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Bazı metal iyonlarının tavuk böbreğinden saflaştırılan glutatyon redüktaz enzimi üzerine in vitro etkilerinin araştırılması

Year 2017, Volume: 6 Issue: 1, 24 - 30, 05.10.2017

Abstract

Glutayon redüktaz enzimi tavuk böbreğinden
saflaştırıldı ve bazı metal iyonlarının bu enzim aktivitesi üzerine in vitro
etkileri araştırıldı. Saflaştırma prosedürü üç basamaktan oluştu; homojenatın
hazırlanması, amonyum sülfat çöktürmesi ve affinite kromatografisi. Bu üç
basamak sonucunda 8,595 EÜ/mg protein spesifik aktivitesine sahip enzim ~ % 57
verimle 369 kat saflaştırıldı. Enzimin saflık kontrolü sodyum dodesil
sülfat-poliakrilamid jel elektroforezi (SDS-PAGE) ile yapıldı ve bazı metal
iyonlarının (Ni+2, Zn+2, Pb+2, Hg+2,
Ag+ and Al+3) glutatyon redüktaz enzimi üzerindeki
inhibisyon etkisi araştırıldı. Metal iyonları için Ki ve IC50
değerleri
Lineweaver-Burk
ve % vs [I] aktivite grafikleriyle belirlendi.
Ni+2,  Hg+2
ve Ag+ yarışmasız inhibisyon gösterirken, Zn+2 ve Pb+2
yarı yarışmalı inhibisyon gösterdi. Diğer metal iyonlarının aksine Al+3
enzim üzerinde aktivatör etkisi gösterdi.




References

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  • [3] Wu G., Fang Y.Z, Yang S., Lupton J. R., Turner N.D., Glutathione Metabolism and Its Implications for Health. Journal of Nutrition, 134, 489-492, 2004.
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  • [5] Worhingyon D. J., Rosemeyer M. A., Glutathione reductase from human erythrocytes. Molecular weight, subunit composition and aggregation properties. E. J.Biochem., 15, 60(2), 459-66, 1976.
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  • [8] Şentürk M., Gülçin İ., Çiftçi M., Küfrevioğlu Ö.İ., Dantrolene inhibits human erythrocyte glutathione reductase. Biol. Pharm. Bull., 31(11), 2036— 2039, 2008.
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Year 2017, Volume: 6 Issue: 1, 24 - 30, 05.10.2017

