Peroxisomal localization of acyl-coenzyme A reductase (long chain alcohol forming) in guinea pig intestine mucosal cells.
Upon differential centrifugation of guinea pig intestine mucosal cells homogenate, fatty acyl-CoA:NADPH oxidoreductase (long chain alcohol forming) was found to be enriched in the light mitochondrial (L) fraction (sedimenting between 66,000 x g min and 500,000 x g min) which contained mainly mitochondria, lysosomes, and peroxisomes. Peroxisomes (marker enzymes: catalase and dihydroxyacetone phosphate acyltransferase) present in the L fraction were separated from other organelles in a Nycodenz density gradient centrifugation employing a vertical rotor. By comparing the distribution of acyl-CoA reductase with different marker enzymes in the gradient, it was concluded that this reductase is primarily localized in the microperoxisomes (microbodies). The topography of the membrane-bound enzyme in the isolated organelles was studied by checking its lability toward trypsin in the absence and presence of the detergent Triton X-100. The results suggested that acyl-CoA reductase is localized on the outer surface (cytosolic side) of microperoxisomal membrane.
Burdett
K
K
Neuroscience Laboratory, University of Michigan, Ann Arbor 48104-1687.
Larkins
L K
LK
Das
A K
AK
Hajra
A K
AK
D044942:Acyl-CoA Dehydrogenase, Long-Chain / Q000378:metabolism*; D000818:Animals; D002458:Cell Fractionation; D006168:Guinea Pigs; D007413:Intestinal Mucosa / Q000166:cytology / Q000201:enzymology*; D008055:Lipids / Q000096:biosynthesis; D008247:Lysosomes / Q000201:enzymology; D008830:Microbodies / Q000201:enzymology*; D008928:Mitochondria / Q000201:enzymology; D014357:Trypsin / Q000737:chemistry
D008055:Lipids; D044942:Acyl-CoA Dehydrogenase, Long-Chain; D014357:Trypsin