Biochemical Journal · 1968 · 31 citations · 24 references
Life SciencesBiochemistryCell BiologyEnzymologyMetabolismMitochondrial BiologyEnergy MetabolismMitochondrial BiochemistryMitochondrial BioenergeticsMitochondrial FunctionMitochondrial MetabolismMitochondrial PhysiologyGlutamate DehydrogenaseMitochondrial Enzymology
The carnitine acetyltransferase and glutamate dehydrogenase activities of guinea-pig liver and other tissues were estimated. Both enzymes are wholly mitochondrial, and can only be fully observed after disruption of the mitochondrion. Triton X-100 (0.1%) or freeze-drying revealed more activity than other methods tried. In mitochondria prepared and suspended in 0.25m-sucrose and in cell cytoplasm only small fractions of the total enzymic activity could be observed in guinea-pig liver: on average 7.5% of carnitine acetyltransferase and 5.5% of glutamate dehydrogenase. It is concluded that, in liver or mammary gland of goat, guinea pig or rat, little or no carnitine acetyltransferase is available in vivo to acetyl-CoA outside the mitochondrion.
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Regulation of Metabolic Processes in Mitochondria
Food and Cosmetics Toxicology · 1967 · 1.2K citations
Life Sciences, Biochemistry, Biology +12
Carnitine and derivatives in rat tissues
David Pearson, Philip K. Tubbs · Biochemical Journal · 1967 · 287 citations · Full text
THE ACETATE ACTIVATING ENZYME SYSTEM OF HEART MUSCLE
Helmut Beinert, D.E. Green, Priscilla Hele et al. · Journal of Biological Chemistry · 1953 · 229 citations · Full text