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Investigation of the Inhibition Effects of Some Metal Ions on Glutathione Reductase Enzyme From Japanese Quail (Coturnix coturnix japonica) Liver

Year 2018, Volume: 39 Issue: 3, 679 - 687, 30.09.2018

Yusuf Temel , Sarkat Salim Mohammed Taher Mohammad Ahmad Hamza İbrahim Hamdi Shafeeq Ümit Muhammet Koçyiğit , Mehmet Çiftçi

https://doi.org/10.17776/csj.414680
Cited By: 5

Abstract

In the present study, the inhibition effect of
some heavy metal ions on glutathione reductase (GR) enzyme which has important
functions in metabolism, was investigated. For this purpose, GR enzyme was
purified with 19.33 EU/mg specific activity, a yield of 14.06% and 128.8-fold
from quail liver by using ammonium sulphate precipitation and 2ʹ, 5ʹ-ADP
Sepharose 4B affinity chromatography. To check the purity of GR enzyme, sodium
dodecyl sulfate polyacrilamide gel electrophoresis (SDS-PAGE) was performed and
single band was observed. The activity of the GR enzyme was measured
spectrophotometrically at 340 nm according to the method of Carlberg and
Mannervik. Then, the inhibitory effects of different heavy metal ions (Co 2+,
Zn 2+, Pb 2+, Fe 2+, Cd 2+, Al 3+
and Fe 3+) on the activity of GR enzyme were examined under in vitro
conditions. For the GR enzyme from quail liver tissue, heavy metal
concentrations (IC50) were obtained in which 50% of GR enzyme
activity was inhibited in vitro conditions. Finally, Ki values for
these metal ions were calculated from the Lineweaver-Burk plots.

