Biochemistry of dystrophic muscle. Mitochondrial succinate-tetrazolium reductase and adenosine triphosphatase

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Abstract
The adenosine triphosphatase of mouse skeletal-muscle mitochondria was activated about equally by Mg2+, Co2+ and Mn + ions; Fe3+ and Ca2+ ions were less active. The enzyme was inhibited by adenosine di-phosphate, chlorpromazine, atabrine and, weakly, by Fions. Its activity was enhanced by 2,4-dinitrophenol, but never by more than about 50%. INT [2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride] was less efficient than oxygen as an acceptor of electrons from the succinate-dehydrogenase system of the mitochondria. Mitochondria from muscle of mice with hereditary muscular dystrophy had, on the average, a 15% higher adenosine triphosphatase activity than normal (compared on the basis of equal mitochondrial N). The succinate -INT-reductase activity was normal.