Department of Agricultural Biotechnology, Faculty of Agriculture, Ondokuz Mayıs University, Samsun, Turkey.
Biotechnol Appl Biochem. 2022 Feb;69(1):145-148. doi: 10.1002/bab.2090. Epub 2021 Jan 7.
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 values of the tested metal ions were calculated to be 0.1112, 0.6113, 0.727, and 0.7774 mM for Cd , Fe , Ag , and Cu , respectively. Our results show that these heavy metals inhibit GST at very low concentrations which could cause dangerous results for aquatic systems.
谷胱甘肽 S-转移酶（GST）能够解毒多种外源物质，尤其是在化疗药物、内源性分子和环境污染物中。由于该酶能够代谢有毒化合物，因此在包括水生生物在内的许多生物中得到了广泛研究。在本研究中，首次从褐色鲳鱼肌肉组织中纯化出 GST 酶。然后，确定了该酶的动力学参数，最适离子强度为 20 mM Tris/HCl，最适 pH 值为 7.0（Tris/HCl），最适底物浓度为 3.125 mM。最后，评估了重金属的抑制作用。测试金属离子的 IC 值分别为 0.1112、0.6113、0.727 和 0.7774 mM，对于 Cd、Fe、Ag 和 Cu。我们的结果表明，这些重金属在非常低的浓度下就可以抑制 GST，这可能会对水生系统造成危险的后果。
