Effect of mutations to the lidocaine binding site of ELIC on the time course of desensitization
| Channel | τdesensitization | P-value | Number of patches | |
| (mean ± SE; ms) | (range; ms) | |||
| Wild-type ELIC | 4,533 ± 584 | 2,397–8,026 | – | 9 |
| I266A ELIC | 6,324 ± 1,132 | 2,834–8,081 | 0.11 | 5 |
| Y14′A ELIC | 272 ± 96 | 146–415 | 1.5 × 10−3 | 3 |
| Y17′A ELIC | 383 ± 64 | 282–541 | 4.7 × 10−4 | 4 |
| Y14′A + Y17′A ELICa | 112 (56%) | – | – | 7 |
| 4,820 | – | |||
| Channel | τdesensitization | P-value | Number of patches | |
| (mean ± SE; ms) | (range; ms) | |||
| Wild-type ELIC | 4,533 ± 584 | 2,397–8,026 | – | 9 |
| I266A ELIC | 6,324 ± 1,132 | 2,834–8,081 | 0.11 | 5 |
| Y14′A ELIC | 272 ± 96 | 146–415 | 1.5 × 10−3 | 3 |
| Y17′A ELIC | 383 ± 64 | 282–541 | 4.7 × 10−4 | 4 |
| Y14′A + Y17′A ELICa | 112 (56%) | – | – | 7 |
| 4,820 | – | |||
The macroscopic recordings obtained from this double mutant had low peak-current amplitudes. Hence, we averaged 27 responses from 7 different outside-out patches to obtain a proper fit; the desensitization time course was fitted adequately with two exponential components. In an attempt to compare these double-exponential kinetics with the mono-exponential kinetics of the wild type and single mutants, we calculated the corresponding decay half-times. These values were as follows (in ms): 3,142, 189, 265, and 219 for wild-type, Y14′A, Y17′A, and Y14′A + Y17′A ELIC, respectively.