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. 1998 Aug 1;112(2):243–257. doi: 10.1085/jgp.112.2.243

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A463C decreases the internal Ba⁺⁺ affinity of the channel. Internal Ba⁺⁺ affinity was measured in both the wild-type channel and A463C with steps to +100 mV in the presence of symmetrical 140 mM KCl. Wild-type channel block in the presence of 100 (A) and 1,000 (C) μM internal Ba⁺⁺. A463C channel block in the presence of 100 (B) and 1,000 (D) μM internal Ba⁺⁺. The data are quantified as percent current versus Ba⁺⁺ concentration (E). (•) Wild-type data, (○) A463C data. The single binding isotherm fits yield K _ds of 75 μM for the wild-type channel and 350 μM for A463C.