The effect of some antibiotics on glutathione reductase enzyme purified from liver and erythrocyte of Lake Van pearl mullet

Altun, Muhammed; Türkoğlu, Vedat; Çelik, İsmail

doi:10.3109/13880209.2014.997830

Cited by 9 publications

(9 citation statements)

References 28 publications

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“…Moreover, the molecular weight of each subunit of the purified enzyme was found as 55 kDa using the SDS-PAGE electrophoresis method. This result has very good fit compared to purified GR enzymes such as from liver and erythrocytes of Lake Van pearl mullet [13], bovine liver [15], bovine filarial worms Setaria cervi [20], and rainbow trout (Oncorhynchus mykiss) liver [21].…”

Section: Resultsmentioning

confidence: 73%

“…As is known, the truest findings for enzyme kinetics are obtained from the purified enzyme. Therefore, GR has been purified many times and from many different sources in unicellular and multicellular organisms, such as liver and erythrocytes of Lake Van pearl mullet, Streptococcus pneumoniae, and bovine liver [13][14][15]. This revealed the value of GR.…”

Section: Introductionmentioning

confidence: 99%

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Investigation of the effects of some water-soluble vitamins on glutathionereductase enzyme purified from bovine liver

Kivanç¹,

Türkoğlu²

2019

Turk J Chem

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Glutathione reductase (GR, EC 1.8.1.7) is an antioxidant enzyme and is involved in the reducing reaction of oxidized glutathione. Glutathione and reduced glutathione are very crucial for micro-and macroorganisms because of their barrier function against radicals. Therefore, the aim of this article was to purify GR and evaluate the relationship between purified GR and vitamins. GR was purified from bovine liver using 2',5'-ADP Sepharose 4B column materials. To check the purity of each subunit of the enzyme, SDS-PAGE electrophoresis was performed and each one was 55 kDa. Afterwards, specific activity and purified ratio for the enzyme were calculated as 54 EU/mg × protein and 2700 times, respectively. Vitamins have a regulatory role in organisms and also some, like vitamin B, are coenzymes due to having cofactor effects. In this project, variable concentrations of some water-soluble vitamins, riboflavin, ascorbic acid, nicotinamide, folic acid, and thiamine, were tested. As a result of these kinetic findings, nicotinamide and folic acid increased the activity of glutathione reductase, while thiamine decreased it. Riboflavin and ascorbic acid did not show a stable effect on enzyme activity. Ki and IC 50 constants were found as 50.16 ± 5.63 mM and 21.04 mM, respectively, when Lineweaver-Burk and activity % vs. inhibitor concentration graphs were drawn for thiamine. The results of this article illustrate that the behaviors of vitamins could be complicated and vary from one living organism to other; in other words, they are unpredictable.

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Section: Resultsmentioning

confidence: 73%

Section: Introductionmentioning

confidence: 99%

Investigation of the effects of some water-soluble vitamins on glutathionereductase enzyme purified from bovine liver

Kivanç¹,

Türkoğlu²

2019

Turk J Chem

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“…Ulusu and Tandoğan reported the subunit molecular weight of GR from bovine liver to be 55 kDa (Ulusu & Tandoğan, ). In another study, the subunit molecular weight of GR purified from Chalcalburnus tarichi liver and erythrocytes was 55 kDa (Altun et al, ).…”

Section: Resultsmentioning

confidence: 98%

“…Active fractions were detected by measuring the enzyme activity as mentioned below. All of the procedures were performed at 4°C (Altun et al, ).…”

Section: Methodsmentioning

confidence: 99%

“…From crystallographic analysis of GR, it consists of main four structures—FAD, NADPH, central and interface structures (Aydemir, Hashemkhani, Durmusoglu, Acar, & Ulusu, ; Kocaoğlu et al, ; Savvides et al, ). There are many reports on the purification, characterization and kinetics of GR from a variety of organisms, including unicellular or multicellular organisms, turkey liver (Taşer & Çiftci, ), liver and erythrocytes of Lake Van pearl mullet (Altun, Türkoğlu, & Çelik, ), bovine filarial worms Setaria cervi (Arora, Ahmad, & Srivastava, ) and Streptococcus pneumoniae (Sikanyika, Aragão, McDevitt, & Maher, ).…”

