The binding of [3H]neurotensin(8-13) to membranes from human frontal cortex at 0°C was time dependent, specific, saturable, and reversible. Saturation isotherms provided an equilibrium dissociation constant (K(D)) of 0.52 nM, and the maximal number of binding sites (B(max)) was 3.5 pmol/g original wet weight of tissue. Scatchard analysis yielded a straight line, and the Hill coefficient was equal to 1, a result indicating that [3H]neurotensin(8-13) bound to single, noncooperative sites. The K(D) values of several analogs of neurotensin determined in competition with [3H]neurotensin(8-13) were similar to those previously determined in competition with [3H]neurotensin. The regional distribution of binding sites for [3H]neurotensin(8-13) was also similar to that for [3H]neurotensin. These results suggest that [3H]neurotensin(8-13) binds to the same sites as [3H]neurotensin and that [3H]neurotensin(8-13) has a higher affinity than [3H]neurotensin for these sites in human brain.
|Original language||English (US)|
|Number of pages||7|
|Journal||Journal of Neurochemistry|
|State||Published - 1988|
ASJC Scopus subject areas
- Cellular and Molecular Neuroscience