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ATP and UTP saturation curves in the presence of 2 mM UTP or 2 mM ATP as compared to the one in the absence of other nucleotide effectors for native Sm (A), native Ec (B), and chimera SM:rS5′ec (C) ATCase holoenzyme. The saturation kinetics of the effects of varying ATP (●), varying ATP in the presence of UTP (○), varying UTP (■), and varying UTP in the presence of ATP (□) on the activity of ATCase were determined in the same way as described in Figure 5.
