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.
- acidic amino acid receptor classes
- glutamate receptors
- synaptic membranes
ASJC Scopus subject areas