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
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
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- Received March 19, 1971.
- © 1971, by the American Society of Biological Chemists, Inc.











