Abstract
Membranes obtained from post-mortem human spinal cord specimens bound [ 3H]resiniferatoxin (RTX) with an affinity of 11 nM in a non-cooperative fashion. This binding behaviour contrasted with the high affinity [ 3H]RTX binding ( K d = 24 pM) to rat spinal cord membranes which displayed apparent positive cooperativity (cooperativity index = 1.8) but was in accord with the low affinity ( K d = 5 nM) non-cooperative RTX binding to guinea pig spinal cord preparations. We conclude that the [ 3H]RTX binding assay utilizing post-mortem human spinal cord membranes affords a novel biochemical approach to explore structure-activity relations at human vanilloid receptors.
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