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

Barzan Mirza Ahmed; Yusuf Temel; Mehmet Çiftci

doi:10.17776/csj.496122

Research Article

Year 2019, Volume: 40 Issue: 4, 802 - 812, 31.12.2019

Barzan Mirza Ahmed Yusuf Temel , Mehmet Çiftci

https://doi.org/10.17776/csj.496122

Cited By: 5

Abstract

References

[1] Booth J., Boyland E., Sims A.P., An enzyme from rat liver catalysing conjugations with glutathione, Biochem. J., 79 (1961) 516-524.
[2] Sherratt P.H., Hayes J., Glutathione S-Transferases Enzyme System That Metabolise Drugs and Other Xenobiotics. Chichester, UK ., (2001) 1-578.
[3] Hayes J.D., Pulford D.J., The glutathione S-transferase supergene family: regulation of GST and the contribution of the lsoenzymes to cancer chemoprotection and drug resistance, part I. Critic. Rev. Biochem. Mol. Biol., 30 (1995) 445-520.
[4] George S.G., Enzymology and molecular biology of phase II xenobiotic-conjugating enzymes in fish, Aquatic Toxicol. (1994) 37-85.
[5] Mannervik B., Alin P., Guthenbergg C., Jensson H., Tahir M.K., Warholm M., Jornvall H., Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties, Proceed National Acad. Sci USA 82 (1985) 7202-206.
[6] Ketterer B., Meyer D.J, Taylor J.B., Pemble S., Coles B., Fraser G., GSTs and protection against oxidative stress. In Glutathione S.Transferase and Drug Resistance, Taylor Francis Bristol, 1990; pp 97-109.
[7] Benson A.M., Talalay P., Keen J.H., Jakoby W.B., Relationship between the soluble glutathione-dependent delta 5-3-ketosteroid isomerase and the glutathione S- transferases of the liver, Proceed National Acad. Sci., 74 (1977) 158-162.
[8] Yu S.J., Insect glutathione S-transferases, Zoological Studies, 35-1 (1996) 9-19.
[9] Cancado G.M., De Rosa V.E., Fernandez J.H., Maron L.G., Jorge R.A., Menossi M., Glutathione S-transferase and aluminum toxicity in maize, Functional Plant. Biol., 32 (2005) 1045–1055.
[10] Townsend D.M., Tew K.D., The role of glutathione-S-transferase in anti-cancer drug resistance, Oncogene 22 (2003) 7369-7375.
[11] Senjo M., Ishibashi T., Purification and characterization of glutathione S-transferase from rat brain cytosol identification of four isozymes and evidence for absence of the Ya subunit, Biomed. Res., 7 (1986) 19-26.
[12] Singh S.V., Leal T., Ansari G.A., Awasthi Y.C., Purification and characterization of glutathione S-transferases of human kidney, Biochem. J., 246 (1987) 179-186.
[13] Kwak S.J, Park S.C., Purification and Characterization of Glutathione S-transferase π from Human Placental Tissues, Seoul J. Med., 29 (1988) 107-118.
[14] Riol M.M., Valinas M.N., Fernandez M.G., Lopez M.P., Glutathione S-transferases from rainbow trout liver and freshly isolated hepatocytes: purification and haracterization, Comp. Biochem. Physiol Part C: Toxicol. Pharmacol., 128 (2001) 227-235.
[15] Huang Q., Liang L., Wei T., Zhang D., Zeng Q.Y., Purification and partial characterization of glutathione transferase from the teleost Monopterus albus. Comp Biochem Physiol Part C: Toxicol Pharmacol 147 (2008) 96-100. [16] Jassim H.A., Ameen F.Z., Al-Jumaily E.F.A., Isolation And Purification Of Glutathione S-Transferasefrom Rat Liver, J Al-Nahrain Univ. Sci., 12 (2009) 137-144.
[17] Akkemik E., Taser P., Bayindir A., Budak H., Ciftci M., Purification and characterization of glutathione S-transferase from turkey liver and inhibition effects of some metal ions on enzyme activity, Environ. Toxicol. Pharmacol. 34 (2012) 888-894.
[18] Aksoy M., Ozaslan M., Kufrevioglu O., Purification of glutathione S-transferase from Van Lake fish (Chalcalburnus tarichii Pallas) muscle and investigation of some metal ions effect on enzyme activity. J Enzyme Inhib. Med. Chem. 31 (2016) 546-550.
[19] Temel Y., Koçyigit U.M., Taysı M.Ş., Gökalp F., Gürdere M.B., Budak Y., Çiftci M., Purification of glutathione S‐transferase enzyme from quail liver tissue and inhibition effects of (3aR, 4S, 7R, 7aS)‐2‐(4‐((E)‐3‐(aryl) acryloyl) phenyl)‐3a, 4, 7, 7a‐tetrahydro‐1H‐4, 7‐methanoisoindole‐1, 3 (2H)‐dione derivatives on the enzyme activity, J. Biochem. Mol. Toxicol. 32 (2018) e22034.
