PMID:16372277
| Citation |
Arnitz, R, Sarg, B, Ott, HW, Neher, A, Lindner, H and Nagl, M (2006) Protein sites of attack of N-chlorotaurine in Escherichia coli. Proteomics 6:865-9 |
|---|---|
| Abstract |
N-Chlorotaurine sodium (NCT) is a promising microbicidal agent for topical treatment of infections. Its targets of attack in Escherichia coli have been investigated by proteomics. Incubation in 1% NCT for 10 and 30 min revealed a change of the charge and a separation of numerous proteins into a series of spots with a different pI. Charge differences could be related to oxidation of cysteine residues to their corresponding sulfonic acids. Heat shock protein 60 appeared, while ribosome-releasing factor, d-ribose periplasmic binding protein, and malonyl-CoA transacylase spots decreased. These results indicate penetration of oxidation capacity into the bacteria and destruction of essential proteins by NCT. |
| Links |
PubMed Online version:10.1002/pmic.200500054 |
| Keywords |
Acyl-Carrier Protein S-Malonyltransferase/metabolism; Bacterial Proteins/drug effects; Chaperonin 60/metabolism; Cysteine/chemistry; Electrophoresis, Gel, Two-Dimensional; Enzyme Inhibitors/pharmacology; Escherichia coli/drug effects; Escherichia coli/metabolism; Oxidation-Reduction; Periplasmic Binding Proteins/metabolism; Protein-Serine-Threonine Kinases/antagonists & inhibitors; Proteomics; Ribosomal Proteins/metabolism; Spectrometry, Mass, Electrospray Ionization; Sulfonic Acids/metabolism; Taurine/analogs & derivatives; Taurine/pharmacology |
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