Detection Of Low-Affinity Î±-Bungarotoxin Binding Sites In The Rat Central Nervous System
The curaremimetic neurotoxin, Î±-bungarotoxin, is shown to interact with two classes of binding sites on rat brain crude mitochondrial fraction membranes. Toxin binding sites are characterized by descriptive, preequilibrium dissociation constants of about 5 and 400 nM. There are at least as many low-affinity toxin binding sites as high-affinity sites. The existence of low- and high-affinity sites is confirmed by experiments with native toxin. Low- and high-affinity toxin binding sites are copurified as judged by sedimentation velocity and density gradient analysis, consistent with the presence of low- and high-affinity toxin binding sites on the same subcellular membrane fragments. The results may offer an explanation for the relatively low antagonistic potency of curaremimetic neurotoxins at acetylcholine-sensitive sites in the vertebrate central nervous system. Â© 1984, American Chemical Society. All rights reserved.
Digital Object Identifier (DOI)
Lukas, Ronald J., "Detection Of Low-Affinity Î±-Bungarotoxin Binding Sites In The Rat Central Nervous System" (1984). Translational Neuroscience. 200.