Abstract

References

  • [1] Müler F., Chemistry & Biochemisry of Flavoenzymes; Williams C.H., Ed.; CRC Pres: Boca Raton, Florida, 121-211, 1992.
  • [2] Gül M., Kutay F.Z., Temocin S., Hanninen O., Cellular and clinical implications of glutathione. Indian J. Exp.Biol., 38, 625-634, 2000.
  • [3] Wu G., Fang Y.Z, Yang S., Lupton J. R., Turner N.D., Glutathione Metabolism and Its Implications for Health. Journal of Nutrition, 134, 489-492, 2004.
  • [4] Townsend D.M., Tew K.D., Tapiero H., The importance of glutathione in human disease. Biomed Pharmacother. 57(3-4), 145-55, 2003.
  • [5] Worhingyon D. J., Rosemeyer M. A., Glutathione reductase from human erythrocytes. Molecular weight, subunit composition and aggregation properties. E. J.Biochem., 15, 60(2), 459-66, 1976.
  • [6] Erat M., Purification of glucose 6-phosphate dehydrogenase and glutathione reductase enzymes using 2,5 -ADP Sepharose 4B affinity column material in single chromatographic step. Protein Expr Purif., 34, 257–260,2004. [7] Erat M., Çiftçi M., Effect of melatonin on enzyme activities of glutathione reductase from human erythrocytes in vitro and from rat erythrocytes in vivo. European Journal of Pharmacology, 537, 59–63, 2006.
  • [8] Şentürk M., Gülçin İ., Çiftçi M., Küfrevioğlu Ö.İ., Dantrolene inhibits human erythrocyte glutathione reductase. Biol. Pharm. Bull., 31(11), 2036— 2039, 2008.
  • [9] Akkemik E., Şentürk M., Özgeriş F.B., Taşer P., Çiftçi M., In vitro effects of some drugs on human erythrocyte glutathione reductase. Turk J Med Sci, 41 (2), 235-241, 2011.
  • [10] Le Trang N., Bhargava K.K., Cerami A., Purification of glutathione reductase from gerbil liver in two steps. Anal. Biochem., 133, 94–99, 1983.
  • [11] Ereser B.T., Sığır Böbrek Korteksinden Glutatyon Redüktazın Saflaştırılması ve Bazı Özelliklerinin Saptanması. Doktora Tezi, Hacettepe Üniversitesi Sağlık Bilimleri Enstitüsü, Ankara, 2010.
  • [12] Erat M., Şakiroğlu H., Çiftçi M., Effects of some antibiotics on glutathione reductase from bovine erythrocytes. Vet. Med. - Czech, 48 (11), 305–312, 2003.
  • [13] Ulusu N.N., Tandoğan B., Purification and kinetic properties of glutathione reductase from bovine liver. Mol. Cell. Biochem., 303, 45–51, 2007.
  • [14] Taşer P., Çiftçi M., Purification and characterization of glutathione reductase from turkey liver. Turk. J. Vet. Anim. Sci., 36(5), 546-553, 2012.
  • [15] Açan N.L., Tezcan E.F., Sheep brain glutathione reductase: purification and general properties, FEBS Lett, 250 (1), 72-74, 1989.
  • [16] Boggaram V., Brobjer K.L., Mannervik B., Purification of glutathione reductase from porcine erytrocytes by the use of affinity chromatography on 2’,5’-ADP-Sepharose 4B and crisitalization of the enzyme. Analytical Biochemistry, 98, 335-340, 1979.
  • [17] Can B., Glutatyon Redüktaz Enziminin Sıçan Böbreğinden Saflaştırılması, Substrat ve İnhibitör Kinetiğinin İncelenmesi. Yüksek Lisans Tezi, Hacettepe Üniversitesi, Sağlık Bilimleri Enstitüsü, Ankara, 2010.
  • [18] Carlberg C., Mannervik B., Glutathione reductase assays. Academic Pres, Orlando, FL.Methods in Enzymology, 113, 484-495, 1985.
  • [19] Adem Ş., Çiftçi M., Purification of rat kidney glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and glutathione reductase enzymes using 2’,5’-ADP Sepharose 4B affinity in a single chromatography step. Protein Expression and Purification, 81, 1–4, 2012.
  • [20] Erat M., Purification of 6-phosphogluconate dehydrogenase from chicken liver and investigation of some kinetic properties. Preparative Biochemistry and Biotechnology, 35, 53-69, 2005.
  • [21] Asnis R.E., A glutathione reductase from Escherichia coli. J. Biol. Chem., 213(1), 77-85, 1955.
  • [22] McCallum M.J., Barrett J., Purification and properties of glutathione reductase from the cestode Moniezia expanse. Int. J. Biochem. Cell. Biol., 27,393-401, 1995.
  • [23] Yadav S.S., Srikanth E., Singh N., Rathaur S., Identification of GR and TrxR systems in Setaria cervi: Purification and characterization of glutathione reductase. Parasitology International, 62, 193–198, 2013.
  • [24] Patel M.P., Marcinkeviciene, J., Blanchard J.S., Enterococus faecalis glutathione reductase: Purification, characterization and expression under normal and hyperbaric O2 conditions. FEMS Microbiology Letters, 166, 155-163, 1998.
  • [25] Libreros-Minotta C.A., Pardo J.P., Mendoza-Hernandez G., Rendon J.L., Purification and characterization of glutathione reductase from Rhodospirillum rubrum. Arch. Biochem. Biophys., 298, 247–253, 1992.
  • [26] Jiang F., Hellmans U., Stroga E., Bergman B., Mannervik B., Cloning, sequencing and regulation of the glutathione reductase gene from the Cyanobacterium anabaena PCC 7120. The Journal of Biological Chemistry, 270 (39), 22882-22889, 1995.
  • [27] Arias D.G., Marquez V.E., Beccaria AJ., Guerrero S.E., Iglesias A.A., Purification and characterization of a glutathione reductase from phaeodactylum tricornutum. Protist, 161, 91–101, 2010.
