期刊
BIOCONJUGATE CHEMISTRY
卷 25, 期 11, 页码 1911-1915出版社
AMER CHEMICAL SOC
DOI: 10.1021/bc500347b
关键词
-
类别
资金
- 973 Program [2013CB910700]
- National Foundation of Natural Science [81373270]
- Shenzhen Science and Technology Innovation Commission [KQTD201103, JC201005270281A, ZDSYZ20130331145112855]
- Guangdong Natural Science Foundation [S2012010008741]
- Peking University
The immobilization of functional proteins onto solid supports using affinity tags is an attractive approach in recent development of protein microarray technologies. Among the commonly used fusion protein tags, glutathione S-transferase (GST) proteins have been indispensable tools for protein protein interaction studies and have extensive applications in recombinant protein purification and reversible protein immobilization. Here, by utilizing pyrimidine-based small-molecule probes with a sulfonyl fluoride reactive group, we report a novel and general approach for site-selective immobilization of Schistosoma japonicum GST (sjGST) fusion proteins through irreversible and specific covalent modification of the tyrosine-111 residue of the sjGST tag. As demonstrated by sjGST-tagged eGFP and sjGST-tagged kinase activity assays, this immobilization approach offers the advantages of high immobilization efficiency and excellent retention of protein structure and activity.
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