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. 2013 Mar 5;288(16):11294–11303. doi: 10.1074/jbc.M113.458133

FIGURE 4.

FIGURE 4.

The Carb-induced response of membrane-reconstituted nAChR after injection into and consequent fusion with the plasma membrane of Xenopus oocytes. A, currents induced by 500 μm Carb were measured at −20 mV holding potential from oocytes injected with aso-nAChR (left trace) and PC-nAChR (right trace). B, a bar graph comparing maximal recorded currents, each normalized to the number of [125I]α-bungarotoxin (BTX)-binding sites, induced by 300 μm acetylcholine from individual oocytes microinjected with 125 ng of affinity-purified Torpedo nAChR protein reconstituted in either PC/PA/Chol (3:1:1 molar ratio; 0.124 ± 0.061 μA/[125I]α-bungarotoxin-binding sites/oocyte; n = 5) or PC lipid vesicles (0.0034 ± 0.0006 μA/[125I]α-bungarotoxin-binding sites/oocyte; n = 6).