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Glutatyon S-transferaz: Koyun Dalak Dokusundan Saflaştırılması ve Karakterizasyonu

Year 2022, Volume: 12 Issue: 4, 2352 - 2363, 01.12.2022
https://doi.org/10.21597/jist.1150868

Abstract

Bu çalışmada, hücre içi majör antioksidan sistem olan glutatyon antioksidan sisteminin önemli enzimlerinden glutatyon S-transferaz (GST; EC 2.5.1.18) sitozolik enzimi koyun dalak dokusundan homojenat hazırlanması, salting out (amonyum sülfat tuzu ile çöktürme yöntemi) ve afinite kromatografisi (glutatyon-agaroz) olmak üzere üç adımda 3.67 EÜ mg-1 protein değeri (spesifik aktivite) ve %3.73 verim ile 122.3 kat saflaştırıldı. Koyun dalak dokusundan saflaştırılan GST enziminin saflık derecesini belirlemek ve doğal alt birim molekül kütlelerinin tespitinde sodyum dodesil sülfat poliakrilamid jel elektroforez (SDS-PAGE) metodu kullanıldı. Koyun dalak dokusu GST enziminin alt birimlerine ait molekül kütlesi yaklaşık olarak 26.36 kDa hesaplandı. Koyun dalak dokusundan saflaştırılan GST enziminin karakterizasyonu için gerçekleştirilen çalışmalarda; optimum pH, K-fosfat tamponu pH=8.0, optimum aktivite gösterdiği iyonik şiddet, K-fosfat tampon çözeltisi 1.0 M, stabil pH, K-fosfat tampon çözeltisi pH = 7.0 ve optimum sıcaklığı 60 oC olarak bulundu. Koyun dalak dokusundan saflaştırılan GST enzimine ait KM ve Vmax değerlerini belirlemek için yapılan kinetik çalışmalarda Lineweaver-Burk grafiklerinden yararlanıldı. Enzimin substratları olan indirgenmiş glutatyon (GSH) ve 1-kloro-2,4-dinitrobenzen (CDNB) için yürütülen kinetik çalışmalarda; GSH için KM değeri 0.629 mM, Vmax değeri 0.056 EÜ mL-1; CDNB için KM değeri 0.321 mM, Vmax değeri 0.129 EÜ mL-1 olarak belirlendi.

