[Solubilization of beta-bungarotoxin-binding protein from rat diaphragm and inhibition of its binding by some other presynaptic neurotoxins].

The mechanism of the transmitter release-blocking action of beta-bungarotoxin at neuromuscular junctions is probably related to the binding of the toxin to a presynaptic voltage-dependent K+ channel. In this paper we report the solubilization of beta-bungarotoxin-binding protein from rat diaphragm membrane preparations with Triton X-100. The specific binding activities of the detergent extracts are 200-400 fmol/mg of protein, and the yields are about 50%-70%. The binding of 125I-beta-bungarotoxin to the extracts could be completely inhibited by dendrotoxin, with an IC50 of about 8 x 10(-8) mol.L. Another beta-neurotoxin, beta-agkistrodotoxin, however, could not inhibit the 125I-beta-bungarotoxin binding at all. This indicates that the acting sites of beta-agkistrodotoxin on the presynaptic membranes are different from those of beta-bungarotoxin.