[20] Krewski D., Yokel R.A., Nieboer E., Borchelt D., Cohen J., Harry J., Rondeau V., Human health risk assessment for aluminium, aluminium oxide, and aluminium hydroxide, J. Toxicol. Environ. Health Part B 10 (2007) 1-269.
[21] Kucuk M., Gulcin I., Purification and characterization of the carbonic anhydrase enzyme from Black Sea trout (Salmo trutta Labrax Coruhensis) kidney and inhibition effects of some metal ions on enzyme activity, Environ. Toxicol. Pharm. 44 (2016) 134-139.
[22] Verstraeten S.V., Aimo L., Oteiza P.I., Aluminium and lead: molecular mechanisms of brain toxicity, Arch. Toxicol., 82 (2008) 789-802.
[23] Ozaslan M.S., Ciftci M., Purification of glutathione S-transferase from Van Lake fish (Chalcalburnus tarichii Pallas) liver and investigation of some metal ions effect on enzyme activity. J. Enzyme İnhib. Med. Chem., 31 (2014) 546-550.
[24] Laemmli U.K., Cleavage of structural proteins during assembly of head of bacteriophage T4. Nature 227 (1970) 680–85.
[25] Dierickx P.J., Purification and characterization of glutathione S-transferase from the human hepatoma derived PLC/PRF/5 cell line, Biomed. Res., 10 (1989) 301-306.
[26] Ahmad R., Srivastava A. K., Walter R.D., Purification and biochemical characterization of cytosolic glutathione-S-transferase from filarial worms Setaria cervi, Comp. Biochem. Physiology Part B: Biochem. Mol. Biol., 151 (2008) 237-245.
[27] Fuerst E.P., Irzyk G.P., Miller K.D., Partial characterization of glutathione S-transferase isozymes induced by the herbicide safener benoxacor in maize, Plant Physiol. 102 (1993) 795-802.
[28] Gronwald J.W., Plaisance K.L., Isolation and Characterization of Glutathione S-Transferase Isozymes from Sorghum, Plant Physiol. 17-1(1998) 877-892.
[29] Gadagbui B.K., James M.O., Activities of affinity-isolated glutathione S-transferase (GST) from channel catfish whole intestine, Aquatic Toxicol., 49 (2000) 27-37.
[30] Hamed R.R., Maharem T.M., Abdel-Meguid N., Sabry G.M., Abdalla A.M., Guneidy R.A., Purification and biochemical characterization of glutathione S-transferase from Down syndrome and normal children erythrocytes: A comparative study, Res. Develop. disabilities 32 (2011) 1470-1482.
[31] Lebda M., Taha N., Noeman S., Korshom M., El-Wahab Mandour, A. Purification and Characterization of Glutathione-S-Transferase from Rat′ s Liver: Effect of Carbon Tetrachloride and Camel′ s Milk, J. Chromat. Separation Techniq, 3-4 (2012) 2-8.
[32] Habig W.H., Pabst M.J., Jakoby W.B., Glutathione S-transferases the first enzymatic step in mercapturic acid formation, J. Biol. Chem. 249 (1974) 7130-7139.
[33] Wingfield P., Protein precipitation using ammonium sulfate, Current Prot. Prot. Sci., 53 (2001) A- 3F.
[34] Bradford M.M., 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.
[35] Laemmli D.K., Cleavage of structural proteins during in assembly of the heat of bacteriophage T4. Nature London, 227 (1970) 680-685.
[36] Lineweaver H., Burk D., The determination of enzyme dissocation constants, J. Am. Chem. Soc., 56-3 (1934) 57-685.
[37] 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.
[38] 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 ntibacterial activities of novel tetralone-based 1,4-benzothiazepine deriva tives, J. Biochem. Mol. Tox. 31 (2017) e21872.
[39] 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.
[40] Bayindir S., Temel Y., Ayna A., Ciftci M., The synthesis of N‐benzoylindoles as inhibitors of rat erythrocyte glucose‐6‐phosphate dehydrogenase and 6‐phosphogluconate dehydrogenase, J. Biochem. Mol. Tox. 32 (2018) e22193.
[41] Temel Y., Taher S.S.M., Hamza M.A., Shafeeq I.H., Koçyiğit U.M., Çiftci M., Investigation of the Inhibition Effects of Some Metal Ions on Glutathione Reductase Enzyme From Japanese Quail (Coturnix coturnix japonica) Liver, Cumhuriyet Sci. J. 39 (2018) 3679-687.
[42] 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.
[43] 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.

