Functional analysis of rat acidic calponin.

@article{Fujii2002FunctionalAO,
  title={Functional analysis of rat acidic calponin.},
  author={Toshihiro Fujii and Sachiko Yabe and Kouta Nakamura and Youichi Koizumi},
  journal={Biological & pharmaceutical bulletin},
  year={2002},
  volume={25 5},
  pages={573-9}
}
Recombinant acidic calponin, a member of the calponin family, interacted with F-actin, but not with microtubules, desmin filaments, tropomyosin, calmodulin, S100 and phosphatidylserine (PS) vesicles with significant affinity. The bindings of acidic calponin to F-actin occurred in a concentration-dependent manner and were saturated at a molar ratio of about 1 acidic calponin to 1-2 actin molecules. The apparent Kd value of acidic calponin to F-actin was calculated to be 1.6 x 10(5) M(-1… CONTINUE READING

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