Characterization of a calcium-dependent calmodulin-binding domain in the 135-kD human protein 4.1 isoform.

@article{Leclerc1998CharacterizationOA,
  title={Characterization of a calcium-dependent calmodulin-binding domain in the 135-kD human protein 4.1 isoform.},
  author={Estelle Leclerc and Susanne Vetter},
  journal={European journal of biochemistry},
  year={1998},
  volume={258 2},
  pages={567-71}
}
The putative calmodulin binding domain of non-erythroid protein 4.1, previously suggested by Kelly et al. [Kelly, G. M., Zelus, B. D. & Moon, R. T. (1991) J. Biol. Chem. 266, 12469-12473] has been synthesized, and its binding to calmodulin has been studied by fluorescence spectroscopy. For this purpose, the peptide has been N-terminally dansylated. The 4.1 peptide Dns-Abu-S76RGLSRLFSSFLKRPKS92, binds calmodulin in a calcium-dependent way with high affinity (Kd = 23 +/- 6 nM). The peptide… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-8 of 8 extracted citations

Similar Papers

Loading similar papers…