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Research Article

PTP1B inhibitory effects of tridepside and related metabolites isolated from the Antarctic lichen Umbilicaria antarctica

, , , , &
Pages 1133-1137 | Received 27 Aug 2008, Accepted 12 Nov 2008, Published online: 21 Jul 2009

Figures & data

Figure 1. The chemical structures of 1–4.

Figure 1.  The chemical structures of 1–4.

Figure 2. Dose-dependent inhibition of compound 1 on PTP1B enzyme activity. The means with S.D. of three independent determinations are shown.

Figure 2.  Dose-dependent inhibition of compound 1 on PTP1B enzyme activity. The means with S.D. of three independent determinations are shown.

Figure 3. Non-competitive inhibitor of PTP1B. (a) Substrate titration reveals that compound 1 is a classical non-competitive inhibitor that inhibits substrate catalysis (Vmax), but not substrate binding (constant Km). (b) Plots of Vmax and Km as a function of concentration of compound 1. Values were derived from nonlinear regression analysis in (a).

Figure 3.  Non-competitive inhibitor of PTP1B. (a) Substrate titration reveals that compound 1 is a classical non-competitive inhibitor that inhibits substrate catalysis (Vmax), but not substrate binding (constant Km). (b) Plots of Vmax and Km as a function of concentration of compound 1. Values were derived from nonlinear regression analysis in (a).

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