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1.
Figure 3

Figure 3. From: Amyloid ?-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process.

Concentration dependence of Aβ aggregation equilibrium in 20 mM sodium phosphate, pH 8, 200 μM EDTA, 0.02% NaN3. Samples were allowed to aggregate for 84−96 h, and large aggregates were removed by centrifugation. The concentration of soluble Aβ determined by ELISA is plotted versus total concentration (from acid hydrolysis): (A) low concentration samples, linear axes; (B) all samples, logarithmic axes.

Erik Hellstrand, et al. ACS Chem Neurosci. 2010 January 20;1(1):13-18.
2.
Figure 1

Figure 1. From: Amyloid ?-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process.

(A) Isolation of monomeric Aβ(M1−42) by gel filtration on a Superdex 75 column in 20 mM sodium phosphate buffer, pH 8, with 200 μM EDTA and 0.02% NaN3. The monomer is collected between the dashed red lines and is free from higher Aβ assembly forms (shoulder before monomer peak) and buffer and salts (tall peak after the monomer peak). (B) Kinetic traces by ThT fluorescence for 32 replicates at concentrations 2.4 (black), 1.2 (red), and 0.6 μM (green) Aβ(M1−42) in 20 mM sodium phosphate, pH 8, 200 μM EDTA, 0.02% NaN3, 20 μM ThT. The first 7 h are shown.

Erik Hellstrand, et al. ACS Chem Neurosci. 2010 January 20;1(1):13-18.
3.
Figure 2

Figure 2. From: Amyloid ?-Protein Aggregation Produces Highly Reproducible Kinetic Data and Occurs by a Two-Phase Process.

Concentration dependence of Aβ aggregation kinetics in 20 mM sodium phosphate, pH 8, 200 μM EDTA, 0.02% NaN3, 20 μM ThT. (A) Kinetics of aggregation monitored using ThT fluorescence. Data for the 13 highest concentrations in a single experiment are shown with Aβ(Μ1−42) concentrations of 5.8 (black), 4.9 (brown), 3.9 (red), 2.9 (orange), 2.6 (yellow), 2.2 (green-yellow), 1.85 (yellow-green), 1.65 (green), 1.46 (cyan), 1.31 (light blue), 1.17 (blue), 1.07 (marine blue), and 0.97 (purple) μM. (B) Fitting of eq 1 to one of the fibrillation traces in panel A, with data points as filled circles and the fitted curve as a solid line. The values for t1/2 as obtained by the fit and tlag by eq 2 are indicated. (C) Lagtime obtained by fitting eq 1 to 672 kinetic traces in seven sets of data (in black, red, green, magenta, cyan, yellow, and blue) versus Aβ(Μ1−42) concentration. Each point is average of 3−32 replicates of the same solution. The solid line is a power function with exponent −1.48 fitted to all data points. Inset: same data with logarithmic axes.

Erik Hellstrand, et al. ACS Chem Neurosci. 2010 January 20;1(1):13-18.

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