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. 2022 Jun 13;204(7):e00078-22. doi: 10.1128/jb.00078-22

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Copyright © 2022 Heryakusuma et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license.

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FIG 1 — Analysis for subunit size and quaternary structure of ANME2c-FsrII-6D. (A) SDS-PAGE gel with F₄₂₀ affinity-purified recombinant ANME2c-FsrII-6D. Lanes: M, protein ladder; 1, ANME2c-FsrII-6D preparation. Fsr, ~70 kDa, intact FsrII; Fsr′, ~52, ~55, and ~58 kDa degradation products of FsrII. (B) Size exclusion-chromatographic analysis of ANME2c-FsrII-6D. The largest peak corresponded to Fsr (20 μg protein). (Inset) Elution of the following calibration standards (catalog number 151-1901; Bio-Rad, Hercules, CA): a, thyroglobulin, 670,000 Da; b, gamma globulin, 158,000 Da; c, ovalbumin, 44,000 Da; d, myoglobin, 17,000 Da; e, vitamin B₁₂, 1,350 Da. Figure S1 shows the calibration plot.