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The binding of neurotensin to synaptic membranes from rat brain was studied at 24 degrees with the use of [3H]neurotensin. The binding was found to be highly specific, saturable, and reversible. Values for KD of 2 nM and 0.9 nM were derived from equilibrium and kinetic experiments, respectively. Virtually no degradation of neurotensin was observed in the incubation medium after exposure to synaptic membranes under the conditions of the binding studies. Competitive inhibition of [3H]neurotensin binding by partial sequences of neurotensin revealed that the addition of the residue arginine-8 to the neurotensin-(9-13)-pentapeptide increases about 500-fold the relative binding potency, whereas the remaining portion of the NH2-terminal region is mainly responsible for full pharmacological potency; the COOH-terminal leucyl residue is essential for binding.
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C Granier, and
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S Leeman, and
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January 1976,
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August 1985,
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June 1984,
Brain research,
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January 1980,
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March 1983,
The Journal of biological chemistry,
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November 1978,
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P Kitabgi, and
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August 1983,
The Journal of neuroscience : the official journal of the Society for Neuroscience,
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August 1986,
The Journal of biological chemistry,
P Kitabgi, and
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March 1994,
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February 1991,
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