Inhibition of anandamide amidase activity in mouse brain microsomes by cannabinoids

Biol Pharm Bull. 1996 Aug;19(8):1109-11. doi: 10.1248/bpb.19.1109.


Mouse brain microsomes contain an amidase that catalyzes the hydrolysis of N-arachidonylethanolamide to arachidonic acid and ethanolamine. The enzymatic activity is dependent on the protein concentration of the microsomes and observed over a wide range of pH, 7.4 to 9.5. Kinetic analysis indicated that K(m) (microM) and Vmax (nmol/min/mg protein) were 17.7 +/- 4.1 and 1.81 +/- 0.32, respectively. Cannabidiol (CBD), cannabinol (CBN) and delta 9-tetrahydrocannabinol (delta 9-THC) significantly inhibited the hydrolysis of the amide by mouse brain microsomes. At a concentration of 160 microM, the inhibitory potency decreased in the following order, CBD (66%) > CBN (46%) > delta 9-THC (31%).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amidohydrolases / antagonists & inhibitors*
  • Animals
  • Brain / enzymology*
  • Cannabinoids / pharmacology*
  • Hydrogen-Ion Concentration
  • Male
  • Mice
  • Microsomes / enzymology*


  • Cannabinoids
  • Amidohydrolases
  • arachidonoylethanolamide synthase