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Quantification of the Content of Fluorescent Flavoproteins in Mitochondria from Liver, Kidney Cortex, Skeletal Muscle, and Brain

https://doi.org/10.1006/bmmb.1993.1051Get rights and content

Abstract

The flavoprotein fluorescence emission spectra of mitochondria from rat liver, rat kidney cortex, rat skeletal muscle, and rat brain were compared using free FAD as a standard. On the basis of distinct spectral characteristics and reduction pattern it was possible to differentiate between fluorescence caused by α-lipoamide dehydrogenase and electron-transfer flavoprotein. The amount of these flavoproteins in the different mitochondria was quantified and compared with the maximal rates of respiration with the substrates glutamate plus malate and octanoylcarnitine plus malate. It was observed that there is a good correlation between the fractional content of electron-transfer flavoprotein (with respect to α-lipoamide dehydrogenase) and the fractional β-oxidation capacity (with respect to the glutamate plus malate oxidation rate). This method is applicable for the detection of defects of α-lipoamide dehydrogenase and electron-transfer flavoprotein in mitochondrial myopathies.

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    Citation Excerpt :

    These data show that an altered FAD content would not be the underlying mechanism of ROS generation by the pathogenic mutants of hE3 (Ambrus et al., 2011). The E3 component also exists as a free enzyme in vivo (Ambrus et al., 2009c; Constantinescu et al., 1995; Jiang et al., 2016; Reed and Hackert, 1990; Reed and Oliver, 1968; Yan et al., 2013), and it is the most abundant flavoprotein in muscle and brain mitochondria (Kunz and Gellerich, 1993). It is to note that E3 binds ∼30 times weaker to the KGDHc than to the PDHc (Erfle and Sauer, 1969; Poulsen and Wedding, 1970; Reed and Oliver, 1968) and interaction with the KGDHc may be further weakened in acidosis (Ambrus et al., 2009c).

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