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. 2023 Dec;38(1):2167078.
doi: 10.1080/14756366.2023.2167078.

Purification and characterisation of glutathione reductase from scorpionfish (scorpaena porcus) and investigation of heavy metal ions inhibition

Kübra Işık  1 , Ercan Soydan  1
Affiliations

Purification and characterisation of glutathione reductase from scorpionfish (scorpaena porcus) and investigation of heavy metal ions inhibition

Kübra Işık et al. J Enzyme Inhib Med Chem. 2023 Dec.

Abstract

In the current study, glutathione reductase was purified from Scorpion fish (Scorpaena porcus) liver tissue and the effects of heavy metal ions on the enzyme activity were determined. The purification process consisted of three stages; preparation of the homogenate, ammonium sulphate precipitation and affinity chromatography purification. At the end of these steps, the enzyme was purified 25.9-fold with a specific activity of 10.479 EU/mg and a yield of 28.3%. The optimum pH was found to be 6.5, optimum substrate concentration was 2 mM NADPH and optimum buffer was 300 mM KH2PO4. After purification, inhibition effects of Mn+2, Cd+2, Ni+2, and Cr3+, as heavy metal ions were investigated. IC50 values of the heavy metals were calculated as 2.4 µM, 30 µM, 135 µM and 206 µM, respectively.

Keywords: Glutathione reductase; enzyme purification; inhibition; metal ion; scorpion fish.

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Conflict of interest statement

No potential conflict of interest was reported by the author(s).

Figures

Figure 1.
Figure 1.
Activity %-inhibitor regression analysis graph for Scorpionfish GR in the presence of different Mn2+ concentrations.
See this image and copyright information in PMC

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