• Chemistry, Medicine
  • Published in
    The Journal of pharmacology…
    1993

Potency of 5-hydroxytryptamine1a agonists to inhibit adenylyl cyclase activity is a function of affinity for the "low-affinity" state of [3H]8-hydroxy-N,N-dipropylaminotetralin ([3H]8-OH-DPAT) binding.

@article{Chamberlain1993PotencyO5,
  title={Potency of 5-hydroxytryptamine1a agonists to inhibit adenylyl cyclase activity is a function of affinity for the "low-affinity" state of [3H]8-hydroxy-N,N-dipropylaminotetralin ([3H]8-OH-DPAT) binding.},
  author={Jack G. Chamberlain and Steve J. Offord and Barry B. Wolfe and L S Tyau and Heng Long Wang and Alan Frazer},
  journal={The Journal of pharmacology and experimental therapeutics},
  year={1993},
  volume={266 2},
  pages={
          618-25
        }
}
In this study, the radiolabeled 5-hydroxytryptamine1A agonist, [3H]8-hydroxy-N,N-dipropylamino tetralin ([3H]8-OH-DPAT), was shown to have both a high (Kd, 0.7 +/- 0.2 nM) and a low (Kd, 17 +/- 4 nM) affinity binding component in rat hippocampal homogenate preparations in the absence of guanine nucleotides. The high-affinity binding component was markedly reduced by the elimination of Mg++ from the incubation medium and the addition of both the nonhydrolyzable guanine nucleotide… CONTINUE READING

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