Purification of glutathione<i>S</i>-transferase from Van Lake fish (<i>Chalcalburnus tarichii</i>Pallas) muscle and investigation of some metal ions effect on enzyme activity

Aksoy, Mine; Özaslan, Muhammet Serhat; Küfrevioğlu, Ömer İrfan

doi:10.3109/14756366.2015.1046063

Cited by 33 publications

(27 citation statements)

References 46 publications

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“…Enzymatic activity inhibition by metals is also well described in the literature . SOD inhibition after subchronic exposure could be due to TiO 2 ‐NP dissociation into cations that compete with enzymatic cofactors (ions) for the allosteric site of SOD, thus causing its inhibition.…”

Section: Discussionmentioning

confidence: 91%

Overview of the toxic effects of titanium dioxide nanoparticles in blood, liver, muscles, and brain of a Neotropical detritivorous fish

Carmo

Siqueira

Azevedo

et al. 2019

Environmental Toxicology

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The toxicity of titanium dioxide nanoparticles (TiO 2 -NP) in the blood, liver, muscle, and brain of a Neotropical detritivorous fish, Prochilodus lineatus, was tested. Juvenile fish were exposed to 0, 1, 5, 10, and 50 mg L −1 of TiO 2 -NP for 48 hours (acute exposure) or 14 days (subchronic exposure) to evaluate changes in hematology, red blood cell (RBC) genotoxicity/mutagenicity, liver function (reactive oxygen species (ROS) production, antioxidant responses, detoxification, and histopathology), acetylcholinesterase (AChE) activity in muscles and brain, and Ti bioaccumulation. TiO 2 -NP did not cause genetic damage to RBC, but acutely decreased white blood cells (WBC) and increased monocytes. Subchronically, RBC decreased, mean cell volume and hemoglobin increased, and WBC and lymphocytes decreased. Therefore, NP has the potential to affect immune system and increase energy expenditure, reducing the fish's ability to avoid predator and to resist pathogens. In the liver, acute exposure decreased ROS and increased glutathione (GSH) content, while subchronic exposure decreased superoxide dismutase activity and increased glutathione-S-transferase (GST) activity and GSH content. GSH and GST seem to play an essential role in metabolizing NP and ROS, likely increasing hepatocytes' metabolic rate, which may be the cause of observed cell hypertrophy, disarrangement of hepatic cords and degenerative morphological alterations. Although most studies indicate that the kidney is responsible for metabolizing and/or eliminating TiO 2 -NP, this study shows that the liver also has a main role in these processes. Nevertheless, Ti still accumulated in the liver, muscle, and brain and decreased muscular AChE activity after acute exposure, showing neurotoxic potential.More studies are needed to better understand the biochemical pathways TiO 2 -NP are metabolized and how its bioaccumulation may affect fish homeostasis and survival in the environment. K E Y W O R D S bioaccumulation, glutathione-S-transferase neurotoxicity, immune system, reactive oxygen species

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Section: Discussionmentioning

confidence: 91%

Overview of the toxic effects of titanium dioxide nanoparticles in blood, liver, muscles, and brain of a Neotropical detritivorous fish

Carmo

Siqueira

Azevedo

et al. 2019

Environmental Toxicology

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“…Then SDS-PAGE were stained and distained and single band was appeared on the gel, it is an evidence to purified enzymes. The same method were used in rat brain cytosol [11], human placenta [13], human hepatoma [25], rainbow trout hepatocytes [14], filarial worms Setaria cervi [26], rat liver [16], turkey liver [17], Van Lake fish liver [23], and muscle tissue of Van Lake fish [18]. SDS-PAGE method is suitable and powerful method to check purity of enzymes with good results by less time and easy to work.…”

