期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 133, 期 41, 页码 16495-16502出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja205392z
关键词
-
资金
- Ministerio de Ciencia e Innovacion [CTQ2008-04444/BQA]
- Government of the Basque Country
- Etortek grant
- European Union [PITN-GA-2008-215536]
Two recombinant fucosyltransferases were employed as synthetic tools in the chemoenzymatic synthesis of core fucosylated N-glycan structures. Enzyme substrates were rapidly identified by incubating a microarray of synthetic N-glycans with the transferases and detecting the presence of core fucose with four lectins and one antibody. Selected substrates were then enzymatically fucosylated in solution on a preparative scale and characterized by NMR and MS. With this approach the chemoenzymatic synthesis of a series of alpha 1,3-, alpha 1,6-, and difucosylated structures was accomplished in very short time and with high yields, which otherwise would have required extensive additional synthetic effort and a complete redesign of existing synthetic routes. In addition, valuable information was gathered regarding the specificities of the lectins employed in this study.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据