Specific [3H]neurotensin binding to rat spinal cord membranes.
The binding of [3H]neurotensin to membranes prepared from rat spinal cord has been studied in vitro. Scatchard analysis of saturation binding data indicated that [3H]neurotensin binds with high affinity (Kd = 6.3 nM) to a single, saturable population of binding sites (Bmax = 12.4 pmol/g tissue). Neurotensin1-13 (IC50 = 5.9 nM) and neurotensin8-13 (IC50 = 3.7 nM) were potent inhibitors of [3H]neurotensin binding whereas neurotensin1-8 was virtually inactive at concentrations up to 10(-5) M. Sodium chloride (150 mM) significantly inhibited binding, while potassium chloride (5 mM), magnesium chloride (10 mM), manganese chloride (1 mM) and GMP-PNP (0.1 mM) were without effect. The characteristics of the binding of [3H]neurotensin obtained in this study are consistent with this ligand binding to a physiologic neurotensin receptor in rat spinal cord membranes.
D000818:Animals; D066298:In Vitro Techniques; D007700:Kinetics; D008297:Male; D008566:Membranes / Q000378:metabolism; D009496:Neurotensin / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D018028:Receptors, Neurotensin; D017981:Receptors, Neurotransmitter / Q000378:metabolism; D013116:Spinal Cord / Q000378:metabolism*; D013816:Thermodynamics
D018028:Receptors, Neurotensin; D017981:Receptors, Neurotransmitter; D009496:Neurotensin