Biochemical Medicine and Metabolic Biology
Volume 50, Issue 1, August 1993, Pages 103-110
Regular ArticleQuantification of the Content of Fluorescent Flavoproteins in Mitochondria from Liver, Kidney Cortex, Skeletal Muscle, and Brain
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Cited by (69)
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2018, Neurochemistry InternationalCitation 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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