Some metals inhibit the glutathione S-transferase from Van Lake fish gills
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.
Anahtar kelimeler
Atıf için künye
Ozaslan, M. S., DEMİR, Y., Küfrevioğlu, Ö. İ., & ÇİFTCİ, M. (2017). Some metals inhibit the glutathione S-transferase from Van Lake fish gills. JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY, 31(11). https://doi.org/10.1002/jbt.21967
BibTeX
@article{ozaslan2017-68782,
author = {Ozaslan, M. Serhat and DEMİR, YELİZ and Küfrevioğlu, Ömer İrfan and ÇİFTCİ, MEHMET},
title = {Some metals inhibit the glutathione S-transferase from Van Lake fish gills},
journal = {JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY},
year = {2017},
volume = {31},
number = {11},
issn = {1095-6670},
doi = {10.1002/jbt.21967},
url = {https://akademik.atauni.edu.tr/yayinlar/68782-some-metals-inhibit-the-glutathione-s-transferase-from-van-lake-fish-gills}
}