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Hsu L L, Halaris AE, Paul SM, Freedman DX. 
“Rat Brain Aryl Acylamidase: Multiple Forms and Stereospecific Inhibition by d-LSD and Serotonin Related Compounds.”. 
Pharmacologist. 1976;18(2):201.
Abstract
Rat brain aryl acylamidase activity (AAA) is inhibited by low concentrations of 5-HT and d-LSD but not by I-LSD (Paul et al., J.Neurochem., in press). Multiple forms of AAA were identified as follows: Rat brains were homogenized in a cold buffer solution (pH 5.5) containing 0.5% (V/V) Triton X-100. The homogenate was kept at 0 for 1 he and centrifuged at 8500 x g for 20 min. An ammonium sulfate precipitate was obtained at 33-67aturation and applied to a BioGel (A-5m) column, elated with Na-phosphate buffer (pH 5.5). At least 2 enzyme activity peaks were observed corresponding to the protein peaks at either pH 5.5 or 7.5. The first enzyme peak (AAA-1) showed a pH optimum at 7.5; the second enzyme peak (AAA-2) showed a pH optimum at 5.5 AAA-1 was markedly inhibited (68%) by d-LSD and 2-Br-LSD, moderately inhibited (26%) by 5-HT and slightly inhibited (15%) by tryptamine but not by I-LSD at 0.1 mM concentrations. However, AAA-2 was only moderately inhibited (24%) by d-LSD and 2-Br-LSD, but not affected by I-LSD, 5-HT or tryptamine at the same concentration. Kinetic studies with AAA-1 indicated competitive inhibition by d-LSD with a Ki value of 4.83 pM.
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