Purification and characterization of the D sub(2)-dopamine receptor from bovine anterior pituitary

The D sub(2)-dopamine receptor from bovine anterior pituitary has been purified similar to 33,000-fold to apparent homogeneity by sequential use of affinity chromatography on immobilized carboxymethylene-oximinospiperone-Sepharose, Datura stramonium) lectin-agarose, and hydroxylapatite chromatography. When reinserted into phospholipid vesicles with purified brain G sub(i)/G sub(o), the purified D sub(2) receptors mediate the agonist stimulation of super(35)S-labeled guanosine 5'-O-(thiotriphosphate) binding to brain G-proteins with a typical D sub(2)-dopaminergic order of potency. These data suggest that the authors have purified an intact functional D sub(2)-dopamine receptor.