[3H]Neurotensin(8–13) Binds in Human Brain to the Same Sites as Does [3H]Neurotensin but with Higher Affinity

Kiyoko S. Kanba, Shigenobu Kanba, Albert Nelson, Haruo Okazaki, Elliott Richelson

Research output: Contribution to journalArticlepeer-review

35 Citations (Scopus)

Abstract

Abstract: 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 (KD) of 0.52 nM, and the maximal number of binding sites (B max) was 3.5 pmol/g original wet weight of tissue. Scat‐chard 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 KD 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 languageEnglish
Pages (from-to)131-137
Number of pages7
JournalJournal of Neurochemistry
Volume50
Issue number1
DOIs
Publication statusPublished - Jan 1988

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cellular and Molecular Neuroscience

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