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. 2010 Feb 26;5(2):e9356. doi: 10.1371/journal.pone.0009356

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This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

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(A) Sensorgrams for Cyr61 (in nM: a, 40; b, 20; c, 5; d, 2.5) binding to immobilized monomeric VTNC. (B) Sensorgrams show Cyr61 (in nM: a, 50; b, 25, c, 12.5; d, 6.25) binding to multimeric VTNC. Data were fitted using global two-state binding model. RU, resonance units. (C) and (D) solid-phase-binding assay for Cyr61 (0–1 µM) interaction with immobilized monomeric or multimeric VTNC, respectively. Binding was estimated with anti-Cyr61 monoclonal antibody followed by alkaline-phosphatase labeled anti-mouse secondary antibody and appropriate substrate as described in Materials and Methods. (E) and (F) Semi log-transformation of the data depicted in (C) and (D), respectively. The (apparent) K_D values for Cyr61/VTNC interactions were calculated by nonlinear regression analysis of the binding data according to the Langmuir isotherm equation. All treatments were performed in quadruplicate or quintuplicate (n = 3).