Identification and initial characterization of high-affinity [3H]dextrorphan binding sites in rat brain

Paul H. Franklin, Thomas F. Murray

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

We have identified specific high-affinity [3H]dextrorphan binding sites in rat forebrain. [3H]Dextrorphan binds saturably and reversibly to an apparently homogeneous class of sites characterized by a Bmax of 2.62±0.06 pmol/mg protein and KD of 60±4 nM. Glycine and glutamate independently increase [3H]dextrorphan binding in a concentration-dependent manner. The pharmacological profile of [3H]dextrorphan binding characterized by equilibrium competition experiments, together with these data suggest that [3H]dextrorphan labels a site at or near the N-methyl-D-aspartate receptor.

Original languageEnglish
Pages (from-to)89-93
Number of pages5
JournalEuropean Journal of Pharmacology: Molecular Pharmacology
Volume189
Issue number1
DOIs
StatePublished - Jul 31 1990
Externally publishedYes

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Dextrorphan
Binding Sites
Brain
Prosencephalon
N-Methyl-D-Aspartate Receptors
Glycine
Glutamic Acid
Pharmacology
Proteins

All Science Journal Classification (ASJC) codes

  • Pharmacology

Cite this

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