Comparison of intraperoxisomal localization form and properties of amphibian (Rana catesbeiana) uricase with those of other animal uricases.
Liver uricase of bull frog (Rana catesbeiana) was present as the soluble form in the peroxisomal matrix and consisted of four identical subunits with a molecular weight of 30,000. These properties were identical with those of fish liver uricase but differed from mammalian liver uricase. Purified uricase from the frog liver was insoluble in hypertonic, hypotonic and detergent solutions at pH 6-9. This insolubility was the same as mammalian liver uricase but differed from fish liver uricase; fish uricase was soluble in these solutions. The frog liver uricase did not cross-react immunologically with both uricases of fish and mammalian liver. An immunological cross-reactivity of liver uricase was observed among amphibia.
D000818:Animals; D005399:Fishes / Q000378:metabolism; D008099:Liver / Q000201:enzymology; D008322:Mammals / Q000378:metabolism; D008830:Microbodies / Q000201:enzymology*; D008970:Molecular Weight; D011892:Rana catesbeiana / Q000378:metabolism*; D013045:Species Specificity; D014503:Urate Oxidase / Q000302:isolation & purification / Q000378:metabolism*
D014503:Urate Oxidase