Omega-conotoxin GVIA binding to a high-affinity receptor in brain: characterization, calcium sensitivity, and solubilization
We describe unique, high-affinity binding sites for omega(/sup 125/I)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.
- Research Organization:
- Johns Hopkins Univ. School of Medicine, Baltimore, MD (USA)
- OSTI ID:
- 6801131
- Journal Information:
- J. Neurosci.; (United States), Vol. 8:9
- Country of Publication:
- United States
- Language:
- English
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RECEPTORS
TISSUE DISTRIBUTION
TOXINS
BIOCHEMICAL REACTION KINETICS
BRAIN
CALCIUM
CATIONS
CELL MEMBRANES
IODINE 125
NERVES
PEPTIDES
RABBITS
RATS
SOLUBILITY
SPECIFICITY
TRACER TECHNIQUES
ALKALINE EARTH METALS
ANIMALS
ANTIGENS
BETA DECAY RADIOISOTOPES
BODY
CELL CONSTITUENTS
CENTRAL NERVOUS SYSTEM
CHARGED PARTICLES
DAYS LIVING RADIOISOTOPES
DISTRIBUTION
ELECTRON CAPTURE RADIOISOTOPES
ELEMENTS
INTERMEDIATE MASS NUCLEI
IODINE ISOTOPES
IONS
ISOTOPE APPLICATIONS
ISOTOPES
KINETICS
MAMMALS
MATERIALS
MEMBRANE PROTEINS
MEMBRANES
METALS
NERVOUS SYSTEM
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
ORGANS
PROTEINS
RADIOISOTOPES
REACTION KINETICS
RODENTS
TOXIC MATERIALS
VERTEBRATES
550201* - Biochemistry- Tracer Techniques