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. 2023 Mar 8;10:1160860. doi: 10.3389/fmolb.2023.1160860

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Copyright © 2023 Tannous, Stellbrinck, Hoter and Naim.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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The interaction of SI and MGAM proteins is sustained in BBMs solubilized with DOC/TX-100 buffer. (A) BBMs were solubilized with DOC/TX-100 buffer as described in the material and methods and processed for immunoprecipitation as described in Figure 2. Similar to Figure 2A, Western blot revealed co-immunoprecipitated SUC and IM with MGAM as shown in the two right lanes. The two left lanes revealed immunoprecipitated SUC and IM with their specific antibodies comparable with the proteins in their neighboring co-immunoprecipitation lanes. (B) BBMs were solubilized as described in (A) and the immunoprecipitates of the two studied disaccharidases were analyzed by Western blot. Similar to Figure 2B, immunoblotting revealed co-immunoprecipitated MGAM protein in the right lane while the left lane contained immunoprecipitated MGAM control. SUC and IM were recognized by HBB 2/614 (anti-SUC) and HBB 3/705 (anti-IM) respectively and MGAM was recognized by anti-MGAM antibodies (77/127/207). IP, immunoprecipitation; IB, immunoblotting.