High-affinity 3H-serotonin binding to caudate: inhibition by hallucinogens and serotoninergic drugs.
Psychopharmacology September 15, 1978 DOI: 10.1007/BF00428022 (opens in new tab)
Study at a glance
AI-extracted from the abstract| Characteristics | Experimental study Peer reviewed |
|---|---|
| Population | Calf caudate homogenate |
| Topics | Serotonin |
| Citations | 55 |
| Key findings | Serotonin binding to calf caudate is specific, saturable, and inhibited almost exclusively by serotonergic agonists and antagonists. |
Abstract
The specific binding of 3H-serotonin to calf caudate homogenate was studied. The dissociation constant was 2nM and the number of specific sites was 14fmoles/mg protein. Of many drugs tested, inhibition of specific 3H-serotonin binding occurred almost exclusively with serotonin agonists and antagonists. The concentrations for 50% inhibition of 3H-serotonin binding by serotonergic agonists follow: bufotenin, 6nM; 5-methoxytryptamine, 12 nM; psilocin, 35nM; dimethyltryptamine, 220 nM; and tryptamine, 270 nM. The concentrations for the antagonists were: LSD 9.5 nM; methysergide 16nM and metergoline 25nM.