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. 2019 Jan 10;9:33. doi: 10.1038/s41598-018-37230-1

Figure 1.

Figure 1

(a) SEC analyses of TTR samples (2 mg/ml) aged at different incubation times at 4 °C using Superdex 200 size exclusion column (GE Healthcare). The TTR samples were incubated in 20 mM sodium acetate buffer (pH 4.4) and 300 μL of the sample was injected to the column after the pH was adjusted to 7. T and D denote tetramer and dimer, respectively. The protein eluting around 73 ml was determined to be a dimer by mass spectrometry (Fig. S1). (b) SEC analyses of TTR samples (uncross-linked) at different concentrations (total monomer concentration) at 4 °C. A mixture of dimeric and native TTR purified by SEC was concentrated to the different concentrations and subjected to the SEC column without further incubation. (c) TEM image of the TTR oligomer eluting at 53 ml in Fig. 1a. (d) TEM image of the TTR oligomer eluting at 61 ml. The elution volumes of the hexamer (H), tetramer (T), and dimer (D) are slightly higher than those of the cross-linked TTR shown in Fig. S2.