Figure 5.
Figure 5. Inhibition of the Kir6.2-ΔC26 mutant by SpTx-1. (A) Currents of the Kir6.2-ΔC26 mutant channels, recorded in the absence (black trace) or presence (red trace) of 10 nM synthetic SpTx-1. (B) Fractions of currents, recorded from WT and Kir6.2-ΔC26 mutant channels, are plotted against the concentration of recombinant SpTx-1. The curves superimposed on data correspond to the fits of an equation for a bimolecular reaction. The fitted Kd values are (1.53 ± 0.13) × 10−8 M (n = 6) for WT channels and (8.52 ± 0.37) × 10−9 M (n = 6) for the Kir6.2-ΔC26 mutant channels. Data represent the mean ± SEM.

Inhibition of the Kir6.2-ΔC26 mutant by SpTx-1. (A) Currents of the Kir6.2-ΔC26 mutant channels, recorded in the absence (black trace) or presence (red trace) of 10 nM synthetic SpTx-1. (B) Fractions of currents, recorded from WT and Kir6.2-ΔC26 mutant channels, are plotted against the concentration of recombinant SpTx-1. The curves superimposed on data correspond to the fits of an equation for a bimolecular reaction. The fitted Kd values are (1.53 ± 0.13) × 10−8 M (n = 6) for WT channels and (8.52 ± 0.37) × 10−9 M (n = 6) for the Kir6.2-ΔC26 mutant channels. Data represent the mean ± SEM.

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