Characterization of the metal ion-binding domains from rat alpha- and beta-parvalbumins.

@article{Henzl2003CharacterizationOT,
  title={Characterization of the metal ion-binding domains from rat alpha- and beta-parvalbumins.},
  author={Michael T. Henzl and Sayeh Agah and John D. Larson},
  journal={Biochemistry},
  year={2003},
  volume={42 12},
  pages={3594-607}
}
We have examined the metal ion-binding domains from rat alpha and beta parvalbumin. We find that the CD-EF fragments differ markedly in their tendency to self-associate. Whereas Ca(2+)-free alpha CD-EF is monomeric, the Ca(2+)-free beta peptide dimerizes weakly (K(2) = 2400 +/- 200 M(-1)). In buffer containing 1.0 mM Ca(2+), the apparent dimerization constant for beta CD-EF (191,000 +/- 29,000 M(-1)) is more than 50 times that of alpha (3400 +/- 200 M(-1)). Alpha CD-EF binds two Ca(2+) with… CONTINUE READING