Zebrafish 10-formyltetrahydrofolate dehydrogenase is similar to its mammalian isozymes for its structural and catalytic properties

Wen Ni Chang, Hung Chang Lin, Tzu Fun Fu

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

10-Formyltetrahydrofolate dehydrogenase from zebrafish has been cloned and expressed in both Escherichia coli and yeast. In addition, the N-terminal and C-terminal domains have also been cloned and expressed. Each expressed protein was purified to homogeneity and structural and kinetic properties determined. These studies show that the zebrafish enzyme is structurally and catalytically very similar to the enzymes from mammalian sources, suggesting that zebrafish can be used to study the in vivo function of 10-formyltetrahydrofolate dehydrogenase.

Original languageEnglish
Pages (from-to)217-222
Number of pages6
JournalProtein Expression and Purification
Volume72
Issue number2
DOIs
Publication statusPublished - 2010 Aug 1

All Science Journal Classification (ASJC) codes

  • Biotechnology

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