Proteolytic activation of calmodulin-dependent cyclic nucleotide phosphodiesterase.

  title={Proteolytic activation of calmodulin-dependent cyclic nucleotide phosphodiesterase.},
  author={Randall L. Kincaid and Irene Stith-Coleman and Martha Vaughan},
  journal={The Journal of biological chemistry},
  volume={260 15},
Purified calmodulin-stimulated cyclic nucleotide phosphodiesterase from brain, a homodimer of 59-kDa subunits, was activated by limited proteolysis with trypsin, alpha-chymotrypsin, Pronase, or papain and could not be further stimulated by addition of Ca2+ and calmodulin. Proteolysis increased Vmax and had little effect on the Km for cGMP. Treatment with alpha-chymotrypsin in the presence of ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) produced, sequentially, 57… CONTINUE READING