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- W2468638892 abstract "The effect of ionic strength and pH on the release of some enzymes of the matrix of peroxisomes in rat's liver was studied. Catalase, L ALpha-hydroxy acid oxidase, isocitrate dehydrogenase, glycerophosphate dehydrogenase and lactate dehydrogenase were easily released from the particles during their lysis and treatment with 0.16 M KCl, whereas urate oxidase, NADH cytochrome c reductase and D-amino acid oxidase were not solubilized. After the solubilization of peroxisomal membrane by 0.2% Triton X-100, the remaining core contained about 50% amino acid oxidase activity, and had 1.28--1.30 g/cm3 density. These results suggest that D-amino acid oxidase associates with urate oxidase in the peroxisomal core." @default.
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- W2468638892 date "1978-06-01" @default.
- W2468638892 modified "2023-10-07" @default.
- W2468638892 title "Enzymologic study of the structural organization of the matrix or rat liver peroxisomes" @default.
- W2468638892 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29368" @default.
- W2468638892 hasPublicationYear "1978" @default.
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