of tropomyosin-troponin to 7 moles of actin.
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Spudich et al. (Sun,) studied this question.
synapsesocial.com/papers/69d72b24b815ed77c2bef1e4 — DOI: https://doi.org/10.1016/s0021-9258(18)62016-2
James A. Spudich
Heart Failure & Transplant
Susan Watt
MRC Laboratory of Molecular Biology
Journal of Biological Chemistry
Medical Research Council
MRC Laboratory of Molecular Biology
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