Keywords

Glutathion Reductase Enzyme Purification Quail Inhibition Liver

References

  • [1]. Veine D.M., Arscott L.D., Williams C.H., Redox potentials for yeast, Escherichia coli and human glutathione reductase relative to the NAD +/NADH redox couple: enzyme forms active in catalysis, Biochem. 37 (1998) 15575-15582.
  • [2]. Wong K.K., Vanoni M.A., Blanchard J.S., Glutathione reductase: solvent equilibrium and kinetic isotope effects, Biochem. 28 (1989) 3586-3590.
  • [3]. Bauer H., Fritz-Wolf K., Winzer A., Kuhner S., Little S., Yardley V., Vezin H., Palfey B., Schirmer R.H., Davioud-Charvet E., A fluoro analogue of the menadione derivative 6-[2`-(3`-methyl) -1`,4`-napht- hoquinolyl] hexanoic acid is a suicide substrate of glutathione reductase. crystal structure of the alkylated human enzyme, J. Am. Chem. Soc. 128 (2006) 10784-10794.
  • [4]. Yawata Y. and Tanaka K.R., Regulatory mechanism activity, Blood. 43 (1974) 99-110.
  • [5]. Tandogan B., Ulusu N.N., Kinetic mechanism and molecular properties of glutathione reductase, Plant Phsy. 31 (2006) 230-237.
  • [6]. Chang J.C., Hoeven V., Haddox C.H., Glutathione reductase in the red blood cells, An. Clin. Lab. Sci. 8 (1978) 23–29.
  • [7]. Garcia-Leiro A., Cerdan M.E., Gonzalez-Siso M.I., Characterization of chromosomal integration sites for heterologous gene expression in saccharomyces cerevisiae, Yeast. 26 (2009) 545–551.
  • [8]. Adem S. and Ciftci M., Purification and characterization of glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and glutathione reductase fromrat heart and inhibition effects of furosemide, digoxin, and dopamine on the enzymes activities, J. Biochem. Mol. Tox. 28 (2016) 246-255.
  • [9]. Yong Z., Teresa S., Wei C., Xiuqing W., Duane M., Yueshan H., Xiangming G., Effects of glutathione reductase inhibition on cellular thiol redox state and related systems, Arch. Biochem. Biophy. 485 (2009) 56-62.
  • [10]. Temel Y., Küfrevioğlu Ö.İ., Çiftci M., Investigation of the effects of purification and characterization of turkey (Meleagris gallopavo) liver mitochondrial thioredoxin reductase enzyme and some metal ions on enzyme activity, Turk. J. Chem. 41 (2017) 48-60.
  • [11]. Temel Y. and Kocyigit U.M., Purification of glucose-6-phosphate dehydrogenase from rat (Rattus norvegicus) erythrocytes and inhibition effects of some metal ions on enzyme activity, J. Biochem. Mol. Tox. 31 (2017) e21927.
  • [12]. Temel Y., Bengü A.Ş., Akkoyun H.T., Akkoyun M.B., Çiftci M., Effect of astaxanthin and aluminum chloride on erythrocyte G6PD and 6PGD enzyme activities in vivo and on erythrocyte G6PD in vitro in rats, J. Biochem. Mol. Tox. 31 (2017) e21954. [13]. Kocyigit U.M., Aslan O.N., Gulcin I., Temel Y., Ceylan M., Synthesis and Carbonic Anhydrase Inhibition of Novel 2-(4-(Aryl)thiazole-2-yl)-3a,4,7,7a-tetrahydro -1H-4,7-methanoisoindole 1,3 (2H) - dione Derivatives, Arch. Pharm. 349 (2016) 955-963.
  • [14]. Ceylan M., Kocyigit U.M., Usta N.C., Gürbüzlü B., Temel Y., Alwasel S.H., Gulcin I., Synthesis, carbonic anhydrase I and II iso enzymes inhibition properties, and antibacterial activities of novel tetralone-based 1,4-benzothiazepine deriva tives, J. Biochem. Mol. Tox. 31 (2017) e21872 .
  • [15]. Bayındır S., Ayna A., Temel Y., Çiftci M., The synthesis of new oxindoles as analogs of natural product 3,3'-bis(indolyl)oxindole and in vitro evaluation for enzyme activity of G6PD and 6PGD, Turk. J. Chem. 42 (2018) 332- 345.
  • [16]. Jan A.T, Azam M., Siddiqui K., Ali A., Choi I., Haq Q.M.R., Heavy Metals and Human Health: Mechanistic Insight into Toxicity and Counter Defense System of Antioxidants, Int. J. Mol. Sci. 16 (2015) 29592–29630.
