The instability of OXPHOS complexes. (A) The steady-state levels of five OXPHOS complexes by Blue-Native gel electrophoresis. Fifteen micrograms of mitochondrial proteins from mutant and WT zebrafish were electrophoresed through a Blue-Native gel, electroblotted and hybridized with antibodies for Ndufs1, Uqcrc2, Cox5a, Atp5c (subunits of complex I, III, IV and V, respectively) as well as Sdha (subunit of complex II) as a loading control. (B) Quantification of levels of complexes I, III, IV and V in mutant and WT zebrafish. (C) The activities of OXPHOS complexes were investigated by enzymatic assays on complexes I, II, III, IV and V in mitochondria isolated from mutant and WT zebrafish. The calculations were based on three independent determinations. Graph details and symbols are explained in the legend to Figure 2.
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