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. Author manuscript; available in PMC: 2009 Nov 11.

Published in final edited form as: Biochemistry. 2008 Oct 18;47(45):11894–11899. doi: 10.1021/bi801211t

A. Time course for the 1-naphthol to 1-naphthyl sulfate exchange reaction monitoring the appearance of [¹⁴C]-1-naphthyl sulfate. Concentrations of PAPS, PAP, 1-naphthol, 1-naphtyl sulfate are 20 ∝M, 4 ∝M, 50 ∝M, and 5 ∝M, respectively, consistent with the equilibrium constant. The concentration of added [¹⁴C]-1-naphtol pulse is 0.5 ∝M. Each reaction included 7.5 ∝g SULT1A1 in 50 ∝L phosphate buffer (final concentration: 50 mM, pH 6.2) at 37°C. The curve fitting was done using Enzyme Kinetics Module 1.2 (SigmaPlot). B. First order plot of the data in A as ln(1 − f) vs. time.

A. Time course for the 1-naphthol to 1-naphthyl sulfate exchange reaction monitoring the appearance of [¹⁴C]-1-naphthyl sulfate. Concentrations of PAPS, PAP, 1-naphthol, 1-naphtyl sulfate are 20 ∝M, 4 ∝M, 50 ∝M, and 5 ∝M, respectively, consistent with the equilibrium constant. The concentration of added [¹⁴C]-1-naphtol pulse is 0.5 ∝M. Each reaction included 7.5 ∝g SULT1A1 in 50 ∝L phosphate buffer (final concentration: 50 mM, pH 6.2) at 37°C. The curve fitting was done using Enzyme Kinetics Module 1.2 (SigmaPlot). B. First order plot of the data in A as ln(1 − f) vs. time.