Preliminary study on the monitoring of glutathione S-tranferase activity toward styrene oxide by electromigration methods

. 2005 Aug ; 28 (12) : 1357-62.

Jazyk angličtina Země Německo Médium print

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/pmid16138687

A new method has been developed for the monitoring of glutathione S-tranferase (GST) detoxification activity toward styrene oxide (SO). The enzymatic reaction was carried out directly in a thermostatted autosampler vial and the formation of conjugates between glutathione (GSH) and SO was monitored by sequential MEKC runs. The determinations were performed in a 50-microm fused silica capillary using 50 mM SDS in 20 mM phosphate 20 mM tetraborate buffer (pH 8.3) as a background electrolyte; separation voltage 28 kV (positive polarity), temperature of capillary 25 degrees C, and detection at 200 nm. The method is rapid, amenable to automation, and requires only small amounts of samples, which is especially important in the case of GST isoenzyme analyses.

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Recent developments in CE and CEC of peptides

. 2008 Jan ; 29 (1) : 179-206.

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