  • [17]. Gutteridge J.M., Lipid peroxidation and antioxidants as biomarkers of tissue damage, Clin. Chem. 41 (1995) 1819-28.
  • [18]. Federico M.R., Toxicity of Glutathione-Binding Metals, A Rev. Targ. Mech. Tox. 3 (2015) 20-62.
  • [19]. Valko M., Morris H., Cronin M.T., Metals, toxicity and oxidative stress, Cur. Med. Chem. 12 (2005) 1161-1208.
  • [20]. Khalid R., Studies on free radicals, antioxidants, and co-factors, Clin. Inter. Ag. 2 (2007) 219-236.
  • [21]. Hubrecht R., Kirkwood J., The UFAW Handbook on the Care and Management of Laboratory and Other Research Animals. John Wiley & Sons. (2010). 655-674.
  • [22]. Carlberg I. and Mannervik B., Purification and characterization of glutathione reductase from calf liver. an improved procedure for affinity chromatography on 2′,5′-ADP-Sepharose-4B, Anal. Biochem. 536 (1981) 531-36.
  • [23]. Latta K. and Augusteyn R.C., The purification and properties of human reductase lens glutathione, Exp. Eye Res. 39 (1984) 343–54.
  • [24]. Lopez-Barea J. and Lee C.Y., Mouse liver glutathione reductase, Europ. J. Biochem. 499 (1979) 487-99.
  • [25]. Madamanchi N.R., Anderson J.V., Alscher R.G., Cramer C.L., Hess C.L., Purification of multiple forms of glutathione reductase from pea (pisum sativum l) seedlings and enzyme levels in ozone-fumigated pea leaves, Plant Phys. 100 (1992) 138-45.
  • [26]. Boese M., Keese M.A., Becker K., Busse R., Mulsch A., Inhibition of glutathione reductase by dinitrosyl-iron-dithiolate complex, J. Biol. Chem. 272 (1997) 21767–2173.
  • [27]. Elliott A.J., Scheiber S.A., Thomas C., Pardini R.S., Inhibition of glutathione reductase by flavonoids. a structure-activity study, Biochem. Pharm. 44 (1992) 1603–1608.
  • [28]. Erat M. and Ciftci M., Effect of melatonin on enzyme activities of glutathione reductase from human erythrocytes in vitro and from rat erythrocytes in vivo, Europ. J. Pharm. 537 (2006) 59–63.
  • [29]. Jervell J., and Vallance-Owen J., Inhibition of glutathione reductase in diabetics and non-diabetics, Diabet. 3 (1967) 353-354.
  • [30]. Ghosh S.K., Ghosh S., Gachhui R., Mandal A., Mercury and organomercurial resistance in Rhodotorula rubra: Activation of glutathione reductase, Bull. Env. Contam. Tox. 77 (2006): 351-358.
  • [31]. Erat M., Ciftci M., Gumustekin K., Gül M., Effects of nicotine and vitamin E on glutathione reductase activity in some rat tissues in vivo and in vitro, Europ. J. Pharm. 554 (2007) 92-97.
  • [32]. Ono S. and Hirano H., FAD-induced in vitro activation of glutathione reductase in the lens of B2 deficient rats. Curr. Eye Res. 3 (1984) 663-665.
  • [33]. Palmer E.J., MacManus J.P., Mutus B., Inhibition of glutathione reductase by oncomodulin, Arch. Biochem. Biophy. 277 (1990) 149-154.
  • [34]. Rafter G.W., Copper inhibition of glutathione reductase and its reversal with gold thiolates, thiol, and disulfide compounds, Biochem. Med. 27 (1982) 381-391.
  • [35]. Sentürk M., Talaz O., Ekinci D., Cavdar H., Küfrevioğlu O.I. In vitro inhibition of human erythrocyte glutathione reductase by some new organic nitrates, Bioorg. Med. Chem. Let. 19 (2009) 3661-3663.
  • [36]. Stýblo M. and David J.T., In vitro inhibition of glutathione reductase by arseno triglutathione, Biochem. Pharm. 49 (1995) 971-977.
  • [37]. Ulusu N., Acan N., Turan B., Tezcan E., Inhibition of glutathione reductase by cadmium ion in some rabbit tissues and the protective role of dietary selenium, Biol. Trace El. Res. 91 (2003) 151-156.
  • [38]. Zhang K., Yang E.B., Tang W.Y., Wong K.P., Mack P., Inhibition of glutathione reductase by plant polyphenols, Biochem. Pharm. 54 (1997) 1047-1053.
