High impact information on UOX

• The most common inclusions are membrane associated plate-like "marginal plates" of hitherto unknown nature in renal peroxisomes and central polytubular "cores" composed of urate oxidase in hepatic peroxisomes [1].
• In the case of xanthine oxidase acting upon xanthine and hypoxanthine as substrates, carbonate radical anion production was also evidenced by the oxidation of 5,5-dimethyl-1-pyrroline-N-oxide and of dihydrorhodamine 123 in the presence of uricase [2].
• PXP-18 also protected urate oxidase, another peroxisomal enzyme, from inactivation at 66 degrees C for 15 min and facilitated the renaturation of ACO denatured by 2 M urea [3].
• The electrode used Aspergillus flavus uricase (EC.1.7.3.3) cross-linked to bovine serum albumin by means of glutaraldehyde, sandwiched between a dimethyldichlorosilane-treated microporous polycarbonate membrane and an inner cellulosic H2O2-selective membrane [4].
• Purine nucleoside phosphorylase, xanthine oxidase, and urate oxidase were immobilized on controlled-pore glass beads [5].

Biological context of UOX

• The activation energy requirement for uric acid hydrolysis by uricase and inactivation of enzyme were 11.6 and 14.5 kJ/M respectively [6].
• Comparative immunology of mammalian uricase using anti-hog liver uricase [7].

Anatomical context of UOX

• Peroxisomes in bovine kidney cortical epithelium possessed crystalloid cores or nucleoids, which were found to be the exclusive sites of urate oxidase localization [8].
• We show here that protein antigens (bovine serum albumin, hog liver uricase, and yeast hexokinase), coupled to autologous red blood cells by way of a biotin-avidin-biotin bridge, elicit an immunological response in mice similar to or higher than that obtained by the use of Freund's adjuvant [9].
• The enzymes (uricase (EC 1.7.3.3), allantoinase (EC 3.5.3.4), and allantoicase (EC 3.5.2.5) which participate in degradation of purine bases, were embedded separately in fibrin membranes formed by fibrinogen-fibrin conversion with thrombin [10].

Associations of UOX with chemical compounds

• Affinity chromatography of urate oxidase on 8-aminoxanthine-bound Sepharose [11].
• In the Belgian national external quality assessment scheme, we observed significantly lowered recoveries for urate in the group of Beckman Synchron users in comparison with the overall median values of the uricase/peroxidase colorimetric methods [12].
• The nature of the interference was studied by differential pulse voltammetry and responses to ascorbic acid oxidase and uricase [13].
• A purification procedure of uricase from ox kidneys has been worked out starting from a n-butanol extract [14].

Other interactions of UOX

• The stability of immobilized uricase or catalase embedded in fibrin membrane upon lyophilization was also tested in a comparison with nonimmobilized enzymes [10].

Analytical, diagnostic and therapeutic context of UOX

• We investigated the localization of urate oxidase, peroxisomal fatty acyl-CoA oxidase, and catalase in bovine kidney by immunoblot analysis and protein A-gold immunocytochemistry, using the respective polyclonal monospecific antibodies raised against the enzymes purified from rat liver [8].
• 2. Results obtained by immunodiffusion suggest that hog uricase has four sites of partial antigens (a, b, c, d), while the enzyme of other mammals has only part of them, and a cladogram of these six mammals is presented showing development of partial antigens [7].
• 3. Results obtained by immunoelectrophoresis suggest that the protein structure of house musk shrew uricase is considerably different from the other five mammals tested [7].

References