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. 2017 May 18;16(7):2560–2570. doi: 10.1021/acs.jproteome.7b00121

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Copyright © 2017 American Chemical Society

This is an open access article published under a Creative Commons Attribution (CC-BY) License, which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.

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Homogeneity and thermal stability of the IgA isotypes IgA1, IgA2m(1), and IgA2m(2). (A) SE-HPLC measurements of the different IgA isotypes purified from HEK293-6E cells (HEK) and N. benthamiana (NB). To facilitate comparison between the different variants the elution time of IgA1 produced in HEK293 cells is marked with dashed lines. (B) Differential scanning calorimetry analysis of IgAs produced in N. benthamiana (NB) and HEK293-6E cells (HEK). The black bold lines show representative DSC thermograms, whereas the gray lines are the deconvoluted peaks of each domain transition. For comparison, the three midterm transitions of the CH2, Fab, and CH3 domain (T_m1 = 71.6 ± 0.1 °C, T_m2= 74.3 ± 0.05 °C, and T_m3 = 76.6 ± 0.1 °C) of IgA1 produced in HEK293 cells are marked with dashed lines.