[Enzymologic study of the structural organization of the matrix or rat liver peroxisomes].
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.
D000594:Amino Acid Oxidoreductases / Q000378:metabolism; D000818:Animals; D002374:Catalase / Q000378:metabolism; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007521:Isocitrate Dehydrogenase / Q000378:metabolism; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D008099:Liver / Q000648:ultrastructure*; D008297:Male; D008830:Microbodies / Q000201:enzymology* / Q000648:ultrastructure; D009251:NADPH-Ferrihemoprotein Reductase / Q000378:metabolism; D009940:Organoids / Q000201:enzymology*; D009994:Osmolar Concentration; D010088:Oxidoreductases / Q000378:metabolism; D051381:Rats; D014503:Urate Oxidase / Q000378:metabolism
D010088:Oxidoreductases; D005993:Glycerolphosphate Dehydrogenase; D007770:L-Lactate Dehydrogenase; D007521:Isocitrate Dehydrogenase; D002374:Catalase; D000594:Amino Acid Oxidoreductases; D009251:NADPH-Ferrihemoprotein Reductase; D014503:Urate Oxidase
Enzimologicheskoe issledovanie strukturnoĭ organizatsii matriksa peroksisom pecheni krys.