Site-specific protein labelling and immobilization mediated by microbial transglutaminase
| Autor: | Samuel K. Oteng-Pabi, Christophe Pardin, Maria Stoica, Jeffrey W. Keillor |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Specific protein
Azides Glutamine Streptomycetaceae Peptide Catalysis Substrate Specificity Labelling Materials Chemistry chemistry.chemical_classification Transglutaminases Cycloaddition Reaction Propylamines Metals and Alloys Proteins General Chemistry Enzymes Immobilized In vitro Cycloaddition Surfaces Coatings and Films Electronic Optical and Magnetic Materials Fluorescent labelling chemistry Biochemistry Pargyline Alkynes Ceramics and Composites Substrate specificity Oligopeptides Microbial transglutaminase Copper |
| Zdroj: | Chemical communications (Cambridge, England). 50(50) |
| ISSN: | 1364-548X |
| Popis: | Microbial transglutaminase (mTG) shows broad substrate specificity that is amenable to in vitro bio-conjugation applications. Herein, test proteins were genetically fused with peptide tags, followed by mTG-mediated propargylation of their reactive Gln residues. The propargylated proteins were subjected to copper-assisted azide-alkyne cycloaddition to demonstrate either fluorescent labelling or immobilization. |
| Databáze: | OpenAIRE |
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