High affinity binding of [3H]neurotensin of rat uterus.
[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 (approximately IC50): NT 8-13 (0.4 nM), NT 1-13 (4 nM), NT 9-13 (130 nM), NT 1-11, NT 1-8 (greater than 100 microM). Quantitatively similar results were obtained using brain tissue. These findings raise the possibility of a role for NT in uterine function.
Pettibone
D J
DJ
Department of Microbial Pharmacometrics, Merck Sharp and Dohme Research Laboratories, West Point, PA 19486.
Totaro
J A
JA
D000818:Animals; D001665:Binding Sites; D001923:Brain Chemistry; D005260:Female; D066298:In Vitro Techniques; D009496:Neurotensin / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D018028:Receptors, Neurotensin; D017981:Receptors, Neurotransmitter / Q000032:analysis*; D014316:Tritium; D014599:Uterus / Q000032:analysis*
D018028:Receptors, Neurotensin; D017981:Receptors, Neurotransmitter; D014316:Tritium; D009496:Neurotensin