Affinity of S100A1 protein for calcium increases dramatically upon glutathionylation.

@article{Goch2005AffinityOS,
  title={Affinity of S100A1 protein for calcium increases dramatically upon glutathionylation.},
  author={Grażyna Goch and Sergiusz Vdovenko and Hanna Kozłowska and Andrzej Bierzyński},
  journal={The FEBS journal},
  year={2005},
  volume={272 10},
  pages={
          2557-65
        }
}
S100A1 is a typical representative of a group of EF-hand calcium-binding proteins known as the S100 family. The protein is composed of two alpha subunits, each containing two calcium-binding loops (N and C). At physiological pH (7.2) and NaCl concentration (100 mm), we determined the microscopic binding constants of calcium to S100A1 by analysing the Ca(2+)-titration curves of Trp90 fluorescence for both the native protein and its Glu32 --> Gln mutant with an inactive N-loop. Using a chelator… CONTINUE READING
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