Abstract
Guanine nucleotides (GNs), including GMP, displace [ 3H]kainic acid binding to chick cerebellar lysed and vesiculated membranes. Saturation studies of [ 3H]GppNHp binding, under conditions that prevent the occupation of the nucleotide binding sites in G-proteins, demonstrate the existence of extracellular membrane receptors specific for guanine nucleotides. Affinity-labeling of a vesicle preparation with [α- 32P]GTP gives one single labeled band, upon electrophoresis, with an apparent molecular mass of 50 kDa. Additional experiments with partially purified kainate receptors suggest that the GN extracellular sites may overlap, at least partially, the kainic acid binding sites, being then responsible for the displacement of [ 3H]kainic acid by GNs. The physiological significance of these findings remains unclear.
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