The availability of carnitine acetyltransferase in mitochondria from guinea-pig liver and other tissues.
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.
D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D002331:Carnitine / Q000378:metabolism; D003065:Coenzyme A / Q000378:metabolism; D003593:Cytoplasm; D005612:Freeze Drying; D005969:Glutamate Dehydrogenase / Q000378:metabolism*; D006041:Goats; D006168:Guinea Pigs; D066298:In Vitro Techniques; D008321:Mammary Glands, Animal / Q000201:enzymology; D008928:Mitochondria / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology*; D051381:Rats; D012756:Sheep; D013395:Sucrose; D013501:Surface-Active Agents
D013501:Surface-Active Agents; D013395:Sucrose; D005969:Glutamate Dehydrogenase; D000217:Acyltransferases; D002331:Carnitine; D003065:Coenzyme A