[Urate oxidase from pig liver: biochemical and immunological properties].
A highly purified uratoxidase was isolated from the pig liver. The sedimentation coefficient of the enzyme was 6.96 S and the molecular weight was 122,000 +/- 4,000. The enzyme was a tetramer consisting of subunits with a molecular weight of 31,600 +/- 2,500. Uratoxidase showed high substrate specificity with 0.05 M borate buffer, pH 8.5. During competitive inhibition 8-azaxanthine (Ki = 3.1 X 10(-7) M) produced the strongest inhibitory effect as compared with other purine compounds. N-chloromercuric benzoate and ascorbic acid also inhibited strongly uratoxidase activity. EDTA-Na2, methyl ester of n-oxybenzoic acid, phenyl methyl sulphonyl fluoride and cystein did not influence the enzyme activity.
D000818:Animals; D001205:Ascorbic Acid / Q000494:pharmacology; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002729:Chloromercuribenzoates / Q000494:pharmacology; D008099:Liver / Q000201:enzymology*; D046911:Macromolecular Substances; D008970:Molecular Weight; D013379:Substrate Specificity; D013552:Swine; D014461:Ultracentrifugation; D014503:Urate Oxidase / Q000037:antagonists & inhibitors / Q000276:immunology*; D014970:Xanthines / Q000494:pharmacology
D002729:Chloromercuribenzoates; D046911:Macromolecular Substances; D014970:Xanthines; C018221:8-azaxanthine; D014503:Urate Oxidase; D001205:Ascorbic Acid
Uratoksidaza iz pecheni svin'i: nekotorye biokhimicheskie i immynologicheskie svoĭstva fermenta.