[3H]Neurotensin(8-13) binds in human brain to the same sites as does [3H]neurotensin but with higher affinity

K. S. Kanba, S. Kanba, A. Nelson, H. Okazaki, E. Richelson

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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 (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 languageEnglish (US)
Pages (from-to)131-137
Number of pages7
JournalJournal of Neurochemistry
Volume50
Issue number1
StatePublished - 1988

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ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Kanba, K. S., Kanba, S., Nelson, A., Okazaki, H., & Richelson, E. (1988). [3H]Neurotensin(8-13) binds in human brain to the same sites as does [3H]neurotensin but with higher affinity. Journal of Neurochemistry, 50(1), 131-137.