Binding of the selective D-1 dopamine receptor ligand 125I SCH 23982 was studied using crude plasma membranes derived from human renal cortex. 125I SCH 23982 bound saturably to a single high affinity site (Kd = 650 pM, Bmax = 19 fmol/mg protein). Binding at 37 degrees was rapid and reversible with forward and reverse rate constants of 5.79 x 10(8) min-1 m-1 and 0.156 min-1 respectively. Antagonist and agonist competition for 125I SCH 23982 binding was also consistent with the existence of a single site possessing pharmacological characteristics similar to a D-1 dopamine receptor. It is suggested that this site may represent a D-1 (or DA1) dopamine receptor present in human renal cortex.