Figure 7.
Figure 7. Effect of deglycosylation on the binding of Hanatoxin. (A and B) Current traces represent ionic currents in response to voltage steps to −50, −40, 0, and +40 mV from a holding potential of −80 mV. Tail currents shown were in response to voltage of −50 mV. In A, 200 nM HaTx was tested on unmodified channels (n = 5) and in B after deglycosylation by PNGase F (n = 4). (C) Relative probability of opening estimated from the tail currents. Data in the presence of HaTx were normalized with respect to the control (black and gray symbols) or immediately after PNGase F treatment (red and cyan symbols). These experiments were performed by using the two-microelectrode voltage-clamp technique. Error bars represent mean ± SEM. DeGly, deglycosylation.

Effect of deglycosylation on the binding of Hanatoxin. (A and B) Current traces represent ionic currents in response to voltage steps to −50, −40, 0, and +40 mV from a holding potential of −80 mV. Tail currents shown were in response to voltage of −50 mV. In A, 200 nM HaTx was tested on unmodified channels (n = 5) and in B after deglycosylation by PNGase F (n = 4). (C) Relative probability of opening estimated from the tail currents. Data in the presence of HaTx were normalized with respect to the control (black and gray symbols) or immediately after PNGase F treatment (red and cyan symbols). These experiments were performed by using the two-microelectrode voltage-clamp technique. Error bars represent mean ± SEM. DeGly, deglycosylation.

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