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Steady-state kinetics data for the determination of Ki for 15-LOX-2 with MLS000536924.

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posted on 11.08.2014, 02:45 by J. Brian Jameson II, Auric Kantz, Lena Schultz, Chakrapani Kalyanaraman, Matthew P. Jacobson, David J. Maloney, Ajit Jadhav, Anton Simeonov, Theodore R. Holman

(A) Initial enzymatic rate (µmol/min/mg) versus substrate concentration (µM) at inhibitor concentrations of 0 µM (open circles) 1 µM (open squares) 2 µM (open diamonds) and 5 µM (closed circles) fitted to the Henri–Michaelis– Menten equation to yield Vmax (µmol/min/mg) and Vmax/KM (µmol/min/mg/µM). All measurements were done in triplicate. (B) KM/Vmax replot (closed circles) (units are µM/µmol/min/mg) versus [Inhibitor] (µM), which yielded a Ki of 2.5+/−0.5 µM. 1/Vmax replot (open circles) (units are 1/µmol/min/mg) versus [Inhibitor] (µM), value did not change with increasing inhibitor concentration, indicating competitive inhibition.

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