• Chemistry, Medicine
  • Published in
    The Journal of biological…
    1989

Characterization of the calmodulin-binding and of the catalytic domains of Bordetella pertussis adenylate cyclase.

@article{Ladant1989CharacterizationOT,
  title={Characterization of the calmodulin-binding and of the catalytic domains of Bordetella pertussis adenylate cyclase.},
  author={Daniel Ladant and Susan Michelson and Robert S. Sarfati and Anne Marie Gilles and Roxane Predeleanu and Octavian B{\^a}rzu},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 7},
  pages={
          4015-20
        }
}
The structural organization of the low molecular mass form (43 kDa) of Bordetella pertussis adenylate cyclase was dissected taking advantage of the known sequence of the bacterial cya gene (Glaser, P., Ladant, D., Sezer, O., Pichot, F., Ullmann, A., and Danchin, A. (1988) Mol. Microbiol. 2, 19-30) and its low content of Trp and Met residues. Cleavage of the 43-kDa protein and of its complementary tryptic fragments (T25 and T18 peptides) with N-chlorosuccinimide and cyanogen bromide followed by… CONTINUE READING

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