• Chemistry, Medicine
  • Published in
    The Journal of biological…
    1982

Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin.

@article{Chalovich1982InhibitionOA,
  title={Inhibition of actomyosin ATPase activity by troponin-tropomyosin without blocking the binding of myosin to actin.},
  author={Joseph M Chalovich and Evan Eisenberg},
  journal={The Journal of biological chemistry},
  year={1982},
  volume={257 5},
  pages={
          2432-7
        }
}
Vertebrate skeletal muscle contraction is the result of a cyclic interaction of thick myosin filaments with the thin filaments, composed primarily of actin, troponin, and tropomyosin, causing these two sets of filaments to slide past each other (2, 3). This cycling is driven by the hydrolysis of ATP by myosin in a reaction which is activated by actin. When the sarcoplasmic reticulum lowers the free Ca2+ concentration from 10−5 to <10−7 m, muscle contraction ceases and the associated actin… CONTINUE READING

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