Characterization of glutathioneS‐transferase enzyme from brown meagre (Sciaena umbra) and inhibitory effects of heavy metals

Abstract

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. IC 50 values of the tested metal ions were calculated to be 0.1112, 0.6113, 0.727, and 0.7774 mM for Cd 2+ , Fe 3+ , Ag + , and Cu 2+ , respectively. Our results show that these heavy metals inhibit GST at very low concentrations which could cause dangerous results for aquatic systems. ©

Acute exposure of fruit bats to low concentrations of heavy metals affects oxidative stress markers

“…GSTs are a family of antioxidant isoenzymes that participate in the cellular detoxification of several xenobiotics. The inhibitory effects of metals in GST activity may be harmful to the cells (Guven and Soydan, 2022). Several studies showed decreased GST activities following HMs exposure in testes of mammals, such as decreased GST after 20mg/kg of Pb (i.p.)…”