Some metals inhibit the glutathione S-transferase from Van Lake fish gills

Ozaslan M. S., DEMİR Y., KÜFREVİOĞLU Ö. İ., ÇİFTCİ M.

JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY, cilt.31, sa.11, 2017 (SCI-Expanded) identifier identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 31 Sayı: 11
  • Basım Tarihi: 2017
  • Doi Numarası: 10.1002/jbt.21967
  • Dergi Adı: JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Anahtar Kelimeler: glutathione S-transferase, inhibition, purification, Van Lake fish, CARBONIC-ANHYDRASE ACTIVITY, RAINBOW-TROUT ERYTHROCYTES, ENZYME-ACTIVITY, HEAVY-METALS, PURIFICATION, LIVER, MECHANISM, CLONING, IONS, HISTOPATHOLOGY
  • Atatürk Üniversitesi Adresli: Evet

Özet

Glutathione S-transferases (GSTs) are the superfamily of multifunctional detoxification isoenzymes and play important role cellular signaling. The present article focuses on the role of Cd2+, Cu2+, Zn2+, and Ag(+)in vitro inhibition of GST. For this purpose, GST was purified from Van Lake fish (Chalcalburnus tarichii Pallas) gills with 110.664EUmg(-1) specific activity and 79.6% yield using GSH-agarose affinity chromatographic method. The metal ions were tested at various concentrations on in vitro GST activity. IC50 values were found for Cd+2, Cu+2, Zn+2, Ag+ as 450.32, 320.25, 1510.13, and 16.43M, respectively. K-i constants were calculated as 197.05 +/- 105.23, 333.10 +/- 152.76, 1670.21 +/- 665.43, and 0.433 +/- 0.251M, respectively. Ag+ showed better inhibitory effect compared with the other metal ions. The inhibition mechanisms of Cd2+ and Cu2+ were non-competitive, whereas Zn2+ and Ag+ were competitive. Co2+, Cr2+, Pb2+, and Fe3+ had no inhibitory activity on GST.