Solubilization and characterization of d-fenfluramine binding sites from bovine cerebral cortex

Valeria Gagliardini, Carlo Taddei, Mario Salmona, Paul Pham, Tiziana Mennini, Maddalena Fratelli

Research output: Contribution to journalArticlepeer-review


Stable d-Fenfluramine binding activity was obtained in high yields, in cholate extracts of bovine cerebral cortex crude membrane preparations Dissociation constant (Kd 17 nM), stereoselectivity and the rank order of potencies of various serotonin uptake inhibitors were similar to those measured in native membranes The inhibitory effect of Na+ ions was also maintained in the soluble state, since the presence of 100 mM Na+ leads to an even greater reduction of the binding than in membrane-associated binding sites. Photoaffinity labeling of soluble binding sites with p-[125l]d-Fenfluramine had led to the identification of a single specific bend of molecular weight around 40-50 kDa. This suggests that d-Fenfluramine binding sites are separate molecular entities from the serotonin transporter, that belongs to a family of integral membrane proteins of 68-73 kDa molecular weight.

Original languageEnglish
Pages (from-to)1109-1118
Number of pages10
JournalLife Sciences
Issue number15
Publication statusPublished - 1994

ASJC Scopus subject areas

  • Pharmacology


Dive into the research topics of 'Solubilization and characterization of d-fenfluramine binding sites from bovine cerebral cortex'. Together they form a unique fingerprint.

Cite this