Characterization of glutathione <i>S</i>-transferase enzyme from brown meagre (<i>Sciaena umbra</i>) and inhibitory effects of heavy metals

Guven N., Soydan E.

BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY, cilt.69, sa.1, ss.145-148, 2022 (SCI-Expanded, Scopus) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 69 Sayı: 1
  • Basım Tarihi: 2022
  • Doi Numarası: 10.1002/bab.2090
  • Dergi Adı: BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Applied Science & Technology Source, BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Chemical Abstracts Core, Compendex, Computer & Applied Sciences, EMBASE, Environment Index, Food Science & Technology Abstracts, INSPEC, MEDLINE, Veterinary Science Database
  • Sayfa Sayıları: ss.145-148
  • Ankara Üniversitesi Adresli: Hayır

Özet

Glutathione S-transferase (GST) detoxifies a broad spectrum of xenobiotics, especially in chemotherapeutic drugs, endogenous molecules, and environmental pollutants. Since the enzyme metabolizes toxic compounds, it has been extensively studied in many living things including aquatic organisms. In the current study, the GST enzyme was purified from brown meagre (Sciaena umbra) muscle tissue for the first time. Then, kinetic parameters of the enzyme were determined as optimum ionic strength: 20 mM Tris/HCl, optimum pH: 7.0 (Tris/HCl), and optimum substrate concentration: 3.125 mM. Eventually, inhibitory effects of the heavy metals were evaluated. IC50 values of the tested metal ions were calculated to be 0.1112, 0.6113, 0.727, and 0.7774 mM for Cd2+, Fe3+, Ag+, and Cu2+, respectively. Our results show that these heavy metals inhibit GST at very low concentrations which could cause dangerous results for aquatic systems.