Marked activation of the N-acylphosphatidylethanolamine-hydrolyzing phosphodiesterase by divalent cations.

@article{Ueda2001MarkedAO,
  title={Marked activation of the N-acylphosphatidylethanolamine-hydrolyzing phosphodiesterase by divalent cations.},
  author={Natsuo Ueda and Qian Liu and Kenji Yamanaka},
  journal={Biochimica et biophysica acta},
  year={2001},
  volume={1532 1-2},
  pages={121-7}
}
N-Acylethanolamines including anandamide (an endogenous ligand for cannabinoid receptors) are released from N-acylphosphatidylethanolamine (N-acyl-PE) by the catalysis of a phosphodiesterase of the phospholipase D type. The enzyme was solubilized from the particulate fractions of rat heart with the aid of octyl glucoside, and partially purified by anion-exchange chromatography. The enzyme hydrolyzed N-palmitoyl-PE with a specific activity of 17 nmol/min/mg protein at 37 degrees C. The enzyme… CONTINUE READING
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