Abstract
The GABAA receptor complex was solubilized from rat brain membranes in Triton X-100, enriched by 1012-S affinity chromatography, and subjected to DEAE anion-exchange chromatography. Two forms were distinguished by their differential elution during this HPLC with a KCl gradient. They displayed similar [3H]muscimol- and [3H]flunitrazepam-binding characteristics, as well as [3H]flunitrazepam-binding inhibition by CL 218872. Rechromatography of these distinct ionic forms indicated that they were not in dynamic equilibrium during chromatography. Resolution of these two pharmacologically similar populations of GABAA receptor by anion-exchange HPLC suggests that they differ in charge densities, a condition which may reflect differing glycosylation or phosporylation states of the complex.
| Original language | English |
|---|---|
| Pages (from-to) | 81-85 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 247 |
| Issue number | 1 |
| DOIs | |
| State | Published - 10 Apr 1989 |
Keywords
- Aminobutyric acid receptor, γ-
- Anion-exchange HPLC
- Benzodiazepine
- CL 218872
- Receptor heterogeneity
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