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

Year 2019, Volume: 40 Issue: 4, 802 - 812, 31.12.2019

Barzan Mirza Ahmed Yusuf Temel , Mehmet Çiftci

https://doi.org/10.17776/csj.496122

Cited By: 5

Abstract

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. K_M and V_max
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 (Cu²⁺, Cd²⁺, Fe²⁺,
Fe³⁺ Zn²⁺, Ag⁺, Co²⁺, and Ti¹⁺)
were investigated on the GST enzyme activity in vitro.

Keywords

Quail, Heart, Glutathione S-transferase, Purification, Characterizations, , Metal Ions.

References

[1] Booth J., Boyland E., Sims A.P., An enzyme from rat liver catalysing conjugations with glutathione, Biochem. J., 79 (1961) 516-524.
[2] Sherratt P.H., Hayes J., Glutathione S-Transferases Enzyme System That Metabolise Drugs and Other Xenobiotics. Chichester, UK ., (2001) 1-578.
[3] Hayes J.D., Pulford D.J., The glutathione S-transferase supergene family: regulation of GST and the contribution of the lsoenzymes to cancer chemoprotection and drug resistance, part I. Critic. Rev. Biochem. Mol. Biol., 30 (1995) 445-520.
[4] George S.G., Enzymology and molecular biology of phase II xenobiotic-conjugating enzymes in fish, Aquatic Toxicol. (1994) 37-85.
[5] Mannervik B., Alin P., Guthenbergg C., Jensson H., Tahir M.K., Warholm M., Jornvall H., Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties, Proceed National Acad. Sci USA 82 (1985) 7202-206.
[6] Ketterer B., Meyer D.J, Taylor J.B., Pemble S., Coles B., Fraser G., GSTs and protection against oxidative stress. In Glutathione S.Transferase and Drug Resistance, Taylor Francis Bristol, 1990; pp 97-109.
[7] Benson A.M., Talalay P., Keen J.H., Jakoby W.B., Relationship between the soluble glutathione-dependent delta 5-3-ketosteroid isomerase and the glutathione S- transferases of the liver, Proceed National Acad. Sci., 74 (1977) 158-162.
[8] Yu S.J., Insect glutathione S-transferases, Zoological Studies, 35-1 (1996) 9-19.
[9] Cancado G.M., De Rosa V.E., Fernandez J.H., Maron L.G., Jorge R.A., Menossi M., Glutathione S-transferase and aluminum toxicity in maize, Functional Plant. Biol., 32 (2005) 1045–1055.
[10] Townsend D.M., Tew K.D., The role of glutathione-S-transferase in anti-cancer drug resistance, Oncogene 22 (2003) 7369-7375.
[11] Senjo M., Ishibashi T., Purification and characterization of glutathione S-transferase from rat brain cytosol identification of four isozymes and evidence for absence of the Ya subunit, Biomed. Res., 7 (1986) 19-26.
[12] Singh S.V., Leal T., Ansari G.A., Awasthi Y.C., Purification and characterization of glutathione S-transferases of human kidney, Biochem. J., 246 (1987) 179-186.
[13] Kwak S.J, Park S.C., Purification and Characterization of Glutathione S-transferase π from Human Placental Tissues, Seoul J. Med., 29 (1988) 107-118.
[14] Riol M.M., Valinas M.N., Fernandez M.G., Lopez M.P., Glutathione S-transferases from rainbow trout liver and freshly isolated hepatocytes: purification and haracterization, Comp. Biochem. Physiol Part C: Toxicol. Pharmacol., 128 (2001) 227-235.
