Detection Of Low-Affinity α-Bungarotoxin Binding Sites In The Rat Central Nervous System

Department

neurobiology

Document Type

Article

Abstract

The curaremimetic neurotoxin, α-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. © 1984, American Chemical Society. All rights reserved.

Publication Date

1-1-1984

Publication Title

Biochemistry

ISSN

00062960

Volume

23

Issue

6

First Page

1160

Last Page

1164

Digital Object Identifier (DOI)

10.1021/bi00301a020

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