Reversible changes in the ATPase activity and in the regulatory light chain content upon heat (30.DEG.C)-treatment of "Akazara" striated adductor myosin.

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  • OJIMA Takao
    Department of Chemistry, Faculty of Fisheries, Hokkaido University
  • NISHITA Kiyoyoshi
    Department of Chemistry, Faculty of Fisheries, Hokkaido University
  • WATANABE Shizuo
    Department of Chemistry, Faculty of Science, Tokyo Institute of Technology

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Description

Myosin from striated adductor muscle of "Akazara" scallop was incubated at 30°C for 5min in a medium containing 2mM MgCl2 and various concentrations of Ca2+ ions. It was observed that the 30°C-treatment resulted in a decrease in the Ca2+-sensitivity of myosin-ATPase as well as in the release of the regulatory light chain (EDTA-LC) of myosin. The 30°C-treated myosin was then subjected to a cooling treatment, being kept for 18 h at 0°C. It was found that EDTA-LC recombined with myosin and that Ca2+-sensitivity of myosin-ATPase was restored.<br> It was also found that Ca2+ alone was about 70 times more effective than Mg2+ alone in preventing the heat-induced release of EDTA-LC from occurring and also in recombination of EDTA-LC with the heat-treated myosin.

Journal

  • J Biochem (Tokyo)

    J Biochem (Tokyo) 89 (4), 1333-1335, 1981

    The Japanese Biochemical Society

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