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. 2017 Nov 16;11:48–58. doi: 10.2174/1874205X01711010048

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© 2017 Henderson et al.

This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: https://creativecommons.org/licenses/by/4.0/legalcode. This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Fig. (3) — An increase in mitochondrial Bax and phosphorylated Bax. (A) Equal amounts of proteins (100 μg/well) from the crude mitochondrial fractions from AD and control individuals were separated on 15% SDS-PAGE, transferred to PVDF-Immobilon, and subjected to immunoblot analyses for Bax (top panel) or ATP synthase-β subunit (middle) and Coomassie blue stained (bottom). (B) Densitometric quantitation of mitochondrial Bax in AD patients relative to control subjects is presented. P<0.05. (C) Equal amounts of mitochondrial proteins from the two randomly-chosen specimens per group (400 μg protein/analysis) were incubated with 2 ug of anti-Bax antibody (2D2 or 6A7) to immunoprecipitate the mitochondrial Bax protein. Immunoprecipitated Bax proteins were then subjected to IB analysis using a specific antibody against phospho-Thr-Pro (top panel) or Bax (middle). The remaining gel was stained with Coomassie blue (bottom panel) to demonstrate equal protein loading. (D) Densitometric quantitation of p-Thr-Pro-Bax in AD patients compared to control subjects is shown. P<0.01.