BINDING OF [3H]KAINIC ACID, AN ANALOGUE OF l‐GLUTAMATE, TO BRAIN MEMBRANES

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Abstract
—The specific binding of [3H]kainic acid to synaptic membranes from rat brain was saturable with a dissociation constant of about 60 nm. The apparent maximal number of binding sites was about 1 pmol/mg protein. The most effective displacer of specific [3H]kainic acid binding was quisqualic acid, a powerful excitant which is structurally similar to l‐glutamate. However, quisqualic acid was one‐third as potent a displacer as kainic acid itself. l‐Glutamate was the next potent in displacing [3H]kainic acid binding, but also was less effective (1/25) than kainic acid itself. All other compounds including suspected neurotransmitters were at least an order of magnitude lower in potency compared to l‐glutamate. When various tissues and brain regions were tested for specific [3H]kainic acid binding, we found the specified binding was localized to grey matter in the brain. In studies of subcellular fractionation of the brain, we found that crude synaptosomal membrane preparations were most enriched in specific [3H]kainic acid binding. Specific [3H]kainic acid binding in various regions of the rat brain varied 5‐ to 6‐fold.