  • [39]. Trang L.N., Kuldeep K.B., Anthony C., Purification of glutathione reductase from gerbil liver in two steps, Anal. Biochem. 133 (1983) 94-99.
  • [40]. Boggaram V., Brobjer T., Larson K., Mannervik B., Purification of glutathione reductase from porcine erythrocytes by the use of affinity chromatography on 2′, 5′-ADP-Sepharose 4B and crystallization of the enzyme, Anal. Biochem. 98 (1979) 335-340.
  • [41]. Erat M., and Ciftci M., In vitro effects of some antibiotics on glutathione reductase from sheep liver, J. Enz. Inh. Med. Chem. 18 (2003) 545-550.
  • [42]. Taşer P. and Ciftci M., Purification and characterization of glutathione reductase from turkey liver, Turk. J. Vet. Ani. Sci. 36 (2012) 546-553.
  • [43]. Carlberg I. and Mannervik B., Glutathione reductase, Meth. Enz. 113 (1985) 484-490.
  • [44]. Bradford M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
  • [45]. Laemmli, U.K., Most commonly used discontinuous buffer system for SDS electrophoresis, Nat. 227 (1970) 680-686.
  • [46]. Lineweaver H. and Burk D., The determination of enzyme dissociation constants, J. Am. Chem. Soc. 56 (1934) 658-666.
  • [47]. Pradedova E.V., Isheeva O.D., Salyaev R.K., Classification of the antioxidant defense system as the ground for reasonable organization of experimental studies of the oxidative stress in plants, Rus. J. Plant Phys. 58 (2011) 210-217.
  • [48]. Hakiman M. and Maziah M., Non enzymatic and enzymatic antioxidant activities in aqueous extract of different ficus deltoidea accessions, J. Med. Plants Res. 3 (2009) 120-131.
  • [49]. Vaisi-Raygani A., Rahimi Z., Zahraie M., Noroozian M. Poutrmotabbed A., Iran. J. Med. Sci. 45 (2007) 271–76.
  • [50]. Coban T.A., Senturk M., Ciftci M., Kufrevioglu O.I., Effects of some metal ions on human erythrocyte glutathione reductase: an in vitro study, Prot. Pept. Let. 14 (2007) 1027-1030.
  • [51]. Coban T. A., Beydemir S., Gülcin I., Ekinci D., Innocenti A., Vullo D., Supuran C.T., Sildenafil is a strong activator of mammalian carbonic anhydrase isoforms I–XIV., Bioorg. Med. Chem. 17 (2009) 5791-5795.
  • [52]. Ekinci D. and Beydemir S., Purification of PON1 from human serum and assessment of enzyme kinetics against metal toxicity, Biol. Trace El. Res. 135 (2010) 112-120.
  • [53]. Ekinci D., Ceyhun S.B., Sentürk M., Erdem D., Küfrevioğlu O.İ., Supuran C.T., Characterization and anions inhibition studies of an α-carbonic anhydrase from the teleost fish Dicentrarchus labrax, Bioorg. Med. Chem. 19 (2011) 744-748.
  • [54]. Li D., Yang M.S., Lin T., Zheng W., Qu J.Y., Study of cadmium-induced cytotoxicity using two-photon excitation endogenous fluorescence microscopy, J. Biomed. Opt. 14 (2009) 054028.
  • [55]. Comakli V., Akkemik E., Ciftci M., Kufrevioglu O.I., Purification and characterization of glucose 6-phosphate dehydrogenase enzyme from rainbow trout (Oncorhynchus mykiss) liver and investigation of the effects of some metal ions on enzyme activity, Tox. Ind. Healt. 31 (2015) 403-411.
  • [56]. Temel Y., Bozkuş T., Karagözoğlu Y., Çiftci M., Glutatyon redüktaz (GR) enziminin japon bıldırcın (Coturnix coturnix japanica) eritrositlerinden saflaştırılması ve karakterizasyonu, Igdır Univ. J. Ins. Sci. Tech. 7 (2017) 143-150.
  • [57]. Kirici M., Atamanalp M., Kirici M., Beydemir Ş., In vitro effects of some metal ions on glutathione reductase in the gills and liver of Capoeta trutta, Reg. Mech. Biosys. 8 (2017) 66-70.
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Bazı Metal İyonlarının Japon Bıldırcın (Coturnix coturnix japonica) Karaciğer Glutatyon Redüktaz Enzimi Aktivitesi Üzerine İnhibisyon Etkilerinin Araştırılması

