PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “URATE OXIDASE”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 667 records · Page 37Linked to original sources
PubMed1979

Mechanism of uricase action.

Uricase (urate:oxygen oxidoreductase, EC 1.7.3.3) exposes a positional and steric specificity in the enzymic conversion of urate to allantoin. C-2 of urate was recovered as C-2 of allantoin. By the consecutive oxidation and hydrolysis reactions a levorotatory intermediate was formed, presumably (-)-2-oxo-4-hydroxy-4-carbohydroxy-5-ureido-imidazoline. The absorption and optical rotation dispersion spectra of the intermediate were established. In the presence of borate buffer, the intermediate was transformed to (+)-alloxanate. The decay of the former compound depends on general base and acid catalysis. RS-(+/-)-allantoin was formed by chemical decarboxylation and S-(+)-allantoin by enzymic decarboxylation.

Allantoin↗
PubMed1980

Fibrin membrane endowed with biological function. V. Multienzyme complex of uricase, catalase, allantoinase and allantoicase.

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. All of these enzymes together with catalase were also embedded in a single fibrin membrane to make an immobilized multienzyme complex. The multienzyme complex in fibrin membrane thus prepared had an ability of degradation of uric acid to urea and glyoxylic acid via allantoin and allantoic acid. The stability of immobilized uricase or catalase embedded in fibrin membrane upon lyophilization was also tested in a comparison with nonimmobilized enzymes.

Acetates↗
PubMed1985

Induction of fatty acid beta-oxidation and peroxisome proliferation in the liver of rhesus monkeys by DL-040, a new hypolipidemic agent.

Many structurally unrelated hypolipidemic agents and certain phthalate-ester plasticizers induce hepatomegaly and proliferation of peroxisomes in liver parenchymal cells of rodents, but there is relatively limited evidence regarding the ability of such compounds to induce peroxisome proliferation in the livers of nonrodent species including man. The present study was designed to determine if DL-040 (4-(((1,3-benzodioxol)-5-yl)methyl)amino-benzoic acid), a newly developed hypolipidemic agent, induces peroxisome proliferation in the liver of adult rhesus monkeys. Feeding of DL-040 (300 mg/kg body wt for 1 week; and 400 mg/kg body wt for 10 weeks) caused a significant increase in peroxisome population as determined by ultrastructural and morphometric analyses. The DL-040-induced peroxisome proliferation was accompanied by increases in the levels of catalase, carnitine acetyltransferase and the peroxisomal fatty acid beta-oxidation system. As expected, DL-040 caused a significant reduction of serum cholesterol and low density lipoprotein content. These data suggest that hepatic peroxisome proliferation is inducible in nonhuman primates at dose levels that exceed therapeutic levels.

Aminobenzoates↗