Figure 3: Assay of recombinant TTR A108V and TTR A108I tetrameric stability by IEF. | Scientific Reports

Figure 3: Assay of recombinant TTR A108V and TTR A108I tetrameric stability by IEF.

From: Cavity filling mutations at the thyroxine-binding site dramatically increase transthyretin stability and prevent its aggregation

Figure 3

(A) Recombinant TTR variants were isolated by native PAGE electrophoresis and then separated by IEF in semi-dissociating conditions (4 M urea). All samples were run in the same gel, but in the case of TTR V30M not side by side. This is a representative picture selected from the 3 replicas considered for the quantification presented in (B). (B) Relative abundance of tetramer was calculated based on the ratio of intensity of tetramer bands (% Tetramer) over intensity of all TTR bands (Total TTR) in samples from recombinant proteins. **P < 0.01; ***P < 0.001 (Student’s t-test). Error bars indicate SD.

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