Publication | Open Access
Subcellular localization of acyl coenzyme A: dihydroxyacetone phosphate acyltransferase in rat liver peroxisomes (microbodies).
194
Citations
34
References
1979
Year
Lipid PeroxidationSubcellular LocalizationMolecular BiologyRedox BiologyOxidative StressBiosynthesisRat Liver HomogenateAldehyde DehydrogenaseBiochemistryLiver PhysiologyLight MitochondrialMetabolomicsCellular EnzymologyNatural SciencesCellular BiochemistryMetabolismMedicineAcyl CoenzymeRat Liver PeroxisomesCarbonyl Metabolism
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.
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