Journal
BIOCONJUGATE CHEMISTRY
Volume 25, Issue 11, Pages 1911-1915Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bc500347b
Keywords
-
Categories
Funding
- 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
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available