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Intraparticulate localization of peroxisomal carnitine acyltransferases in chick embryo liver.

Hepatic peroxisomes from 20-d-old chick embryo were purified by sucrose density gradient centrifugation. The specific activities of catalase and D-amino acid oxidase (DAAO) in the peroxisomal fraction were 24- and 32-fold, respectively, higher than those in the homogenate. The isolated peroxisomes included activities of 85.5 and 416 nmol/min/mg protein of carnitine palmitoyltransferase (CPT) and carnitine acetyltransferase (CAT), respectively. CPT was easily solubilized by treatment with Tween 20 or sonication from the peroxisomes, being similar in this respect to catalase. On the other hand, CAT was more resistant to solubilization, behaving similarly to DAAO. These results indicate that CPT as well as catalase is located in the peroxisomal matrix in a soluble form, and that CAT as well as DAAO is weakly associated with some insoluble components.