Year 2018, Volume: 39 Issue: 3, 679 - 687, 30.09.2018

Yusuf Temel , Sarkat Salim Mohammed Taher Mohammad Ahmad Hamza İbrahim Hamdi Shafeeq Ümit Muhammet Koçyiğit , Mehmet Çiftçi

https://doi.org/10.17776/csj.414680
Cited By: 5

Abstract

Bu çalışmada, bazı ağır metal iyonlarının
metabolizmada önemli fonksiyonlara sahip olan glutatyon reduktaz (GR) enziminin
aktivitesi üzerine inhibisyon etkileri araştırılmıştır. Bu amaçla, GR enzimi
bıldırcın karaciğerinden amonyum sülfat çöktürmesi ve 2ʹ, 5ʹ-ADP Sepharose 4B
afinite kromatografisi kullanılarak 19.33 EU/mg spesifik aktivite ile % 14.06
verimle 128.8 kat saflaştırılmıştır. GR enziminin saflığını kontrolü için,
sodyum dodesil sülfat poliakrilamid jel elektroforezi (SDS-PAGE) yapıldı ve
jelde tek bant gözlendi. GR enziminin aktivitesi, Carlberg ve Mannervik
yöntemine göre 340 nm'de spektrofotometrik olarak ölçüldü. Daha sonra, GR
enziminin aktivitesi üzerine farklı ağır metal iyonlarının (Co 2+,
Zn 2+, Pb 2+, Fe 2+, Cd 2+,     Al 3+
ve Fe 3+) inhibisyon etkileri in vitro koşullarda araştırıldı.
Bıldırcın karaciğer dokusundan saflaştırılan GR enzim aktivitesinin % 50'sinin
in vitro koşullarda inhibe edildiği ağır metal konsantrasyonları (IC50)
değerleri belirlendi. Son olarak, bu metal iyonları için Ki değerleri
Lineweaver-Burk grafiğinden hesaplandı.

