Subcellular localization of acyl coenzyme A: dihydroxyacetone phosphate acyltransferase in rat liver peroxisomes (microbodies)

• Published in: The Journal of biological chemistry Vol. 254; no. 21; pp. 10896 - 10900
• Main Authors: Hajra, A K, Burke, C L, Jones, C L
• Format: Journal Article
• Language: English
• Published: United States American Society for Biochemistry and Molecular Biology 10-11-1979
• Subjects: Acyltransferases - analysis; Animals; Cell Fractionation; Centrifugation, Density Gradient; Dihydroxyacetone Phosphate; Female; Liver - enzymology; Lysosomes - enzymology; Microbodies - enzymology; Organoids - enzymology; Rats; Subcellular Fractions - enzymology
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/s0021-9258(19)86607-3

Upon differential centrifugation of rat liver homogenate, the enzyme acyl-CoA:dihydroxyacetone-phosphate acyltransferase (EC
2.3.1.42) was found to be localized in the light mitochondrial (L) fraction which is enriched with lysosomes and peroxisomes.
Peroxisomes were separated from lysosomes in a density gradient centrifugation using rats which were injected with Triton
WR 1339. By comparing the enzyme distribution with the distribution of different marker enzymes, it was concluded that dihydroxyacetone
phosphate acyltransferase is primarily localized in rat liver peroxisomes (microbodies). Similarly, the enzyme acyl dihydroxyacetone-phosphate:NADPH
oxidoreductase (EC 1.1.1.101) was shown to be enriched in the peroxisomal fraction, although a portion of this reductase is
also present in the microsomal fraction.