| Autor: |
Apfel, Christian M., Evers, Stefan, Hubschwerlen, Christian, Pirson, Wolfgang, Page, Malcolm G. P., Keck, Wolfgang |
| Zdroj: |
Antimicrobial Agents and Chemotherapy; April 2001, Vol. 45 Issue: 4 p1053-1057, 5p |
| Abstrakt: |
ABSTRACTAn assay was developed to determine the activity of peptide deformylase (PDF) inhibitors under conditions as close as possible to the physiological situation. The assay principle is the detection of N-terminal [35S]methionine labeling of a protein that contains no internal methionine. If PDF is active, the deformylation of the methionine renders the peptide a substrate for methionine aminopeptidase, resulting in the removal of the N-terminal methionine label. In the presence of a PDF inhibitor, the deformylation is blocked so that the N-formylated peptide is not processed and the label is detected. Using this assay, it is possible to determine the PDF activity under near-physiological conditions in a cell-free transcription-translation system as well as in intact bacterial cells. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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