[15] Huang Q., Liang L., Wei T., Zhang D., Zeng Q.Y., Purification and partial characterization of glutathione transferase from the teleost Monopterus albus. Comp Biochem Physiol Part C: Toxicol Pharmacol 147 (2008) 96-100. [16] Jassim H.A., Ameen F.Z., Al-Jumaily E.F.A., Isolation And Purification Of Glutathione S-Transferasefrom Rat Liver, J Al-Nahrain Univ. Sci., 12 (2009) 137-144.
[17] Akkemik E., Taser P., Bayindir A., Budak H., Ciftci M., Purification and characterization of glutathione S-transferase from turkey liver and inhibition effects of some metal ions on enzyme activity, Environ. Toxicol. Pharmacol. 34 (2012) 888-894.
[18] Aksoy M., Ozaslan M., Kufrevioglu O., Purification of glutathione S-transferase from Van Lake fish (Chalcalburnus tarichii Pallas) muscle and investigation of some metal ions effect on enzyme activity. J Enzyme Inhib. Med. Chem. 31 (2016) 546-550.
[19] Temel Y., Koçyigit U.M., Taysı M.Ş., Gökalp F., Gürdere M.B., Budak Y., Çiftci M., Purification of glutathione S‐transferase enzyme from quail liver tissue and inhibition effects of (3aR, 4S, 7R, 7aS)‐2‐(4‐((E)‐3‐(aryl) acryloyl) phenyl)‐3a, 4, 7, 7a‐tetrahydro‐1H‐4, 7‐methanoisoindole‐1, 3 (2H)‐dione derivatives on the enzyme activity, J. Biochem. Mol. Toxicol. 32 (2018) e22034.
[20] Krewski D., Yokel R.A., Nieboer E., Borchelt D., Cohen J., Harry J., Rondeau V., Human health risk assessment for aluminium, aluminium oxide, and aluminium hydroxide, J. Toxicol. Environ. Health Part B 10 (2007) 1-269.
[21] Kucuk M., Gulcin I., Purification and characterization of the carbonic anhydrase enzyme from Black Sea trout (Salmo trutta Labrax Coruhensis) kidney and inhibition effects of some metal ions on enzyme activity, Environ. Toxicol. Pharm. 44 (2016) 134-139.
[22] Verstraeten S.V., Aimo L., Oteiza P.I., Aluminium and lead: molecular mechanisms of brain toxicity, Arch. Toxicol., 82 (2008) 789-802.
[23] Ozaslan M.S., Ciftci M., Purification of glutathione S-transferase from Van Lake fish (Chalcalburnus tarichii Pallas) liver and investigation of some metal ions effect on enzyme activity. J. Enzyme İnhib. Med. Chem., 31 (2014) 546-550.
[24] Laemmli U.K., Cleavage of structural proteins during assembly of head of bacteriophage T4. Nature 227 (1970) 680–85.
[25] Dierickx P.J., Purification and characterization of glutathione S-transferase from the human hepatoma derived PLC/PRF/5 cell line, Biomed. Res., 10 (1989) 301-306.
[26] Ahmad R., Srivastava A. K., Walter R.D., Purification and biochemical characterization of cytosolic glutathione-S-transferase from filarial worms Setaria cervi, Comp. Biochem. Physiology Part B: Biochem. Mol. Biol., 151 (2008) 237-245.
[27] Fuerst E.P., Irzyk G.P., Miller K.D., Partial characterization of glutathione S-transferase isozymes induced by the herbicide safener benoxacor in maize, Plant Physiol. 102 (1993) 795-802.
[28] Gronwald J.W., Plaisance K.L., Isolation and Characterization of Glutathione S-Transferase Isozymes from Sorghum, Plant Physiol. 17-1(1998) 877-892.