  • [28] Arscott L.D., Veine D.M., Williams C.H., Jr. Mixed disulfide with glutathione as an intermediate in the reaction catalyzed by glutathione reductase from yeast and as a major form of the enzyme in the cell. Biochemistry. 39(16), 4711-21, 2000.
  • [29] Lamotte F., Vianey-Liuaud N., Duviau M.P., Korehel K., Glutathione reductase in wheat grain. 1. Isolation and characterization. J. Agric. Food Chem., 48, 4978-4983, 2000.
  • [30] Mahan J.R., Burke J.J., Purification and characterization of glutathione reductase from corn mesophyll chloroplast. Physiol. Plant., 71, 352-358, 1987.
  • [31] Mullineaux P., Enard C., Hellens R, Creissen G., Characterization of glutathione reductase gene and its genetic locus from pea (Pisum sativum L.). Planta, 200, 186-194, 1996.
  • [32] Molavi B., Mehta J.L., Oxidative stress in cardiovascular disease: molecular basis of its deleterious effects, its detection, and therapeutic considerations. Curr Opin Cardiol., 19(5), 488-93, 2004.
  • [33] Valko M., Morris H., Cronin M.T., Metals, toxicity and oxidative stress. Curr. Med. Chem. 12(10), 1161-208. [34] Garner, L.A., 2004. Contact dermatitis to metals. Dermatol. Ther., 17, 321–327,2005.
  • [35] Costa M., Davidson T.L., Chen H., Ke Q., Zhang P., Yan Y., Huang C., Kluz T., Nickel carcinogenesis: epigenetics and hypoxia signaling. Mutat. Res., 592, 79-88, 2005.
  • [36] Athar M., Hasan S.K., Srivastava R.C., Evidence for the involvement of hydroxyl radicals in nickel mediated enhancement of lipid peroxidation: implications for nickel carcinogenesis. Biochem. Biophys. Res. Commun. 147, 1276–1281, 1987.
  • [37] Misra M., Rodriguez R.E., Kasprzak K.S., Nickel induced lipid peroxidation in the rat: correlation with nickel effect on antioxidant defense systems. Toxicology., 64, 1–17, 1990.
  • [38] Shainkin-Kestenbaum R., Caruso C., Berlyne G.M., Effect of nickel on oxygen free radical metabolism. Inhibition of superoxide dismutase and enhancement of hydroxydopamine autoxidation. Biol. Trace. Elem. Res., 28, 213-21,1991.
  • [39] Kalliri E., Grzyska P.K., Hausinger R.P., Kinetic and spectroscopic investigation of CoII, NiII, and N-oxalylglycine inhibition of the FeII/alphaketoglutarate dioxygenase, TauD. Biochem. Biophys. Res. Commun., 338, 191-7, 2005.
  • [40] Romero C.S., Olmo R., Teijon C., Blanco M.D., Teijon J.M., Romero A.,. Structural and functional implications of the hexokinase-nickel interaction. J. Inorg. Biochem., 99, 2395-402, 2005.
  • [41] Mahmoudi A., Nazari K., Mohammadian N., Moosavi-Movahedi A.A., Effect of Mn2+, Co2+, Ni2+, and Cu2+ on horseradish peroxidase: activation, inhibition, and denaturation studies Appl. Biochem. Biotechnol., 104, 81-94, 2003.
  • [42] Wu W., Graves L.M., Jaspers I., Devlin R.B., Reed W., Samet JM., Activation of the EGF receptor signaling pathway in human airway epithelial cells exposed to metals. Am. J. Physiol., 277, 924-31, 1999.
  • [43] Haase H., Maret W., Intracellular zinc fluctuations modulate protein tyrosine phosphatase activity in insulin/insulin-like growth factor-1 signaling. Exp. Cell Res., 291, 289–298, 2003.
  • [44] Perry D.K., Smyth M.J., Stennicke H.R., Salvesen G.S., Duriez P., Poirier G.G., Hannun Y.A., Zinc is a potent inhibitor of the apoptotic protease, caspase-3. A novel target for zinc in the inhibition of apoptosis. J. Biol. Chem., 272, 18530-3, 1997.
  • [45] Walther U.I., Wilhelm B., Walther S.C., Muckter H., Forth W., Effect of zinc chloride on GSH synthesis rates in various lung cell lines. In Vitr Mol Toxicol., 13(2), 145-52, 2000.
  • [46] Mize C.E., Langdon R.G., Hepatic glutathione reductase. I. Purification and general kinetic properties. J. Biol. Chem,. 237, 1589-95, 1962.
  • [47] Bishop G.M., Dringen R., Robinson S.R., Zinc stimulates the production of toxic reactive oxygen species (ROS) and inhibits glutathione reductase in astrocytes. Free Radic. Biol. Med., 42, 1222-30, 2007.
  • [48] Bradford M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analitical Biochemistry, 72, 248, 1976.
  • [49] Ninfali P., Orsenigo T., Barociani L., Rapa S., Rapid purification of glucose 6-phosphate dehydrogenase from mammal’s erythrocytes. Preparative Biochemistry, 20,297-309, 1990.
  • [50] Morelli A., Benatti U., Gaetani G.F., De Flora A., Biochemical mechanisms of glucose 6-phosphate dehydrogenase deficiency. Proc Natl Acad Sci., 75, 4-9, 1978.
  • [51] Laemmli DK, Clevage of structual proteins during in assembly of the head of bacteriophage. T Nature, 227, 680-683, 1970.
  • [52] Karplus PA, Krauth-Siegel RL, Schirmer RH, and Schulz GE., Inhibition of human glutathione reductase by the nitrosourea drugs 1,3-bis(2-chloroethyl)-l-nitrosourea and 1-(2-chloroethyl)-3-(2-hydroxyethyl)-l-nitrosourea. Eur J Biochem., 171,193-198, 1988.
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There are 65 citations in total.

