The Regulation of Rabbit Skeletal Muscle Contraction

I. BIOCHEMICAL STUDIES OF THE INTERACTION OF THE TROPOMYOSIN-TROPONIN COMPLEX WITH ACTIN AND THE PROTEOLYTIC FRAGMENTS OF MYOSIN

  1. James A. Spudich and
  2. Susan Watt
  1. From the Medical Research Council Laboratory of Molecular Biology, Cambridge, England

    Abstract

    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.

    Footnotes

      • Received March 19, 1971.
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