Purification of glutathione S-transferase from Van Lake fish (Chalcalburnus tarichii Pallas) muscle and investigation of some metal ions effect on enzyme activity


AKSOY M. , Ozaslan M. S. , KÜFREVİOĞLU Ö. İ.

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.31, ss.546-550, 2016 (SCI İndekslerine Giren Dergi) identifier identifier identifier

  • Cilt numarası: 31 Konu: 4
  • Basım Tarihi: 2016
  • Doi Numarası: 10.3109/14756366.2015.1046063
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Sayfa Sayısı: ss.546-550

Özet

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. K-M values were 1.59 and 0.53mM for 1-chloro-2,4-dinitrobenzene (CDNB) and glutathione (GSH), respectively. V-max values for CDNB and GSH were also determined as 5.58 and 1.88 EU/mL, respectively. In addition, inhibition effects of Ag+, Cu2+, Cd2+, Fe3+, Pb2+, Cr2+, Co2+ and Zn2+ metal ions were investigated on the enzyme activity and IC50, K-i values were calculated for these metal ions.