May 1, 1976

Studies on peroxisomes. VI. Relationship between the peroxisomal core and urate oxidase

Journal of Biochemistry
H HayashiS Niinobe


The peroxisomal core from the liver of rats was purified 450-fold as a marker of urate oxidase [EC] activity. This preparation has a high specific activity of urate oxidase but not of other peroxisomal enzymes: D-amino acid oxidase [EC], L-alpha-hydroxy acid oxidase [EC], or catalase [EC]. No activity of marker enzymes for other subcellular particles; cytochrome c oxidase [EC1.9.3.1] (mitochondria), acid phosphatase [EC] (lysosomes), or glucose-6-phosphatase [EC] (microsomes), was detected in this preparation. The core obtained showed a single protein band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and the position of the band was found to correspond to a molecular weight 35,000. When the peroxisomal core was subjected to treatment at various pH's with 0.1 M carbonate buffer, urate oxidase was almost completely solubulized at pH 11.0, although approximately 35% of the core protein still remained in the pellet After solubilization of the core at pH 11.0, the specific activity of urate oxidase in the supernatant increased about 1.6 times; the density of the insoluble protein remaining in the pellet was identical with the that of the original core on sucrose den...Continue Reading

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Mentioned in this Paper

Biological Markers
(S)-2-Hydroxy-acid oxidase
Centrifugation, Density Gradient
Acid Phosphatase
Cytochrome C Oxidase
Positioning Attribute
D-Amino Acid Dehydrogenase

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