SOLUBILIZATION AND PURIFICATION OF A HIGH-AFFINITY NEUROTENSIN RECEPTOR FROM NEWBORN HUMAN BRAIN

High affinity neurotensin receptors were solubilized in an active form from newborn human brain using the non-denaturing detergent 3-](3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid (CHAPS). The solubilized receptor was purified in a single step by affinity chromatography. The binding properties of the purified receptor towards [I-125-Tyr3]neurotensin are very similar to those of the membrane bound and of the crude CHAPS-solubilized receptor in terms of affinity and specificity. The purified receptor is a single protein chain of molecular weight 100 kDa as shown by gel filtration and by affinity labelling with [I-125-Tyr3]neurotensin in the presence of the cross-linking agent disuccinimidyl suberate.