The dopamine D-1 receptor from striatal membranes was compared with the dopamine DA-1 receptor from renal proximal tubules. The dopamine-1 receptors were solubilized with 1% sodium cholate and phospholipids after pretreatment with the dopamine-1 agonist, SKF R-38393. The soluble receptors were reconstituted into phospholipid vesicles after removal of sodium cholate. The receptors were studied by radioligand binding using the dopamine-1 antagonist [125I]-SCH 23982. The reconstituted dopamine D-1 and DA-1 receptor densities were similar. However, the affinity of the solubilized D-1 receptor was 17-fold greater than the solubilized DA-1 receptor. The affinity of membrane bound D-1 receptor to the radioligand was also greater than that noted for membrane bound DA-1 receptor. The mechanism for this difference remains to be determined.