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

研究成果: 雜誌貢獻文章同行評審

27 引文 斯高帕斯(Scopus)

摘要

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.

原文英語
頁(從 - 到)4762-4764
頁數3
期刊Journal of Biological Chemistry
258
發行號8
出版狀態已發佈 - 1983
對外發佈Yes

ASJC Scopus subject areas

  • Biochemistry

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