Ca2+ regulation of gelsolin activity: binding and severing of F-actin.

@article{Kinosian1998Ca2RO,
  title={Ca2+ regulation of gelsolin activity: binding and severing of F-actin.},
  author={Henry J. Kinosian and Jay Newman and Bryan Lincoln and Lynn A. Selden and Lewis C. Gershman and James E. Estes},
  journal={Biophysical journal},
  year={1998},
  volume={75 6},
  pages={3101-9}
}
Regulation of the F-actin severing activity of gelsolin by Ca2+ has been investigated under physiologic ionic conditions. Tryptophan fluorescence intensity measurements indicate that gelsolin contains at least two Ca2+ binding sites with affinities of 2.5 x 10(7) M-1 and 1.5 x 10(5) M-1. At F-actin and gelsolin concentrations in the range of those found intracellularly, gelsolin is able to bind F-actin with half-maximum binding at 0.14 microM free Ca2+ concentration. Steady-state measurements… CONTINUE READING
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