[29] Gadagbui B.K., James M.O., Activities of affinity-isolated glutathione S-transferase (GST) from channel catfish whole intestine, Aquatic Toxicol., 49 (2000) 27-37.
[30] Hamed R.R., Maharem T.M., Abdel-Meguid N., Sabry G.M., Abdalla A.M., Guneidy R.A., Purification and biochemical characterization of glutathione S-transferase from Down syndrome and normal children erythrocytes: A comparative study, Res. Develop. disabilities 32 (2011) 1470-1482.
[31] Lebda M., Taha N., Noeman S., Korshom M., El-Wahab Mandour, A. Purification and Characterization of Glutathione-S-Transferase from Rat′ s Liver: Effect of Carbon Tetrachloride and Camel′ s Milk, J. Chromat. Separation Techniq, 3-4 (2012) 2-8.
[32] Habig W.H., Pabst M.J., Jakoby W.B., Glutathione S-transferases the first enzymatic step in mercapturic acid formation, J. Biol. Chem. 249 (1974) 7130-7139.
[33] Wingfield P., Protein precipitation using ammonium sulfate, Current Prot. Prot. Sci., 53 (2001) A- 3F.
[34] Bradford M.M., 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.
[35] Laemmli D.K., Cleavage of structural proteins during in assembly of the heat of bacteriophage T4. Nature London, 227 (1970) 680-685.
[36] Lineweaver H., Burk D., The determination of enzyme dissocation constants, J. Am. Chem. Soc., 56-3 (1934) 57-685.
[37] 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.
[38] 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 ntibacterial activities of novel tetralone-based 1,4-benzothiazepine deriva tives, J. Biochem. Mol. Tox. 31 (2017) e21872.
[39] 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.
[40] Bayindir S., Temel Y., Ayna A., Ciftci M., The synthesis of N‐benzoylindoles as inhibitors of rat erythrocyte glucose‐6‐phosphate dehydrogenase and 6‐phosphogluconate dehydrogenase, J. Biochem. Mol. Tox. 32 (2018) e22193.
[41] Temel Y., Taher S.S.M., Hamza M.A., Shafeeq I.H., Koçyiğit U.M., Çiftci M., Investigation of the Inhibition Effects of Some Metal Ions on Glutathione Reductase Enzyme From Japanese Quail (Coturnix coturnix japonica) Liver, Cumhuriyet Sci. J. 39 (2018) 3679-687.
[42] 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.
[43] 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.

There are 42 citations in total.

Details

Primary Language	English
Journal Section	Natural Sciences
Authors	Barzan Mirza Ahmed Yusuf Temel 0000-0001-8148-3718 Mehmet Çiftci
Publication Date	December 31, 2019
Submission Date	December 12, 2018
Acceptance Date	May 13, 2019
Published in Issue	Year 2019Volume: 40 Issue: 4

Cite

APA	Mirza Ahmed, B., Temel, Y., & Çiftci, M. (2019). Purification and characterization glutathione S-transferase enzyme from quail (Coturnix, coturnix japonica) heart and investigation the effect of some metal ions on enzyme activity. Cumhuriyet Science Journal, 40(4), 802-812. https://doi.org/10.17776/csj.496122

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Abstract

References

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

Abstract

Keywords

References

Details

Cite

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