Solubilization and Characterization of a [3H]Hemicholinium‐3 Binding Site in Rat Brain

Kiyofumi Yamada, Mario D. Saltarelli, Joseph T. Coyle

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)

Abstract

Abstract: A sodium‐dependent high‐affinity [3H]‐hemicholinium‐3 ([3H]HCh‐3) binding site was solubilized from rat striatal synaptic plasma membranes by 0.2% deoxycholate. Deoxycholate solubilization of the [3H]HCh‐3 binding site was dependent upon both detergent concentration and ionic strength of the solubilization medium. Specific [3H]HCh‐3 binding to the solubilized preparation was both sodium‐ and chloride‐dependent and saturable, exhibiting an affinity of 14.2 nM and a capacity (Bmax) of 695 fmol/mg protein. Choline and other analogs inhibited specific [3H]HCh‐3 binding to the solubilized preparation in a concentration‐dependent manner with the similar rank order of potency observed in crude synaptic membranes. Treatments known to disrupt both protein and lipid moieties resulted in diminished specific [3H]HCh‐3 binding. These results suggest that the characteristics of the solubilized [3H]HCh‐3 binding site are similar to those of the membrane‐bound site.

Original languageEnglish
Pages (from-to)1759-1764
Number of pages6
JournalJournal of neurochemistry
Volume50
Issue number6
DOIs
Publication statusPublished - 06-1988
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cellular and Molecular Neuroscience

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