Keywords

Glutatyon Redüktaz Enzim Saflaştırma İnhibisyon Bıldırcın Karaciğer

References

  • [1]. Veine D.M., Arscott L.D., Williams C.H., Redox potentials for yeast, Escherichia coli and human glutathione reductase relative to the NAD +/NADH redox couple: enzyme forms active in catalysis, Biochem. 37 (1998) 15575-15582.
  • [2]. Wong K.K., Vanoni M.A., Blanchard J.S., Glutathione reductase: solvent equilibrium and kinetic isotope effects, Biochem. 28 (1989) 3586-3590.
  • [3]. Bauer H., Fritz-Wolf K., Winzer A., Kuhner S., Little S., Yardley V., Vezin H., Palfey B., Schirmer R.H., Davioud-Charvet E., A fluoro analogue of the menadione derivative 6-[2`-(3`-methyl) -1`,4`-napht- hoquinolyl] hexanoic acid is a suicide substrate of glutathione reductase. crystal structure of the alkylated human enzyme, J. Am. Chem. Soc. 128 (2006) 10784-10794.
  • [4]. Yawata Y. and Tanaka K.R., Regulatory mechanism activity, Blood. 43 (1974) 99-110.
  • [5]. Tandogan B., Ulusu N.N., Kinetic mechanism and molecular properties of glutathione reductase, Plant Phsy. 31 (2006) 230-237.
  • [6]. Chang J.C., Hoeven V., Haddox C.H., Glutathione reductase in the red blood cells, An. Clin. Lab. Sci. 8 (1978) 23–29.
  • [7]. Garcia-Leiro A., Cerdan M.E., Gonzalez-Siso M.I., Characterization of chromosomal integration sites for heterologous gene expression in saccharomyces cerevisiae, Yeast. 26 (2009) 545–551.
  • [8]. Adem S. and Ciftci M., Purification and characterization of glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and glutathione reductase fromrat heart and inhibition effects of furosemide, digoxin, and dopamine on the enzymes activities, J. Biochem. Mol. Tox. 28 (2016) 246-255.
  • [9]. Yong Z., Teresa S., Wei C., Xiuqing W., Duane M., Yueshan H., Xiangming G., Effects of glutathione reductase inhibition on cellular thiol redox state and related systems, Arch. Biochem. Biophy. 485 (2009) 56-62.
  • [10]. Temel Y., Küfrevioğlu Ö.İ., Çiftci M., Investigation of the effects of purification and characterization of turkey (Meleagris gallopavo) liver mitochondrial thioredoxin reductase enzyme and some metal ions on enzyme activity, Turk. J. Chem. 41 (2017) 48-60.
  • [11]. Temel Y. and Kocyigit U.M., Purification of glucose-6-phosphate dehydrogenase from rat (Rattus norvegicus) erythrocytes and inhibition effects of some metal ions on enzyme activity, J. Biochem. Mol. Tox. 31 (2017) e21927.
  • [12]. Temel Y., Bengü A.Ş., Akkoyun H.T., Akkoyun M.B., Çiftci M., Effect of astaxanthin and aluminum chloride on erythrocyte G6PD and 6PGD enzyme activities in vivo and on erythrocyte G6PD in vitro in rats, J. Biochem. Mol. Tox. 31 (2017) e21954. [13]. Kocyigit U.M., Aslan O.N., Gulcin I., Temel Y., Ceylan M., Synthesis and Carbonic Anhydrase Inhibition of Novel 2-(4-(Aryl)thiazole-2-yl)-3a,4,7,7a-tetrahydro -1H-4,7-methanoisoindole 1,3 (2H) - dione Derivatives, Arch. Pharm. 349 (2016) 955-963.
  • [14]. Ceylan M., Kocyigit U.M., Usta N.C., Gürbüzlü B., Temel Y., Alwasel S.H., Gulcin I., Synthesis, carbonic anhydrase I and II iso enzymes inhibition properties, and antibacterial activities of novel tetralone-based 1,4-benzothiazepine deriva tives, J. Biochem. Mol. Tox. 31 (2017) e21872 .
  • [15]. Bayındır S., Ayna A., Temel Y., Çiftci M., The synthesis of new oxindoles as analogs of natural product 3,3'-bis(indolyl)oxindole and in vitro evaluation for enzyme activity of G6PD and 6PGD, Turk. J. Chem. 42 (2018) 332- 345.
  • [16]. Jan A.T, Azam M., Siddiqui K., Ali A., Choi I., Haq Q.M.R., Heavy Metals and Human Health: Mechanistic Insight into Toxicity and Counter Defense System of Antioxidants, Int. J. Mol. Sci. 16 (2015) 29592–29630.
  • [17]. Gutteridge J.M., Lipid peroxidation and antioxidants as biomarkers of tissue damage, Clin. Chem. 41 (1995) 1819-28.
