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, sa.4, ss.546-550, 2016 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 31 Sayı: 4
  • Basım Tarihi: 2016
  • Doi Numarası: 10.3109/14756366.2015.1046063
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.546-550
  • Anahtar Kelimeler: Glutathione S-transferase, inhibition, metal ions, purification, Van Lake fish, CRYSTAL-STRUCTURE, 3-DIMENSIONAL STRUCTURE, BIOCHEMICAL-CHARACTERIZATION, KINETIC MECHANISM, RAINBOW-TROUT, LIVER, BIOMARKERS, ATRAZINE, CLONING, DETOXIFICATION
  • Atatürk Üniversitesi Adresli: Evet

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.