D-aspartate oxidase in rat, bovine and sheep kidney cortex is localized in peroxisomes

D-Aspartate oxidase (EC 1.4.3.1) was assayed in subcellular fractions and in highly purified peroxisomes from rat, bovine and sheep kidney cortex as well as from rat liver. During all steps of subcellular-fractionation procedures, D-aspartate oxidase co-fractionated with peroxisomal marker enzymes....

Full description

Saved in:
Bibliographic Details
Published inBiochemical journal Vol. 261; no. 1; pp. 233 - 238
Main Authors Zaar, K, Völkl, A, Fahimi, H D
Format Journal Article
LanguageEnglish
Published England 01.07.1989
Subjects
Amino Acid Oxidoreductases - metabolism
Animals
Cattle
D-Aspartate Oxidase
Female
kidney
Kidney Cortex - enzymology
Kidney Cortex - ultrastructure
Microbodies - enzymology
peroxisomes
Rats
Rats, Inbred Strains
Sheep
Online AccessGet full text

Cover

More Information
Summary:D-Aspartate oxidase (EC 1.4.3.1) was assayed in subcellular fractions and in highly purified peroxisomes from rat, bovine and sheep kidney cortex as well as from rat liver. During all steps of subcellular-fractionation procedures, D-aspartate oxidase co-fractionated with peroxisomal marker enzymes. In highly purified preparations of peroxisomes, the enrichment of D-aspartate oxidase activity over the homogenate is about 32-fold, being comparable with that of the peroxisomal marker enzymes catalase and D-amino acid oxidase. Disruption of the peroxisomes by freezing and thawing released more than 90% of the enzyme activity, which is typical for soluble peroxisomal-matrix proteins. Our findings provide strong evidence that in these tissues D-aspartate oxidase is a peroxisomal-matrix protein and should be added as an additional flavoprotein oxidase to the known set of peroxisomal oxidases.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2610233