Binding Sites for [³H]Glutamate and [³H]Aspartate in Human Cerebellum

Abstract

The binding of [3H]aspartate and [3H]glutamate to membranes prepared from frozen human cerebellar cortex was studied. The binding sites differed in their relative proportions, their inhibition by amino acids and analogues, and by the effects of cations. A proportion (about 30%) of [3H]glutamate binding was to sites similar to those labelled by [3H]aspartate. An additional component of [3H]glutamate binding (about 50%) was displaced by quisqualate and alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid, and may represent a "quisqualate-preferring" receptor. Neither N-methyl-D-aspartic acid-sensitive nor DL-2-amino-4-phosphonobutyric acid-sensitive [3H]glutamate binding was detected.