Section: Discussionmentioning

confidence: 99%

“…Glutathione S-tansferase GSTs have been purified and characterized from different sources such as rat brain cytosol [11], humane kidney [12], human placental tissues [13], and rainbow trout hepatocytes [14], liver of the freshwater fish Monopterus albus [15], rat liver [16], turkey liver [17], muscle tissue of Van Lake fish [18] and quail liver [19]. There have been used different techniques such as the affinity, ion exchange, hydrophobic, and gel filtration chromatography to purification.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization glutathione S-transferase enzyme from quail (Coturnix, coturnix japonica) heart and investigation the effect of some metal ions on enzyme activity

Ahmed

Temel

Çiftçi

2019

Cumhuriyet Science Journal

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In this study glutathione S-transferase enzyme (EC: 2.5.1.18) from the heart of japonica quail was purified with 34.0 EU/mg specific activity, 10.44% purification yield and 78.29 purification folds and characterized. Purification processes are consist of three steps, firstly homogenate was prepared, and then ammonium sulfate precipitation was performed and finally glutathione-agarose gel affinity column chromatography was performed. To check the purity of GST enzyme used SDS-PAGE method. Then the M.W calculated at approximately 26.3 kDa by SDS-PAGE method. Enzymatic activity was determined spectrofotometrically according to Beutler`s method at 340 nm. Also characterizations study carry out, and the results obtained are stability-pH = 9.0 in Tris/HCL buffer, optimum pH = 8.0 in Tris/HCl buffer, optimum temperature 60 °C, optimum ionic strength was 1.2 M in Tris/HCl buffer. And kinetic studies performed for GST enzyme purified from quail heart by used both glutathione and 1-chloro 2,4-dinitrobenzen as substrate. KM and Vmax values are determined as 1.642 mM and 0.502 EU/mL respectively for GSH substrate and 3.880 mM and 0.588 EU/mL respectively for CDNB substrate. In addition, the effect of some metal ions (Cu 2+ , Cd 2+ , Fe 2+ , Fe 3+ Zn 2+ , Ag + , Co 2+ , and Ti 1+) were investigated on the GST enzyme activity in vitro.

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“…A spectrophotometer was used to estimate the changes in absorbance at 340 nm for 3 min. One unit of activity is defined as the formation of 1.0 μmol product per minute …”

Section: Methodsmentioning

confidence: 99%

Evaluation of chalcones as inhibitors of glutathione S‐transferase

Özaslan

Demir

Aslan

et al. 2018

J Biochem & Molecular Tox

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Glutathione S-transferases (GSTs) are the superfamily of multifunctional detoxification isoenzymes and play an important role in cellular signaling. In the present study, potential inhibition effects of chalcones were tested against human GST. For this purpose, GST was purified from human erythrocytes with 5.381 EU⋅mg specific activity and 51.95% yield using a GSH-agarose affinity chromatographic method. The effects of chalcones on in vitro GST activity were tested at various concentrations. K constants of chalcones were found in the range of 7.76-41.93 μM. According to the results, 4-fluorochalcone showed a better inhibitory effect compared with the other compounds. The inhibition mechanisms of 2'-hydroxy-4-methoxychalcone and 4-methoxychalcone were noncompetitive, whereas the inhibition mechanisms of 4'- hydroxychalcone, 4- fluorochalcone, and 4,4'- diflurochalcone were competitive.

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Purification of glutathioneS-transferase from Van Lake fish (Chalcalburnus tarichiiPallas) muscle and investigation of some metal ions effect on enzyme activity

Cited by 33 publications

References 46 publications

Overview of the toxic effects of titanium dioxide nanoparticles in blood, liver, muscles, and brain of a Neotropical detritivorous fish

Overview of the toxic effects of titanium dioxide nanoparticles in blood, liver, muscles, and brain of a Neotropical detritivorous fish

Purification and characterization glutathione S-transferase enzyme from quail (Coturnix, coturnix japonica) heart and investigation the effect of some metal ions on enzyme activity

Evaluation of chalcones as inhibitors of glutathione S‐transferase

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