Details

Journal Section Articles
Authors

Yusuf Karagözoğlu

Mehmet Çiftci

Publication Date October 5, 2017
Published in Issue Year 2017 Volume: 6 Issue: 1

Cite

APA Karagözoğlu, Y., & Çiftci, M. (2017). Bazı metal iyonlarının tavuk böbreğinden saflaştırılan glutatyon redüktaz enzimi üzerine in vitro etkilerinin araştırılması. Türk Doğa Ve Fen Dergisi, 6(1), 24-30.
AMA Karagözoğlu Y, Çiftci M. Bazı metal iyonlarının tavuk böbreğinden saflaştırılan glutatyon redüktaz enzimi üzerine in vitro etkilerinin araştırılması. TJNS. October 2017;6(1):24-30.
Chicago Karagözoğlu, Yusuf, and Mehmet Çiftci. “Bazı Metal iyonlarının Tavuk böbreğinden saflaştırılan Glutatyon redüktaz Enzimi üzerine in Vitro Etkilerinin araştırılması”. Türk Doğa Ve Fen Dergisi 6, no. 1 (October 2017): 24-30.
EndNote Karagözoğlu Y, Çiftci M (October 1, 2017) Bazı metal iyonlarının tavuk böbreğinden saflaştırılan glutatyon redüktaz enzimi üzerine in vitro etkilerinin araştırılması. Türk Doğa ve Fen Dergisi 6 1 24–30.
IEEE Y. Karagözoğlu and M. Çiftci, “Bazı metal iyonlarının tavuk böbreğinden saflaştırılan glutatyon redüktaz enzimi üzerine in vitro etkilerinin araştırılması”, TJNS, vol. 6, no. 1, pp. 24–30, 2017.
ISNAD Karagözoğlu, Yusuf - Çiftci, Mehmet. “Bazı Metal iyonlarının Tavuk böbreğinden saflaştırılan Glutatyon redüktaz Enzimi üzerine in Vitro Etkilerinin araştırılması”. Türk Doğa ve Fen Dergisi 6/1 (October 2017), 24-30.
JAMA Karagözoğlu Y, Çiftci M. Bazı metal iyonlarının tavuk böbreğinden saflaştırılan glutatyon redüktaz enzimi üzerine in vitro etkilerinin araştırılması. TJNS. 2017;6:24–30.
MLA Karagözoğlu, Yusuf and Mehmet Çiftci. “Bazı Metal iyonlarının Tavuk böbreğinden saflaştırılan Glutatyon redüktaz Enzimi üzerine in Vitro Etkilerinin araştırılması”. Türk Doğa Ve Fen Dergisi, vol. 6, no. 1, 2017, pp. 24-30.
Vancouver Karagözoğlu Y, Çiftci M. Bazı metal iyonlarının tavuk böbreğinden saflaştırılan glutatyon redüktaz enzimi üzerine in vitro etkilerinin araştırılması. TJNS. 2017;6(1):24-30.

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