Section: Introductionmentioning

confidence: 99%

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Investigation of the effects of natural compounds isolated from Arum rupicola var. rupicola on glutathione reductase enzyme purified from bovine liver

Kivanç

Türkoğlu

2019

Biomedical Chromatography

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Glutathione reductase (GR, E.C. 1.8.1.7), a flavoenzyme, is responsible for recycling of oxidized glutathione disulfide. This study was performed in two main sections. In the first GR was purified from bovine liver by affinity column chromatography and the purification rate and specific activity of the enzyme were calculated as 1832-fold and 141 EU/mg protein, respectively. The subunit molecular weight of the enzyme was determined as 55 kDa by means of SDS-PAGE. The second section isolated natural components of Arum rupicola Boiss. var. rupicola using column chromatography.The isolation protocol for this plant was performed with a series of different-sized columns with hexane-ethyl acetate. According to the thin-layer chromatography plate, seven substances (R1-R7) were isolated. Our study's aim was to find new activators or inhibitors for GR activity. With this aim, all isolated substances were tested for GR activity. R6 showed competitive inhibition, while R4 had noncompetitive inhibition of GR activity. R1 played a role as an activator of GR activity.The inhibitory activity percentage vs. concentration graph was plotted. Values of IC 50 for R4 and R6 were calculated as 0.193 mg/mL and 3.98 μg/mL, respectively, from the equation of this graph.Additional supporting information may be found online in the Supporting Information section at the end of the article. How to cite this article: Kıvanç MR, Türkoglu V. Investigation of the effects of natural compounds isolated from Arum rupicola var. rupicola on glutathione reductase enzyme purified from bovine liver. Biomedical Chromatography. 2019;33:e4560.

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An in vivo and in vitro comparison of the effects of amoxicillin, gentamicin, and cefazolin sodium antibiotics on the mouse hepatic and renal glutathione reductase enzyme

Güller

Budak

Şişecioğlu

et al. 2020

J Biochem & Molecular Tox

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Despite the fact that the use of antibiotics is increasing worldwide, it is clear that antibiotics can lead to oxidative stress. This is the first study to make a comparison of the impact of frequently prescribed antibiotics, including amoxicillin, gentamicin, and cefazolin sodium, on the gene, protein, and activity of glutathione reductase (GR), which is one of the primary antioxidant enzymes, in mouse liver and kidney tissues. First, the GR enzyme was purified by the 2′,5′‐ADP Sepharose 4B affinity chromatography with a specific activity of 84.615 EU/mg protein and 9.63 EU/mg protein from the mouse liver and kidney, respectively. The in vitro inhibitory effects of the antibiotics in question was determined. While cefazolin sodium did not exhibit any inhibitory effect, gentamicin and amoxicillin inhibited GR activity in both tissues. Furthermore, the in vivo effects of these drugs were investigated, and amoxicillin and cefazolin sodium‐inhibited GR activity in both liver and kidney tissues, while gentamicin did not have any effect on the kidney. Besides, while gentamicin downregulated and cefazolin sodium upregulated Gr gene expression, amoxicillin did not alter it. Protein expression was only affected by the administration of cefazolin sodium in the kidney. This study is important as it demonstrates that while amoxicillin and gentamicin showed parallel effects on the GR activity in liver and kidney tissues both in vitro and in vivo, cefazolin sodium had a very strong effect on hepatic and renal GR in vivo. Furthermore, the antibiotics used in this study induced oxidative stress in both tissues.

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The effect of some antibiotics on glutathione reductase enzyme purified from liver and erythrocyte of Lake Van pearl mullet

Cited by 9 publications

References 28 publications

Investigation of the effects of some water-soluble vitamins on glutathionereductase enzyme purified from bovine liver

Investigation of the effects of some water-soluble vitamins on glutathionereductase enzyme purified from bovine liver

Investigation of the effects of natural compounds isolated from Arum rupicola var. rupicola on glutathione reductase enzyme purified from bovine liver

An in vivo and in vitro comparison of the effects of amoxicillin, gentamicin, and cefazolin sodium antibiotics on the mouse hepatic and renal glutathione reductase enzyme

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