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. Author manuscript; available in PMC: 2010 Feb 10.
Published in final edited form as: Bioorg Med Chem Lett. 2008 Jun 13;18(22):5856. doi: 10.1016/j.bmcl.2008.06.029

Figure 3.

Figure 3

Comparision of the inactivation of PTP1B by compounds 1, 2, 3, and hydrogen peroxide. Thiol-free PTP1B (25 nM) was added to a cuvette containing 3,3-dimethyl glutarate buffer (50 mM, pH 7.0), p-NPP (10 mM), and the hydroperoxide of interest (1, 2, 3, or H2O2) at 24 °C. Enzyme inactivation progress curves showing the amount of PTP1B activity remaining as a function of time were obtained by monitoring the enzyme-catalyzed release of p-nitrophenolate ion from the substrate p-NPP at 410 nm. Note: curves for control “no inactivator” and 150 nM H2O2 are overlapping.