Evidence for domain organization within the 61-kDa calmodulin-dependent cyclic nucleotide phosphodiesterase from bovine brain.

@article{Charbonneau1991EvidenceFD,
  title={Evidence for domain organization within the 61-kDa calmodulin-dependent cyclic nucleotide phosphodiesterase from bovine brain.},
  author={Hubert Charbonneau and Sanjay Kumar and Jeffrey P. Novack and Donald K Blumenthal and Patrick R. Griffin and Jeffrey Shabanowitz and Donald Frederick Hunt and Joseph A. Beavo and Kenneth Albert Walsh},
  journal={Biochemistry},
  year={1991},
  volume={30 32},
  pages={
          7931-40
        }
}
The complete amino acid sequence of the 61-kDa calmodulin-dependent, cyclic nucleotide phosphodiesterase (CaM-PDE) from bovine brain has been determined. The native protein is a homodimer of N alpha-acetylated, 529-residue polypeptide chains, each of which has a calculated molecular weight of 60,755. The structural organization of this CaM-PDE has been investigated with use of limited proteolysis and synthetic peptide analogues. A site capable of interacting with CaM has been identified, and… CONTINUE READING
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