Freezing eliminates a specific population of l-glutamate receptors in synaptic membranes

Graham E. Fagg, E. Edward Mena, Daniel T. Monaghan, Carl W. Cotman

Research output: Contribution to journalArticle

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Abstract

The binding of l-[3H]glutamate (l-Glu) to freeze-thawed synaptic membranes (SPMs) exhibited saturation kinetics, with Kd 507 nM and Bmax 6.99 pmol/mg protein. The effects of ions, the susceptibility to Triton X-100 and the pharmacological properties of the binding indicated that those sites detected in freeze-thawed SPMs were only of the C1-/Ca2+-independent type. The C1-/Ca2+-dependent (2-amino-4-phosphonobutyrate-sensitive) l-Glu binding sites which are additionally present in fresh SPMs are abolished by freezing.

Original languageEnglish (US)
Pages (from-to)157-162
Number of pages6
JournalNeuroscience Letters
Volume38
Issue number2
DOIs
StatePublished - Jul 29 1983

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Keywords

  • 2-amino-4-phosphonobutyrate
  • acidic amino acid receptor classes
  • freezing
  • glutamate receptors
  • ions
  • synaptic membranes

ASJC Scopus subject areas

  • Neuroscience(all)

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