| Literature DB >> 2845019 |
J A Wagner1, A M Snowman, A Biswas, B M Olivera, S H Snyder.
Abstract
We describe unique, high-affinity binding sites for omega[125I]conotoxin GVIA in membranes from rat brain and rabbit sympathetic ganglia which appear to be primarily associated with N-type voltage-dependent calcium channels. The dissociation constant (KD) for the toxin in rat brain membranes is 60 pM. Physiologic extracellular concentrations of calcium inhibit toxin binding noncompetitively (IC50 = 0.2 mM). The regional distribution of the binding sites in rat brain differs markedly from that of dihydropyridine calcium antagonist receptors associated with L-type calcium channels. In detergent-solubilized brain membranes, toxin binding retains the same affinity, specificity, and ionic sensitivity as in particulate preparations.Entities:
Mesh:
Substances:
Year: 1988 PMID: 2845019 PMCID: PMC6569423
Source DB: PubMed Journal: J Neurosci ISSN: 0270-6474 Impact factor: 6.167