  • [18]. Federico M.R., Toxicity of Glutathione-Binding Metals, A Rev. Targ. Mech. Tox. 3 (2015) 20-62.
  • [19]. Valko M., Morris H., Cronin M.T., Metals, toxicity and oxidative stress, Cur. Med. Chem. 12 (2005) 1161-1208.
  • [20]. Khalid R., Studies on free radicals, antioxidants, and co-factors, Clin. Inter. Ag. 2 (2007) 219-236.
  • [21]. Hubrecht R., Kirkwood J., The UFAW Handbook on the Care and Management of Laboratory and Other Research Animals. John Wiley & Sons. (2010). 655-674.
  • [22]. Carlberg I. and Mannervik B., Purification and characterization of glutathione reductase from calf liver. an improved procedure for affinity chromatography on 2′,5′-ADP-Sepharose-4B, Anal. Biochem. 536 (1981) 531-36.
  • [23]. Latta K. and Augusteyn R.C., The purification and properties of human reductase lens glutathione, Exp. Eye Res. 39 (1984) 343–54.
  • [24]. Lopez-Barea J. and Lee C.Y., Mouse liver glutathione reductase, Europ. J. Biochem. 499 (1979) 487-99.
  • [25]. Madamanchi N.R., Anderson J.V., Alscher R.G., Cramer C.L., Hess C.L., Purification of multiple forms of glutathione reductase from pea (pisum sativum l) seedlings and enzyme levels in ozone-fumigated pea leaves, Plant Phys. 100 (1992) 138-45.
  • [26]. Boese M., Keese M.A., Becker K., Busse R., Mulsch A., Inhibition of glutathione reductase by dinitrosyl-iron-dithiolate complex, J. Biol. Chem. 272 (1997) 21767–2173.
  • [27]. Elliott A.J., Scheiber S.A., Thomas C., Pardini R.S., Inhibition of glutathione reductase by flavonoids. a structure-activity study, Biochem. Pharm. 44 (1992) 1603–1608.
  • [28]. Erat M. and Ciftci M., Effect of melatonin on enzyme activities of glutathione reductase from human erythrocytes in vitro and from rat erythrocytes in vivo, Europ. J. Pharm. 537 (2006) 59–63.
  • [29]. Jervell J., and Vallance-Owen J., Inhibition of glutathione reductase in diabetics and non-diabetics, Diabet. 3 (1967) 353-354.
  • [30]. Ghosh S.K., Ghosh S., Gachhui R., Mandal A., Mercury and organomercurial resistance in Rhodotorula rubra: Activation of glutathione reductase, Bull. Env. Contam. Tox. 77 (2006): 351-358.
  • [31]. Erat M., Ciftci M., Gumustekin K., Gül M., Effects of nicotine and vitamin E on glutathione reductase activity in some rat tissues in vivo and in vitro, Europ. J. Pharm. 554 (2007) 92-97.
  • [32]. Ono S. and Hirano H., FAD-induced in vitro activation of glutathione reductase in the lens of B2 deficient rats. Curr. Eye Res. 3 (1984) 663-665.
  • [33]. Palmer E.J., MacManus J.P., Mutus B., Inhibition of glutathione reductase by oncomodulin, Arch. Biochem. Biophy. 277 (1990) 149-154.
  • [34]. Rafter G.W., Copper inhibition of glutathione reductase and its reversal with gold thiolates, thiol, and disulfide compounds, Biochem. Med. 27 (1982) 381-391.
  • [35]. Sentürk M., Talaz O., Ekinci D., Cavdar H., Küfrevioğlu O.I. In vitro inhibition of human erythrocyte glutathione reductase by some new organic nitrates, Bioorg. Med. Chem. Let. 19 (2009) 3661-3663.
  • [36]. Stýblo M. and David J.T., In vitro inhibition of glutathione reductase by arseno triglutathione, Biochem. Pharm. 49 (1995) 971-977.
  • [37]. Ulusu N., Acan N., Turan B., Tezcan E., Inhibition of glutathione reductase by cadmium ion in some rabbit tissues and the protective role of dietary selenium, Biol. Trace El. Res. 91 (2003) 151-156.
  • [38]. Zhang K., Yang E.B., Tang W.Y., Wong K.P., Mack P., Inhibition of glutathione reductase by plant polyphenols, Biochem. Pharm. 54 (1997) 1047-1053.
  • [39]. Trang L.N., Kuldeep K.B., Anthony C., Purification of glutathione reductase from gerbil liver in two steps, Anal. Biochem. 133 (1983) 94-99.
