Abstract: An enzyme‐linked fluorometric assay is described for the continuous monitoring of the unidirectional efflux of glutamate from guinea‐pig synaptosomes. Glutamate efflux from freshly suspended, polarized synaptosomes occurs at 0.35–0.39 nmol min−1 mg of protein−1 and is not significantly affected by external Ca2+. KC1 depolarization (30 mM KCI) in the absence of Ca2+ doubles this rate, whereas in the presence of Ca2+, the initial kinetics of the assay are consistent with the release in the first 5 s of 0.6 nmol mg of protein−1. The final extent of Ca2+‐dependent release amounts to 1.9 nmol mg of protein−1, or 8.5% of the total intrasynaptosomal glutamate content. Preincubation of synaptosomes at 30°C for 2 h before depolarization leads to a decrease in Ca2+‐independent release and an increase in Ca2+‐dependent release, consistent with an intrasynaptosomal relocation of the amino acid.
Journal of Neurochemistry – Wiley
Published: Jul 1, 1987
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