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. 2008 Jun 20;283(25):17615–17623. doi: 10.1074/jbc.M709844200

FIGURE 1.

FIGURE 1.

ELISA analysis of the interaction of recombinant equine Igs with FgBP1. A, subclass specificity of the interaction. FgBP1 bound strongly to IgG4 and IgG7, but the remaining five IgG subclasses and IgA showed little or no binding. Open diamond, reqIgG1; cross, reqIgG2; open square, reqIgG3; open circle, reqIgG4; open triangle, reqIgG5; plus sign, reqIgG6; closed triangle, reqIgG7; closed square, reqIgA. B and C, pH dependence of the binding to FgBP1. For both equine IgG4 (B) and IgG7 (C), binding to FgBP1 was most efficient at pH 7.4-8.5. Closed diamond, pH 5.0; open square, pH 7.4; closed triangle, pH 8.5. Binding of reqIgGs is expressed as absorbance obtained for the binding to FgBP1 minus absorbance for binding to the FgBPM- control (binding to the latter was typically <0.15 absorbance units). The mean (±S.E.) of three independent experiments is shown.