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PMID: 500614 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

The Journal of biological chemistry ·Vol. 254 ·No. 21 ·1979-11-10 ·Pages 10896-900

Hajra AK, Burke CL, Jones CL

Abstract

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.

MeSH Terms
Acyltransferases/analysis Animals Cell Fractionation Centrifugation, Density Gradient Dihydroxyacetone Phosphate Female Liver/enzymology Lysosomes/enzymology Microbodies/enzymology Organoids/enzymology Rats Subcellular Fractions/enzymology
Chemicals
Dihydroxyacetone Phosphate Acyltransferases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hajra A K
Burke C L
Jones C L
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1979-11-10
Pages
10896-900
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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