Rehm_1988_Biochem.Biophys.Res.Commun_153_231

The binding sites of dendrotoxin I, mast cell degranulating peptide, and beta-bungarotoxin are thought to be associated with neuronal K+ channels. The different binding sites seem to reside on the same molecular assembly as each toxin can allosterically inhibit the binding of the others. Affinity chromatography on a beta-BTX Aca 22 affinity column has shown that there is an heterogeneous population of dendrotoxin I binding proteins. Two subtypes were separated: DTXI binding proteins with low affinity for beta-BTX (60-70% of total) and DTXI binding proteins with high affinity for beta-BTX (30-40% of total). Binding of 125I-DTXI and 125I-MCD to the former subtype is inhibited by beta-BTX with a low affinity (IC50 = 560 nM), while inhibition at the latter subtype occurs with a high affinity (IC50 = 10-16 nM). The DTXI binding subtype with low affinity for beta-BTX contains most (85-90%) of the binding sites for 125I-MCD.