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. 2012 Dec 3;288(3):1739–1749. doi: 10.1074/jbc.M112.404657

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© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 2. — Polymerization of WT and Asp-11-mutant actins. A, polymerization of WT (filled circles), D11Q (filled triangles), and D11N (filled squares) actin solutions. Final concentration of actin was 10 μm, and polymerization was monitored by the increase of light scattering at 360 nm (left abscissa). In parallel, release of phosphate from polymerizing WT (open circles) and D11Q (open triangles) actin was monitored using the EnzCheck phosphate assay kit (right abscissa). Arrow indicates light scattering of D11N actin polymer at 160 min. B, fluorescence micrograph of WT, D11Q, and D11N actin filaments stained by rhodamine-phalloidin overnight at 5 °C. For D11N actin, the partially purified fraction from Q-Sepharose column chromatography and the purified fraction by a depolymerization/polymerization cycle are shown. Bar, 10 μm. AU, arbitrary units.