Add time:08/26/2019         Source:sciencedirect.com

[3H]Batrachotoxinin A-20-α-benzoate (BTX-B) bound to a single class of high affinity (Kd = 79 nM), low capacity (Bmax = 4.8 pmol/mg protein) sites associated with voltage-sensitive sodium channels in mouse brain vesicle preparations. DDT stimulated the specific binding of 20 nM [3H]BTX-B, producing half-maximal enhancement at 14 μM and maximal (2-fold) enhancement at 100 μM. Equilibrium saturation studies of [3H]BTX-B binding in the presence of 100 μM DDT showed that this compound produced a 1.8-fold increase in the affinity of sodium channels for [3H]BTX-B (Kd = 43 nM) but had little effect on binding capacity (Bmax = 5.8 pmol/mg protein). Kinetic studies revealed that the increase in affinity resulted primarily from a decrease in the rate of dissociation of the ligand-receptor complex. These findings show that [3H]BTX-B is a useful allosteric probe of the binding of DDT to its site of action on sodium channels.

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