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. 2014 Aug 19;289(40):28006–28018. doi: 10.1074/jbc.M114.589077

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© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 9. — Competitive dissociation of [5F]FFR-[Lys]Pg from its complex with SKΔK414 by FFR-Pm. A. Displacement of [5F]FFR-[Lys]Pg from its stabilized complex with SKΔK414 by FFR-Pm in the absence of lysine analogs is shown at dead time mixing concentrations of 20 nm [5F]FFR-[Lys]Pg, 0.5 μm SKΔK414, and 0.5 μm FFR-Pm (top) and 1.0 μm SKΔK414 and 1.0 μm FFR-Pm (bottom). B, displacement of [5F]FFR-[Lys]Pg from its stabilized complex with SKΔK414 by FFR-Pm in 50 mm 6-AHA is shown at dead time mixing concentrations of 20 nm [5F]FFR-[Lys]Pg, 0.5 μm SKΔK414, and 0.7 μm FFR-Pm (top) and 1 μm SKΔK414 and 1.4 μm FFR-Pm (bottom). C, displacement of [5F]FFR-[Lys]Pg from its stabilized complex with SKΔK414 by FFR-Pm in 50 mm benzamidine is shown at dead time mixing concentrations of 20 nm [5F]FFR-[Lys]Pg, 0.5 μm SKΔK414, and 0.5 μm FFR-Pm (top); 1 μm SKΔK414 and 1.2 μm FFR-Pm (middle); and 2 μm SKΔK414 and 2 μm FFR-Pm (bottom). Red solid lines represent the fits from numerical integration as described under “Experimental Procedures.”