Divalent cation binding to the high- and low-affinity sites on G-actin.

@article{Zimmerle1987DivalentCB,
  title={Divalent cation binding to the high- and low-affinity sites on G-actin.},
  author={C T Zimmerle and K Patane and Carl Frieden},
  journal={Biochemistry},
  year={1987},
  volume={26 20},
  pages={6545-52}
}
Metal binding to skeletal muscle G-actin has been assessed by equilibrium dialysis using 45Ca2+ and by kinetic measurements of the increase in the fluorescence of N-acetyl-N'-(5-sulfo-1-naphthyl)-ethylenediamine-labeled actin. Two classes of cation binding sites were found on G-actin which could be separated on the basis of their Ca2+ affinity: a single high-affinity site with a Kd considerably less than 1 microM and three identical moderate-affinity binding sites with a Kd of 18 microM. The… CONTINUE READING
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