A possible role of glutathione as an endogenous agonist at the N-methyl-D-aspartate recognition domain in rat brain.

@article{Ogita1995APR,
  title={A possible role of glutathione as an endogenous agonist at the N-methyl-D-aspartate recognition domain in rat brain.},
  author={Kiyokazu Ogita and Riyo Enomoto and Fumio Nakahara and N Ishitsubo and Yukio Yoneda},
  journal={Journal of neurochemistry},
  year={1995},
  volume={64 3},
  pages={1088-96}
}
Glutathione, both reduced (GSH) and oxidized (GSSG), was effective in displacing binding of L-[3H]-glutamic acid (L-[3H]Glu) and DL-(E)-2-[3H]amino-4-propyl-5-phosphono-3- pentenoic acid ([3H]CGP-39653) in rat brain synaptic membranes, with less potent displacement of binding of DL-alpha-amino-3-hydroxy-5-[3H]-methylisoxazole-4-propionic and [3H]kainic acids. Liquid chromatographic analysis revealed that both GSH and GSSG were contaminated with L-Glu by < 1%. Both GSH and GSSG potentiated (+)-5… CONTINUE READING
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