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. Author manuscript; available in PMC: 2012 Aug 16.
Published in final edited form as: Biochemistry. 2011 Jul 15;50(32):6888–6900. doi: 10.1021/bi2007993

Figure 5. Effects of Sucrose on the Steady-State Kinetic Parameters for SRPK1.

Figure 5

Initial velocities for SRPK1 are plotted as a function of total SRSF1 at fixed ATP (A) or as a function of ATP at fixed SRSF1 (C) using 0% (●), 10% (○), 25% (▲), and 30% (△) sucrose. In the absence of sucrose, the kcat and Km for SRSF1 are 56 ± 5 min−1 and 70 ± 6 nM using fixed ATP (100 μM) and the kcat and Km for ATP are 50 ± 5 min−1 and 12 ± 2 μM using fixed SRSF1 (1 μM). The effects of added sucrose on the relative steady-state kinetic parameters [kcat°/kcat and (kcat/Km)°/(kcat/Km)] are plotted as a function of relative solvent viscosity (ηrel) under conditions of varying SRSF1 (B) or ATP (D). For varying SRSF1, kcatη and (kcat/Km)η are 1.2 ± 0.16 and 0.90 ± 0.10. For varying ATP, kcatη and (kcat/Km)η are 1.2 ± 0.18 and 1.0 ± 0.05. Initial velocities for SRPK1 as a function of Block Mutant are plotted in panel (E) at fixed ATP (100 μM). In the absence of sucrose, the kcat and Km for SRSF1 are 2.4 ± 0.25 min−1 and 2.1 ± 0.60 μM. For varying Block Mutant,kcatη and (kcat/Km)η are −.020 ± 0.043 and 0.090 ± 0.010.