Isolation of Putative Benzodiazepine Receptors from Rat Brain Membranes by Affinity Chromatography
- 1 January 1982
- journal article
- research article
- Published by Wiley in Journal of Neurochemistry
- Vol. 38 (1) , 15-19
- https://doi.org/10.1111/j.1471-4159.1982.tb10848.x
Abstract
The benzodiazepine receptor from rat brain was solubilised and purified 5200‐fold by affinity chromatography. The affinity column contained an immobilized benzodiazepine (delorazepam) and biospecific elution with 6 mm‐chlorazepate was achieved. The purified receptor is apparently homogeneous in SDS‐polyacrylamide gel electrophoresis. The native protein had a molecular weight of 240,000, and the subunit one of 60,000. The dissociation constant (KD) is 8 nm for [3H]diazepam. A correlation exists between the value of affinity obtained for benzodiazepine derivatives and their known pharmacological effectiveness.Keywords
This publication has 10 references indexed in Scilit:
- Receptors for the Age of Anxiety: Pharmacology of the BenzodiazepinesScience, 1980
- Putative benzodiazepine receptor: A protein solubilised from brainFEBS Letters, 1979
- Solubilization of histamine H-1, GABA and benzodiazepine receptorsLife Sciences, 1979
- Solubilization of benzodiazepine binding site from rat cortexLife Sciences, 1979
- A new staining technique for proteins in polyacrylamide gels using Coomassie brilliant blue G250Analytical Biochemistry, 1977
- Benzodiazepine receptors in rat brainNature, 1977
- Isolation of the Insulin Receptor of Liver and Fat-Cell MembranesProceedings of the National Academy of Sciences, 1972
- Muscle fibrils: Solubilization and gel electrophoresisFEBS Letters, 1971
- Protein Purification by Affinity ChromatographyJournal of Biological Chemistry, 1970
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951