Abstract
Binding of 3H-spiperone and 3H-raclopride to membranes of cells stably-transfected with a human dopamine D 2 receptor clone was investigated, as was that of 3H-spiperone to those stably-transfected with a human D 4 receptor clone. 3H-spiperone and 3H-raclopride labeled the same number of sites in the D 2 receptor preparation. The inhibition of binding by clozapine, spiperone, (−) eticlopride, haloperidol and the novel substituted benzamide 1192U90 was also investigated. Clozapine and 1192U90 showed greater inhibition of 3H-raclopride binding than 3H-spiperone binding to the D 2 receptor. Comparison with inhibition of 3H-spiperone binding to the D 4 receptor revealed that clozapine and 1192U90 displayed apparent selectivity (as assessed by K i ratios) for the D 4 receptor when compared with binding of 3H-spiperone, but not 3H-raclopride, to the D 2 receptor.
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