Localization of xanthine oxidase in crystalline cores of peroxisomes. A cytochemical and biochemical study.
The ultrastructural cytochemical localization of xanthine oxidase activity in rat liver was investigated by the cerium technique. The reaction product was found in the cytoplasm of endothelial cells in liver sinusoids and, in addition, in crystalline cores of peroxisomes of liver parenchymal cells. Xanthine oxidase was also present in peroxisomal cores of beef liver and kidney, but not in rat kidney peroxisomes, which lack crystalline cores. The localization in peroxisomal cores of rat liver was confirmed also biochemically using highly purified peroxisomal fractions and subfractions containing exclusively the crystalline cores. Moreover, high levels of molybdenum were found in isolated peroxisomal cores by atomic absorption spectroscopy, thus corroborating the association of the molybdenum-containing enzyme with the cores. Since urate oxidase is also present within the same compartment of peroxisomes, it is possible that the crystalline cores harbor a complex of several enzymes involved in the purine metabolism.
Department of Anatomy, University of Heidelberg, Federal Republic of Germany.
S
S
Angermüller
G
G
Bruder
A
A
Völkl
H
H
Wesch
H D
HD
Fahimi
D000818:Animals; D006651:Histocytochemistry; D007668:Kidney / Q000201:enzymology / Q000648:ultrastructure; D008099:Liver / Q000201:enzymology / Q000648:ultrastructure; D008297:Male; D008830:Microbodies / Q000201:enzymology*; D008982:Molybdenum / Q000032:analysis; D051381:Rats; D011919:Rats, Inbred Strains; D014969:Xanthine Oxidase / Q000032:analysis*
D008982:Molybdenum; D014969:Xanthine Oxidase