Photoaffinity labeling of different benzodiazepine receptors at physiological temperature

J Neurochem. 1984 Dec;43(6):1745-8. doi: 10.1111/j.1471-4159.1984.tb06103.x.

Abstract

Irreversible labeling of benzodiazepine receptors in membranes from cerebellum or hippocampus was compared at 0 degrees C using [3H]flunitrazepam as a photoaffinity ligand. [3H]Flunitrazepam reproducibly and irreversibly labeled mainly one protein (P51) in cerebellum and at least two proteins (P51 and P55) in hippocampus at both temperatures. Differential inhibition at 37 degrees C of irreversible [3H]flunitrazepam binding to the individual proteins by several selective benzodiazepine receptor ligands supports the hypothesis that P51 and P55 are associated with different benzodiazepine receptors.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Affinity Labels / metabolism*
  • Animals
  • Anti-Anxiety Agents*
  • Benzodiazepines*
  • Benzodiazepinones / pharmacology
  • Brain / metabolism*
  • Carbolines / pharmacology
  • Cell Membrane / metabolism
  • Cerebellum / metabolism
  • Flunitrazepam / metabolism*
  • Hippocampus / metabolism
  • Photochemistry
  • Pyridazines / pharmacology
  • Rats
  • Receptors, GABA-A / drug effects
  • Receptors, GABA-A / metabolism*
  • Temperature

Substances

  • Affinity Labels
  • Anti-Anxiety Agents
  • Benzodiazepinones
  • Carbolines
  • Pyridazines
  • Receptors, GABA-A
  • Benzodiazepines
  • Flunitrazepam
  • CL 218872
  • beta-carboline-3-carboxylic acid ethyl ester
  • 2-oxoquazepam