Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

High affinity binding of (/sup 3/H)neurotensin of rat uterus

Journal Article · · Peptides (Fayetteville, N.Y.); (United States)
(/sup 3/H)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 (/sup 3/H)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 (/sup 3/H)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.
Research Organization:
Merck Sharp and Dohme Research Labs., West Point, PA (USA)
OSTI ID:
5209876
Journal Information:
Peptides (Fayetteville, N.Y.); (United States), Journal Name: Peptides (Fayetteville, N.Y.); (United States) Vol. 8:6; ISSN PPTDD
Country of Publication:
United States
Language:
English