Anandamide amidohydrolase activity in rat brain microsomes. Identification and partial characterization.

@article{Desarnaud1995AnandamideAA,
  title={Anandamide amidohydrolase activity in rat brain microsomes. Identification and partial characterization.},
  author={F Desarnaud and Hugues Cadas and Daniele Piomelli},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 11},
  pages={6030-5}
}
An amidohydrolase activity present in rat brain microsomes catalyzes the hydrolysis of N-arachidonoyl-[3H]ethanolamine ([3H]anandamide), an endogenous cannabimimetic substance, forming [3H]ethanolamine and arachidonic acid. Amidohydrolase activity is maximal at pH 6 and 8, is independent of divalent cations, has an apparent Km for [3H]anandamide of 12.7 +/- 1.8 microM, and has a Vmax of 5630 +/- 200 pmol/min/mg of protein. Phenylmethylsulfonyl fluoride, a serine protease inhibitor, and p… CONTINUE READING
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