Interaction of sulfhydryl reagents with A-type channels of Lymnaea neurons

The effect of sulfhydryl reagents on macroscopic inactivation of A-current in internally perfused Lymnaea neurons under voltage-clamp conditions was investigated. It was found that the binding of Hg2+ rather than PHMB with channel proteins resulted in a strong decrease of the peak current and the inactivation rate. Hg2+ markedly influenced the steady-state inactivation but did not change the rate of recovery from inactivation. It was found that both reagents reacted with the same groups of the channel protein and that those are most likely sulfhydryl groups. These groups seemed not to be involved in the gating charge movement. Hg2+ ions can immobilize some part of the gating charge thereby resulting in strong changes of the steady-state inactivation.