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. 1971 Feb;47(2):246–251. doi: 10.1104/pp.47.2.246

Uricase and Allantoinase in Glyoxysomes 1

R R Theimer a, Harry Beevers a
PMCID: PMC365850  PMID: 16657604

Abstract

In fat-degrading tissues of seedlings of seven different plant species examined, uricase activity (urate:O2 oxidoreductase, EC 1.7.33) was associated with particulate fractions. After equilibrium density centrifugation on sucrose density gradients the enzyme activity was recovered in the glyoxysomal band (density: 1.25 grams per cubic centimeter). Allantoinase is also present in glyoxysomes but, equally, in the proplastid region (density: 1.22 grams per cubic centimeter). Xanthine oxidase, xanthine dehydrogenase, allantoicase, and urease were not detected in glyoxysomes from castor bean endosperm. Uricase in these particles shows its maximal activity at pH 8.9. The apparent Km is 7.4 μm. Urate concentrations greater than 120 μm as well as certain other purine compounds inhibit the enzyme. Cyanide at a concentration of 10 μm is a potent inhibitor. 2,6-Dichlorophenolindophenol did not substitute for oxygen as electron acceptor.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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