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斑马鱼10-甲酰四氢叶酸脱氢酶在结构和催化特性上与其哺乳动物同工酶相似。

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

作者信息

Chang Wen-Ni, Lin Hung-Chang, Fu Tzu-Fun

机构信息

Institute of Basic Medical Science, College of Medicine, National Cheng Kung University, Tainan, Taiwan.

出版信息

Protein Expr Purif. 2010 Aug;72(2):217-22. doi: 10.1016/j.pep.2010.04.003. Epub 2010 Apr 8.

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.

摘要

斑马鱼的10-甲酰四氢叶酸脱氢酶已被克隆,并在大肠杆菌和酵母中表达。此外,该酶的N端和C端结构域也已被克隆和表达。每种表达的蛋白质都被纯化至同质,并测定了其结构和动力学性质。这些研究表明,斑马鱼的这种酶在结构和催化方面与哺乳动物来源的酶非常相似,这表明斑马鱼可用于研究10-甲酰四氢叶酸脱氢酶的体内功能。

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