| Literature DB >> 20381623 |
Wen-Ni Chang1, Hung-Chang Lin, Tzu-Fun Fu.
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. Copyright 2010 Elsevier Inc. All rights reserved.Entities:
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Year: 2010 PMID： 20381623 DOI： 10.1016/j.pep.2010.04.003
Source DB: PubMed Journal: Protein Expr Purif ISSN： 1046-5928 Impact factor: 1.650