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. 2014 Oct 15;2(10):e12154. doi: 10.14814/phy2.12154

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© 2014 The Authors. Physiological Reports published by Wiley Periodicals, Inc. on behalf of the American Physiological Society and The Physiological Society.

This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

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Figure 2. — Representative western blot of rested and contracted mitochondria samples probing for proteins from different intracellular organelles as follows (n = 15); loading 15 μg of mitochondrial protein for PLIN2 (lipid droplets), 20 μg of mitochondrial protein for SERCA 1 and 10 μg of mitochondrial protein for SERCA 2 (endo(sarco)plasmic reticulum) and 10 μg of mitochondrial protein for beta‐dystroglycan (sarcolemma) and whole homogenate (WH) with COX IV from corresponding membranes. PLIN2, SERCA1 and SERCA 2 are undetectable in mitochondria samples loaded. Beta‐dystroglycan was detected in purified mitochondria samples with no significant differences between rest and contraction (P = 0.62).