The degradation of urate in liver peroxisomes: Association of allantoinase with allantoicase in amphibian liver but not in fish and invertebrate liver

Y. Takada, T. Noguchi

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)

Abstract

Allantoinase and allantoicase were co-purified from frog (Rana catesbeiana) liver. The ratio of the two enzyme activities remained constant during purification and was unchanged by a variety of treatments of the purified enzyme. These results suggest that allantoinase and allantoicase are located in the same protein. It was found that the two hepatic enzyme activities are also associated with the same protein in other frogs (Xenopus laevis and Rana nigromacultata), tadpoles (R. catesbeiana), and newts (Triturus pyrrhogaster). In contrast, allantoinase and allantoicase were found to be different proteins in marine fish and invertebrate liver.

Original languageEnglish
Pages (from-to)4762-4764
Number of pages3
JournalJournal of Biological Chemistry
Volume258
Issue number8
Publication statusPublished - 1983
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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