Purification of glutathione S-transferase from Van Lake fish (Chalcalburnus tarichii Pallas) muscle and investigation of some metal ions effect on enzyme activity
JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.31, sa.4, ss.546-550, 2016 (SCI-Expanded, Scopus)
- 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
- 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.