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. 2013 Aug 13;8(8):e73888. doi: 10.1371/journal.pone.0073888

Figure 5. Kinetics of ATP hydrolysis by mutant α3β3γS3Cε133C.

Figure 5

ATPase activities of α3β3γS3Cε133C (S3C), and α3β3γWTε133C (WT) at 2 mM ATP were determined. The α3β3γε complex of was added to 3 nM at the times indicated by the first arrowheads. (A) DTT (50 mM) and LDAO (0.1%) were added at the times indicated by the second and third arrowheads, respectively. (B) The order of addition of DTT and LDAO was reversed.