The serotonin (5-HT) transporter from calf striatum cerebral membranes was solubilized with digitonin and characterized by gel exclusion chromatography. [H-3]Imipramine and [H-3]paroxetine were utilized as markers for labeling it. H-3-imipramine labels a high- and a low-affinity site on striatum membranes, whereas it binds to a single high-affinity site on the solubilized fraction. [H-3]Paroxetine binds with the same affinity to a single site on both membranes and solubilized preparations. After gel exclusion chromatography of the solubilizate both [H-3]imipramine rind [H-3]paroxetine bind on an identical fraction of 205 kDa molecular weight, with a similar maximum number of binding sites (Bmax). Our results suggest that both H-3-imipramine and [H-3]paroxetine bind to a common site on the 5-HT transporter.
Solubilization and characterization of [3H]imipramine and [3H]paroxetine binding sites from calf striatum.
GIANNACCINI, GINO;MARTINI, CLAUDIA;LUCACCHINI, ANTONIO
1994-01-01
Abstract
The serotonin (5-HT) transporter from calf striatum cerebral membranes was solubilized with digitonin and characterized by gel exclusion chromatography. [H-3]Imipramine and [H-3]paroxetine were utilized as markers for labeling it. H-3-imipramine labels a high- and a low-affinity site on striatum membranes, whereas it binds to a single high-affinity site on the solubilized fraction. [H-3]Paroxetine binds with the same affinity to a single site on both membranes and solubilized preparations. After gel exclusion chromatography of the solubilizate both [H-3]imipramine rind [H-3]paroxetine bind on an identical fraction of 205 kDa molecular weight, with a similar maximum number of binding sites (Bmax). Our results suggest that both H-3-imipramine and [H-3]paroxetine bind to a common site on the 5-HT transporter.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
