Lower activation energy for sliding of F-actin on a less thermostable isoform of carp myosin.

@article{Chaen1996LowerAE,
  title={Lower activation energy for sliding of F-actin on a less thermostable isoform of carp myosin.},
  author={Shigeru Chaen and Misako Nakaya and Xinzhou Guo and Shoji Watabe},
  journal={Journal of biochemistry},
  year={1996},
  volume={120 4},
  pages={
          788-91
        }
}
We have examined the temperature-dependence of sliding velocity of fluorescent F-actin on myosins isolated from 10 degrees C- and 30 degrees C-acclimated carp. Activation energies for the sliding of F-actin were 63 and 111 kJ/mol for the 10 degrees C- and 30 degrees C-acclimated carp myosins, respectively. Arrhenius plots of the sliding velocity from 10 degrees C- and 30 degrees C-acclimated carp myosin were shown to intersect at high temperature (about 30 degrees C). The thermostability… CONTINUE READING
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