Abstract
The β-carbolines harmane and norharmane competitively inhibit [ 3H]flunitrazepam ([ 3H]FNZ) binding to deoxycholate-solubilized benzodiazepine receptors from calf cerebral cortex, with K i in the micromolar range [ 3H]Propyl-β-carboline-3-carboxylate ([ 3H]PrCC) binds to the soluble receptors with an affinity similar to its binding to particulate receptors (0.41 nM vs 0.48 nM, respectively). The component that binds [ 3H]PrCC displays a sedimentation profile on sucrose gradient centrifugation similar to that of [ 3H]FNZ binding component (sedimentation coefficient about IIS).
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