Some properties of carnitine acetyltransferase activity in extracts of various animal tissues and in intact mitochondria have been studied. Enzyme activity was found as soluble and membrane‐associated forms which were separated by isoelectric focusing, ion‐exchange chromatography and centrifugation. It was shown that the two forms of enzyme are freely interconvertible and have similar kinetic properties. Intact mitochondria oxidize acetyl‐CoA (+ carnitine) very much more slowly than acetylcarnitine. The results suggest the existence of only a single type of carnitine acetyltransferase.
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Edwards et al. (1974) studied this question.
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