Abstract
Peroxisomes and mitochondria were purified from rat liver by differential and equilibrium density centrifugation. Enoyl-CoA hydratase activity was assayed with two substrates: crotonyl-CoA (C4) and dodecenoyl-CoA (C12). The chain length specificity of the hydratase(s) in the two organelles differed strikingly: the ratio of activity on the C4 substrate/C12 substrate was 8–10 for the peak mitochondrial fraction and about 2 for the peak peroxisomal fraction. The subcellular distribution of the hydratase activity also depended on chain length. Peroxisomes contain 30–50% of the dodecenoyl-CoA hydratase activity but only 9–15% of the crotonase activity of rat liver.
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