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- W1874430456 abstract "Glutathione S-transferases (GSTs) are an important enzyme family which play a critical role in detoxification system. In our study, GST was purified from muscle tissue of Chalcalburnus tarichii Pallas with 301.5-fold purification and 19.07% recovery by glutathione agarose affinity chromatography. The purity of enzyme was checked by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, showing a two band, because of having heterodimer structure. KM values were 1.59 and 0.53 mM for 1-chloro-2,4-dinitrobenzene (CDNB) and glutathione (GSH), respectively. Vmax values for CDNB and GSH were also determined as 5.58 and 1.88 EU/mL, respectively. In addition, inhibition effects of Ag(+), Cu(2+), Cd(2+), Fe(3+), Pb(2+), Cr(2+), Co(2+) and Zn(2+) metal ions were investigated on the enzyme activity and IC50, Ki values were calculated for these metal ions." @default.
- W1874430456 created "2016-06-24" @default.
- W1874430456 creator A5006229233 @default.
- W1874430456 creator A5018783172 @default.
- W1874430456 creator A5052632159 @default.
- W1874430456 date "2015-05-28" @default.
- W1874430456 modified "2023-10-14" @default.
- W1874430456 title "Purification of glutathione<i>S</i>-transferase from Van Lake fish (<i>Chalcalburnus tarichii</i>Pallas) muscle and investigation of some metal ions effect on enzyme activity" @default.
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- W1874430456 doi "https://doi.org/10.3109/14756366.2015.1046063" @default.
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