Protease Susceptibility of Fast Skeletal Myosin Heavy Chain form Carp Acclimated to Cold and Warm Tempratures

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  • Nakaya Misako
    Laboratory of Aquatic Moecular Biology and Biotechnology, Graduate School of Agricultural and Life Seiences, The University of Tokyo
  • Watabe Shugo
    Laboratory of Aquatic Moecular Biology and Biotechnology, Graduate School of Agricultural and Life Seiences, The University of Tokyo

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Description

Myosins and their rod fragments from fast skeletal muscles of carp acclimated to 10 and 30°C were digested with α-chymotrypsin. Myosins in 0.12M NaCl were digested at 10°C with the protease at an enzyme-to-myosin weight ratio of 1/100 which cleaved mainly the region connecting myosin subfragm-<br>ent-1 and rod. When relative amounts of remaining myosin heavy chain band from the 10°C-acclimat-ed carp were plotted on a logarithmic scale against reaction time, digestion wasfound to proceed in the first order reaction with 4.2×10-4 s-1, which was lower than 6.1×10-4 s-1 for the 30°C-acclimated carp (P<0.05). The other region, which is susceptible to protease and located between myosin subfragment-2 and light meromyosin, was examined at 10°C using myosin rod in 0.5M KCl and α-chymotryp-sin with an enzyme-to-rod weight ratio of 1/120. Both myosin rods from the 10-and 30°C-acclimated carp gave about 2×10-4 s-1, with no differences in protease susceptibility. These results are in marked contrast to our previous observation that myosin from the 10°C-acclimated carp is less thermostable in the crossbridge head and α-helical region of the rod part than that from the 30°C-acclimated carp.

Journal

  • Fisheries science

    Fisheries science 63 (3), 462-465, 1997

    The Japanese Society of Fisheries Science

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