The characteristics of [3H]sulpiride binding to the D2 dopamine receptor in rat striatal membranes were examined under several conditions. In the absence of sodium ions, the specific binding of [3H]sulpiride could not be detected. In the direct binding experiment, at 25 degrees C, the affinity of [3H]sulpiride for D2 receptors was increased in a dose-dependent manner of sodium ions whereas magnesium ions have opposite effects on an affinity of [3H]sulpiride binding. The lowering incubation temperature (4 degrees C) also produced a further increase in affinity of the ligand. Under all conditions, [3H]sulpiride labeled a single homogenous site of the receptor. On the other hand, the result from quantitative analysis of agonist/[3H]sulpiride competition curves indicated an existence of high (RH) and low (RL) affinity states for agonists and the proportion of two-affinity states was modulated by guanosine triphosphate (GTP), magnesium ions and lowering temperatures. GTP, together with sodium ions, caused a full conversion of RH to RL, while an increase in the affinity for agonists with a partial conversion of RL to RH could be induced by magnesium ions at 25 degrees C. At a lower (4 degrees C) temperature, the agonist competition curve indicated an existence of a single agonist low-affinity state (RL) and then, the effects of GTP and magnesium ions in the agonist affinity observed at 25 degrees C were abolished. These results can be incorporated into a two-step, ternary complex model involving an inhibitory guanine nucleotide binding protein for the agonist and antagonist interaction with D2 receptors.(ABSTRACT TRUNCATED AT 250 WORDS)