Cytochrome c oxidase activity in T/t 6 (balanced lethal) mutant mice

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Abstract
R-1 (1450g) and R-2 (25,000g) liver fractions from T/t 6 and B6CBAF1 hybrid mice were analyzed for their protein content, mitochondria concentrations, and activities of three respiratory-chain enzymes of the mitochondrial inner membrane: cytochrome c oxidase (ferrocytochrome c: oxygen oxidoreductase, E.C. 1.9.3.1), α-glycerophosphate dehydrogenase [l-glycerol-3-phosphate: (acceptor) oxidoreductase, E.C. 1.1.99.5], and succinate-cytochrome c reductase. Only cytochrome c oxidase activity, calculated as units per 1010 mitochondria, was significantly lower in both R-1 and R-2 fractions of T/t 6 mice. Cytochrome c oxidase activity varied greatly among T/t 6 mice, as did their liver mitochondria concentrations and body weights. Cytochrome c oxidase activity in the R-1 fraction of T/t 6 mice, calculated as units per 1010 mitochondria per gram of body weight, averaged about 40% lower than in B6CBAF1 mice. α-Glycerophosphate dehydrogenase activity was often elevated in T/t 6 mice, particularly in the R-2 fraction. The T/t locus, a complex genetic locus on chromosome 17, may contain genes important to the function and biogenesis of mitochondria.