Fig. 5: Stimulation of the steady-state ATPase activity of wild-type CCT/TRiC and the double mutant by α-lactalbumin. | Communications Biology

Fig. 5: Stimulation of the steady-state ATPase activity of wild-type CCT/TRiC and the double mutant by α-lactalbumin.

From: Reduced ADP off-rate by the yeast CCT2 double mutation T394P/R510H which causes Leber congenital amaurosis in humans

Fig. 5

Initial velocities of ATP hydrolysis by the tagged wild-type CCT/TRiC and the double mutant were measured as a function of α-lactalbumin concentration at a fixed ATP concentration of 300 μM. The final oligomer concentration of CCT/TRiC was 20 nM. The data for each variant were normalized by its steady-state ATPase activity in the absence of α-lactalbumin. See Materials and Methods for more details. Error bars represent standard errors.

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