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 language | English |
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Pages (from-to) | 1759-1764 |
Number of pages | 6 |
Journal | Journal of neurochemistry |
Volume | 50 |
Issue number | 6 |
DOIs | |
Publication status | Published - 06-1988 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Cellular and Molecular Neuroscience