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. Author manuscript; available in PMC: 2011 Dec 8.
Published in final edited form as: Biochemistry. 1997 Mar 18;36(11):3126–3132. doi: 10.1021/bi962065d

Figure 4.

Figure 4

Aspartate saturation kinetics in the presence of nucleotide effectors for native Sm (A), native Ec (B), and chimera SM:rS5′ec (C) ATCase holoenzyme. The aspartate saturation of ATCase activity was determined in the presence of (□) either 4 mM (for the native Sm enzyme) or 2 mM ATP (for the native Ec enzyme and the chimeric enzyme, respectively), (△) 2 mM CTP, (▽) 2 mM UTP, (◇) 2 mM CTP plus 2 mM UTP, and (○) without any nucleotide effector. Standard assay conditions were used, and each curve is the average of at least three independent assays.