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. 2021 Jan 7;148(10):1161–1170. doi: 10.1017/S0031182020002425

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© The Author(s) 2021

This is an Open Access article, distributed under the terms of the Creative Commons Attribution licence (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted re-use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. 1. — In-gel NADH dehydrogenase activity staining. (A, B) Clear native and (C) blue native gradient gel; 100 μg of mitochondrial proteins from Phytomonas serpens (PS), Blechomonas ayalai (BA), Herpetomonas tarakana (HT), Kentomonas sorsogonicus (KS), Leptomonas seymouri (LS), Novymonas esmeraldas (NE), Sergeia podlipaevi (SP) and Wallacemonas raviniae (WR) were applied to each lane. The NADH dehydrogenase activity was detected without (A, C) or with (B) 100 μm DPI. The slices with NADH dehydrogenase activity from blue native gel (C) subjected to MS analysis are marked by numbers 1–4. The positions of molecular weight markers (dimer of BSA and monomer, dimer and trimer of ferritin) are indicated.