Fluorescence measurements of the binding of cations to high-affinity and low-affinity sites on ATP-G-actin.

@article{Carlier1986FluorescenceMO,
  title={Fluorescence measurements of the binding of cations to high-affinity and low-affinity sites on ATP-G-actin.},
  author={M F Carlier and Dominique Pantaloni and Edward D. Korn},
  journal={The Journal of biological chemistry},
  year={1986},
  volume={261 23},
  pages={10778-84}
}
The binding of cations to ATP-G-actin has been assessed by measuring the kinetics of the increase in fluorescence of N-acetyl-N'-(5-sulfo-1-naphthyl)-ethylenediamine-labeled actin. Ca2+ and Mg2+ compete for a single high-affinity site on ATP-G-actin with KD values of 1.5-15 nM for Ca2+ and 0.1-1 microM for Mg2+, i.e. with affinities 3-4 orders of magnitude higher than previously reported (Frieden, C., Lieberman, D., and Gilbert, H. R. (1980) J. Biol. Chem. 255, 8991-8993). As proposed by… CONTINUE READING

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