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

43 Citations (Scopus)

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

Fingerprint

Synaptic Membranes
Glutamate Receptors
Freezing
Population
Octoxynol
Glutamic Acid
Binding Sites
Pharmacology
Ions
Proteins

Keywords

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

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Freezing eliminates a specific population of l-glutamate receptors in synaptic membranes. / Fagg, Graham E.; Edward Mena, E.; Monaghan, Daniel T; Cotman, Carl W.

In: Neuroscience Letters, Vol. 38, No. 2, 29.07.1983, p. 157-162.

Research output: Contribution to journalArticle

Fagg, Graham E. ; Edward Mena, E. ; Monaghan, Daniel T ; Cotman, Carl W. / Freezing eliminates a specific population of l-glutamate receptors in synaptic membranes. In: Neuroscience Letters. 1983 ; Vol. 38, No. 2. pp. 157-162.
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