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High affinity binding of [H]neurotensin to rat uterus
Authors:D. J. Pettibone and J. A. Totaro
Affiliation:

Department of Microbial Pharmacometrics Merck Sharp and Dohme Research Laboratories, West Point, PA 19486, USA

Abstract:[3H]Neurotensin (NT) was found to bind specifically and with high affinity to crude membranes prepared from rat uterus. Scatchard analysis of saturation binding studies indicated that [3H]NT apparently binds to two sites (high affinity Kd 0.5 nM; low affinity Kd 9 nM) with the density of high affinity sites (41 fmoles/mg prot.) being about one-third that of the low affinity sites (100 fmoles/mg prot.). In competition studies, NT and various fragments inhibited [3H]NT binding with the following potencies (IC50): NT 8–13 (0.4 nM), NT 1–13 (4 nM), NT 9–13 (130 nM), NT 1–11, NT 1–8 (>100 μM). Quantitatively similar results were obtained using brain tissue. These findings raise the possibility of a role for NT in uterine function.
Keywords:Neurotensin receptors   Radioligand binding   Uterus   Brain
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