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. Author manuscript; available in PMC: 2011 Sep 10.
Published in final edited form as: Physiol Res. 2010 Apr 20;59(6):927–935. doi: 10.33549/physiolres.931979

Fig. 2.

Fig. 2

Effects of the disruption of disulfide bonds on the deactivation kinetics of P2X4R. (A) Sample recordings of ectodomain cysteine double mutants showing differences in the current decay after washout of ATP. All traces were recorded 4-6 min after the application of 3 μM IVM, and a non-desensitizing concentration of ATP (1-3 μM for SS1-3 and SS5 and 30 μM for SS4) was used for stimulation. The time of ATP application is indicated by horizontal bars. Numbers below the traces indicate the deactivation time constant (τoff) values. (B) Comparison of IVM effects on the deactivation time constant (τoff) of A- (closed bars) and T- (open bars) single-point mutants of cysteine residues forming the disulfide bonds SS1-5.