Abstract
High affinity (apparent K d ⋍ 0.65 nM) and saturable (B max ⋍ 6.6 fmoles/mg protein) binding sites for cholecystokinin (CCK) have been demonstrated in crude synaptosomal membranes from rat cerebral cortex. Scatchard analysis of the equilibrium binding data indicates a single population of non-interacting sites. The specific binding of 125I-CCK 33 to brain membranes is reversible ( t 1 2 ⋍ 6 minutes ), and can be inhibited by structurally related CCK analogues but not by unrelated neuropeptides or drugs. Specific CCK binding reaches equilibrium at a temperature-dependent rate, and is abolished when membranes are pre-treated with heat. Kinetic and competition studies suggest that these high affinity binding sites represent physiologically-relevant receptors for CCK in brain.
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