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Niwaguchi T, Inoue T, Nakahara Y. 
“Studies on Enzymatic Dealkylation of D-Lysergic Acid Diethylamide (LSD)”. 
Biochem Pharmacol. 1974;23(6):1073-1078.
Abstract
Dealkylation of d-lysergic acid diethylamide (LSD) by animal liver preparations was studied. Method Rat (150-200 g), rabbit (2.5 - 3.0 kg) and guinea pig (250-300 g) livers were homogenised and centrifuged and the microsomal fractions were suspended in isotonic KC1. An incubation mixture was prepared containing 3 ml 900 g supernatant fraction and 0.63 umol LSD. Incubation was terminated after 2 hr and unchanged LSD and metabolites were extracted. TLC, u.v. spectrometry fluorometry and mass spectrometry were carried out for metabolite identification. Inhibitors were added before incubation. Results LSD was metabolised with maximal activity occurring between pH 7.2 and 7.6 Maximal enzyme activity was obtained in presence of 2;,umoles NADP and nicotinaměde in the supernatant fraction. Little activity was observed in microsome except in the presence of NADPH. NAD And adaerobic-conditions diminished enzyme activity. TLC showed LSD present with 2 metabolitea. Metabolite I was D-lysergic acid monoethylamide (LAE) and metabolite II was D-No-demethyl-lysergic acid diethylamide (norLSD). SKF-525A (1 x 10-3M) completely blocked the enzymatic dealkylation of LSD; chlorpromazine, rtitrazopam and meprobamate markedly inhibited dealkylation and iproniazid moderately inhibited dealkylation. Reserpine had little effect. Conclusion Results obtained from peripheral organs may be related to interactions between LSD and some tranequillisers to transmitters in the brain.
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