Abstract
Opioid receptor binding properties of [ 3H]Tyr- d-Ala-Phe-Phe-NH 2 (TAPP) were characterized in rat brain and Chinese hamster ovary (CHO) cells expressing the rat μ-receptor. In rat brain, [ 3H]TAPP labeled a single class of opioid sites with a dissociation constant (K d) of 0.31 nM and maximal number of binding sites (B max) of 119 fmol/mg protein. In CHO-μ/1 cell membranes, the K d and B max values were 0.78 n M and 1806 fmol/mg protein, respectively. Binding to rat brain was demonstrated to be pharmacologically identical to that obtained with CHO-μ/1 cell membranes and modulated by Na + ions and guanine nucleotides. The high affinity and selectivity of [ 3H]TAPP together with its low non-specific binding make this radioligand a useful tool for labeling the native and cloned μ-opioid receptor.
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