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. Author manuscript; available in PMC: 2011 Jun 1.
Published in final edited form as: Clin Proteomics. 2010 Jun 1;6(1-2):6–17. doi: 10.1007/s12014-009-9040-5

Fig. 6.

Fig. 6

Quantity changes of transthyretin (TTR) isoforms. Locations of TTR isoforms are indicated by circles in the partial image of two-dimensional gel described in Fig. 4 and numbered 1 to 6 from acidic to basic. Average fluorescence intensity of an indicated isoform is plotted for control (n=5) and high-fat fed (n=8) mice. Plasma sample from each mouse was resolved on a two-dimensional gel and image was captured using a laser-scanner (Pharos FX plus, Bio-Rad) with the excitation–emission setting at 473–520 nm. Detection, matching, and quantification of each protein spot were performed using the PDQuest 7.0.1 program (Bio-Rad) assuming loading of equal amount of total protein per gel. All of TTR spots were cut out from the polyacrylamide gel and analyzed by MS/MS at the Michigan Proteome Consortium. Concentration of total TTR (top right panel) was estimated as a sum of fluorescence intensities of all isoforms. Error bars represent the SEM. Statistical analysis was performed using ANOVA. Single asterisk indicates p<0.05