Binding of the radiolabeled glycine site antagonist [3H]MDL 105,519 to homomeric NMDA-NR1a receptors.

@article{Siegel1996BindingOT,
  title={Binding of the radiolabeled glycine site antagonist [3H]MDL 105,519 to homomeric NMDA-NR1a receptors.},
  author={Barry W. Siegel and Kotikanyadanam Sreekrishna and Bruce Baron},
  journal={European journal of pharmacology},
  year={1996},
  volume={312 3},
  pages={
          357-65
        }
}
We have characterized the binding of [3H]MDL 105,519 ((E)-3-(2-phenyl-2-carboxyethenyl)-4,6-dichloro-1 H-indole-2-carboxylic acid), a NMDA receptor glycine recognition site antagonist, to homomeric NMDA subunit 1a (NR 1a) receptors. Chinese hamster ovary cells (CHO-K1) were transfected with the rat NR 1a gene and cell lines stably expressing the receptor were isolated from amongst clones resistant to the neomycin analog G418. Saturation analysis indicated that the radioligand bound to the… CONTINUE READING
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