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Fillion G, Goiny M, Fillion M P, Jacob J. 
“Influence d'ions et de divers reactifs des proteins sur les liaisons de haute affinite de la 5-hydroxytryptamine et du diethylamide de l'acide lysergique par des membranes synaptosomales de cerveau.”. 
J.Pharmacol.. 1978;9(2):183-84.
The effects of various ions and protein reagents on high affinity binding old 5-HT by brain synaptosomal membranes was studied. Ca2+ and K+ did not modify the binding of LSD or 5-HT. Na+ at 1 to 200 mM reduced LSD and 5-HT binding by competitive inhibition. Among the protein reagents, 2-methoxy-5nitrobenzyl bromide, which reacts with tryptophan residues, was inactive at mM concentrations, indicating that tryptophan groups were not involved in binding of LSD or 5-HT. 3-(3-dimethylaminopropyl)carbodiimide, which reacts with carboxyl groups, inhibited both types of binding. Substances which react with sulfhydryl(SH) groups (iodoacetamide, glutathione, parachloromercuribenzoate and N-ethylmaleimide) inhibited the binding of one or other of the ligands, The protective effect of dithiothreitol, which prevented inhibition of binding by N-ethylmaleimide, showed that inhibition of LSD was competitive whilst that of 5-HT was noncompetitive. SH groups thus participate directly in 5-HT binding but are only near the site of LSD binding.
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