Fig. 3. The impact of β2N265 mutations on maximal γ-aminobutyric acid (GABA) efficacy. Each  panel displays a voltage-clamp current sweep from an oocyte expressing different types of GABA receptor type A (GABAA) receptors. Currents were elicited first with 10 mm GABA for 4 s (  open bar ), then with 10 mm GABA plus 2 μm alphaxalone (  solid bar ). Maximal GABA currents were enhanced by alphaxalone in all three receptors. The arrows point to the GABA current immediately before alphaxalone enhancement, which was used to calculate GABA efficacy. (  A ) Wild-type α1β2γ2L; (  B ) α1β2(N265S)γ2L; (  C ) α1β2(N265M)γ2L. Alphaxalone enhances α1β2(N265M)γ2L more than wild-type or α1β2(N265S)γ2L receptors, indicating that GABA efficacy is lower in α1β2(26 5m)γ2L than in the other channels. 

Fig. 3. The impact of β2N265 mutations on maximal γ-aminobutyric acid (GABA) efficacy. Each  panel displays a voltage-clamp current sweep from an oocyte expressing different types of GABA receptor type A (GABAA) receptors. Currents were elicited first with 10 mm GABA for 4 s (  open bar ), then with 10 mm GABA plus 2 μm alphaxalone (  solid bar ). Maximal GABA currents were enhanced by alphaxalone in all three receptors. The arrows point to the GABA current immediately before alphaxalone enhancement, which was used to calculate GABA efficacy. (  A ) Wild-type α1β2γ2L; (  B ) α1β2(N265S)γ2L; (  C ) α1β2(N265M)γ2L. Alphaxalone enhances α1β2(N265M)γ2L more than wild-type or α1β2(N265S)γ2L receptors, indicating that GABA efficacy is lower in α1β2(26 5m)γ2L than in the other channels. 

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