Abstract
A fluorogenic derivatization method was developed to distinguish the protein N-terminal acetylation status. The unacetylated protein selectively reacted with 4-chloro-7-nitrobenzofurazan (NBD-Cl) at neutral pH to provide high fluorescence. In contrast, the protein with N-terminal acetylation was essentially nonfluorescent under the same conditions despite the presence of many internal lysine residues. Fluorescence of the NBD-labeled protein was very stable, and only micromolar concentrations of proteins were required for reliable detection. This method also provides a general and practical way to quantify proteins when their N-terminal amino group is available.
Original language | English |
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Pages (from-to) | 13-15 |
Number of pages | 3 |
Journal | Analytical Biochemistry |
Volume | 428 |
Issue number | 1 |
DOIs | |
State | Published - 1 Sep 2012 |
Keywords
- Fluorescent labeling
- NBD-Cl
- Protein N-terminal acetylation
- Thymosin
- Z-domain