  • [40]. Boggaram V., Brobjer T., Larson K., Mannervik B., Purification of glutathione reductase from porcine erythrocytes by the use of affinity chromatography on 2′, 5′-ADP-Sepharose 4B and crystallization of the enzyme, Anal. Biochem. 98 (1979) 335-340.
  • [41]. Erat M., and Ciftci M., In vitro effects of some antibiotics on glutathione reductase from sheep liver, J. Enz. Inh. Med. Chem. 18 (2003) 545-550.
  • [42]. Taşer P. and Ciftci M., Purification and characterization of glutathione reductase from turkey liver, Turk. J. Vet. Ani. Sci. 36 (2012) 546-553.
  • [43]. Carlberg I. and Mannervik B., Glutathione reductase, Meth. Enz. 113 (1985) 484-490.
  • [44]. Bradford M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
  • [45]. Laemmli, U.K., Most commonly used discontinuous buffer system for SDS electrophoresis, Nat. 227 (1970) 680-686.
  • [46]. Lineweaver H. and Burk D., The determination of enzyme dissociation constants, J. Am. Chem. Soc. 56 (1934) 658-666.
  • [47]. Pradedova E.V., Isheeva O.D., Salyaev R.K., Classification of the antioxidant defense system as the ground for reasonable organization of experimental studies of the oxidative stress in plants, Rus. J. Plant Phys. 58 (2011) 210-217.
  • [48]. Hakiman M. and Maziah M., Non enzymatic and enzymatic antioxidant activities in aqueous extract of different ficus deltoidea accessions, J. Med. Plants Res. 3 (2009) 120-131.
  • [49]. Vaisi-Raygani A., Rahimi Z., Zahraie M., Noroozian M. Poutrmotabbed A., Iran. J. Med. Sci. 45 (2007) 271–76.
  • [50]. Coban T.A., Senturk M., Ciftci M., Kufrevioglu O.I., Effects of some metal ions on human erythrocyte glutathione reductase: an in vitro study, Prot. Pept. Let. 14 (2007) 1027-1030.
  • [51]. Coban T. A., Beydemir S., Gülcin I., Ekinci D., Innocenti A., Vullo D., Supuran C.T., Sildenafil is a strong activator of mammalian carbonic anhydrase isoforms I–XIV., Bioorg. Med. Chem. 17 (2009) 5791-5795.
  • [52]. Ekinci D. and Beydemir S., Purification of PON1 from human serum and assessment of enzyme kinetics against metal toxicity, Biol. Trace El. Res. 135 (2010) 112-120.
  • [53]. Ekinci D., Ceyhun S.B., Sentürk M., Erdem D., Küfrevioğlu O.İ., Supuran C.T., Characterization and anions inhibition studies of an α-carbonic anhydrase from the teleost fish Dicentrarchus labrax, Bioorg. Med. Chem. 19 (2011) 744-748.
  • [54]. Li D., Yang M.S., Lin T., Zheng W., Qu J.Y., Study of cadmium-induced cytotoxicity using two-photon excitation endogenous fluorescence microscopy, J. Biomed. Opt. 14 (2009) 054028.
  • [55]. Comakli V., Akkemik E., Ciftci M., Kufrevioglu O.I., Purification and characterization of glucose 6-phosphate dehydrogenase enzyme from rainbow trout (Oncorhynchus mykiss) liver and investigation of the effects of some metal ions on enzyme activity, Tox. Ind. Healt. 31 (2015) 403-411.
  • [56]. Temel Y., Bozkuş T., Karagözoğlu Y., Çiftci M., Glutatyon redüktaz (GR) enziminin japon bıldırcın (Coturnix coturnix japanica) eritrositlerinden saflaştırılması ve karakterizasyonu, Igdır Univ. J. Ins. Sci. Tech. 7 (2017) 143-150.
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There are 57 citations in total.

Details

Primary Language English
Journal Section Natural Sciences
Authors

Yusuf Temel

Sarkat Salim Mohammed Taher

Mohammad Ahmad Hamza

İbrahim Hamdi Shafeeq

Ümit Muhammet Koçyiğit

Mehmet Çiftçi

Publication Date September 30, 2018
Submission Date April 12, 2018
Acceptance Date August 27, 2018
Published in Issue Year 2018Volume: 39 Issue: 3

Cite

APA Temel, Y., Taher, S. S. M., Hamza, M. A., Shafeeq, İ. H., et al. (2018). Investigation of the Inhibition Effects of Some Metal Ions on Glutathione Reductase Enzyme From Japanese Quail (Coturnix coturnix japonica) Liver. Cumhuriyet Science Journal, 39(3), 679-687. https://doi.org/10.17776/csj.414680

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