References

  • AAdem S, Ciftci M. 2012. 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): 1–4.
  • Akkemik E, Şentürk M, Özgeriş FB, Taşer P, Çiftci M. 2011. In vitro eff ects of some drugs on human erythrocyte glutathione reductase 41(2): 235–241.
  • Akkemik E, Taser P, Bayindir A, Budak H, Ciftci M. 2012a. Purification and characterization of glutathione S-transferase from turkey liver and inhibition effects of. Environmental Toxicology and Pharmacology 34(3): 888–894.
  • Akkemik E, Taser P, Bayindir A, Budak H, Ciftci M. 2012b. Purification and characterization of glutathione S-transferase from turkey liver and inhibition effects of some metal ions on enzyme activity. Environmental Toxicology and Pharmacology 34(3): 888–894.
  • Aksoy M, Ozaslan MS, Kufrevioglu OI. 2016. Purification of glutathione S-transferase from Van Lake fish (Chalcalburnus tarichii Pallas) muscle and investigation of some metal ions effect on enzyme activity. Journal of Enzyme Inhibition and Medicinal Chemistry 31(4): 546–550.
  • Aybek H, Temel Y, Ahmed BM, Ağca CA, Çiftci M. 2020. Deciphering of The Effect of Chemotherapeutic Agents on Human Glutathione S-Transferase Enzyme and MCF-7 Cell Line. Protein and Peptide Letters 27(9): 888–894.
  • Balcı N, Türkan F, Şakiroğlu H, Aygün A, Şen F. 2019. Purification and characterization of glutathione S-transferase from blueberry fruits (Vaccinium arctostaphylos L.) and investigated of some pesticide inhibition effects on enzyme activity. Heliyon, 5(4): e01422.
  • Balcı N, Şakiroğlu H, Türkan F, Bursal E. 2021. In vitro and in silico enzyme inhibition effects of some metal ions and compounds on glutathione S-transferase enzyme purified from Vaccinium arctostapylous L. Journal of Biomolecular Structure and Dynamics, 1-7.
  • Balendiran GK, Dabur R, Fraser D. 2004. The role of glutathione in cancer. Cell Biochemistry and Function, 22(6): 343–352.
  • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical biochemistry 72(1-2): 248-254.
  • Çetin A, Bursal E, Türkan F. 2021. 2-methylindole analogs as cholinesterases and glutathione S-transferase inhibitors: Synthesis, biological evaluation, molecular docking, and pharmacokinetic studies. Arabian Journal of Chemistry, 14(12): 103449.
  • De Koning AJ, De Koning CB, De Koning PD. 2005. Antioxidants. Handbook of food science, Technology, and Engineering - 4 : 1653–1662.
  • Demirdag R, Yerlikaya E, Kufrevioglu O.I, Gundogdu C. 2013. Purification of glutathione S-transferase isoenzymes from tumour and nontumour human stomach and inhibitory effects of some heavy metals on enzymes activities. Journal of Enzyme Inhibition and Medicinal Chemistry, 28(5): 911-915.
  • Gülçin I. 2010. Antioxidant properties of resveratrol: A structure-activity insight. Innovative Food Science and Emerging Technologies, 11(1): 210–218.
  • Gülçin I. 2012. Antioxidant activity of food constituents: An overview. Archives of Toxicology, 86(3): 345–391.
  • Gülçin İ, Taslimi P, Aygün A, Sadeghian N, Bastem E, Kufrevioglu OI, Şen F. 2018. Antidiabetic and antiparasitic potentials: Inhibition effects of some natural antioxidant compounds on α-glycosidase, α-amylase and human glutathione S-transferase enzymes. International Journal of Biological Macromolecules, 119: 741–746.
  • Orhan H, Şahin G. 1995.Glutatyon S-Transferazların klinik ve toksikolojik önemi. Türkiye Klinikleri Tıp Bilimleri, 15: 303-15.
  • Habig WH, Pabst MJ, Jakoby WB. 1974. Glutathione S-transferases: the first enzymatic step in mercapturic acid formation. Journal of biological Chemistry 249(22): 7130-7139.
  • Karaman M, Temel Y, Bayindir S. (2020). Inhibition effect of rhodanines containing benzene moieties on pentose phosphate pathway enzymes and molecular docking. Journal of Molecular Structure, 1220: 128700.
  • Kopustinskiene DM, Jakstas V, Savickas A, Bernatoniene J. 2020. Flavonoids as anticancer agents. Nutrients, 12(2): 1–25.
  • Kuchibhotla P, Rao BD. 1995. A methodology for fast scheduling of partitioned systolic algorithms. Journal of VLSI Signal Processing, 10(2): 111–126.
  • Laemmli UK. 1970. 1970 Nature Publishing Group. Nature Publishing Group, 228, 1979.
  • Liao S, Williams-Ashman HG. 1964. Glutathione reductase. Enzyme, 13(1955): 888–894.
  • Lineweaver H, Burk D. 1934. The Determination of enzyme dissociation constants. Journal of the American Chemical Society, 56(3): 658–666.
  • Loscalzo J, Freedman J. 1986. Purification and characterization of human platelet glutathione-S- transferase. Blood 67(6): 1595–1599.
  • Özaslan MS, Demir Y, Aksoy M., Küfrevioğlu ÖI, Beydemir Ş. 2018. Inhibition effects of pesticides on glutathione-S-transferase enzyme activity of Van Lake fish liver. Journal of Biochemical and Molecular Toxicology, 32(9): e22196
  • Özaslan MS, Demir Y, Aslan HE, Beydemir Ş, Küfrevioğlu Öİ. 2018. Evaluation of chalcones as inhibitors of glutathione S-transferase. Journal of Biochemical and Molecular Toxicology, 32(5): 1–6.
  • Pljesa-Ercegovac M, Savic-Radojevic A, Matic M, Coric V, Djukic T, Radic T, Simic T. 2018. Glutathione transferases: Potential targets to overcome chemoresistance in solid tumors. International Journal of Molecular Sciences, 19(12): 3785
  • Shahıdı F. 2015.Fereidoon (ed.). Handbook of antioxidants for food preservation. Woodhead Publishing.
  • Sayın Y. 2022. Kaz Karaciğer Dokusundan Glutatyon S-Transferaz Enziminin Saflaştırılması, Karakterizasyonu ve Bazı Kimyasalların Enzim Aktivitesi Üzerine Etkilerinin İncelenmesi, Ağrı İbrahim Çeçen Üniversitesi Fen Bilimleri Enstitüsü Kimya Ana Bilim Dalı, Yüksek Lisans Tezi (Basılmış).
  • Taysi MŞ, Temel Y. 2021. Glutathione S-transferase: Purification and characterization from quail (Coturnix coturnix japonica) liver and the impact of some metal ions on enzyme activity. BioNanoScience, 11(1): 91–98.
  • Temel Y, Koçyigit UM, Taysı MŞ, Gökalp F, Gürdere MB, Budak Y, Çiftci M. 2018. 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. Journal of biochemical and molecular toxicology, 32(3): e22034.
  • Temel Y, Kufrevioǧlu ÖI, Çiftci M. 2017. Investigation of the effects of purification and characterization of turkey (Meleagris gallopavo) liver mitochondrial thioredoxin reductase enzyme and some metal ions on enzyme activity. Turkish Journal of Chemistry, 41(1):48-60
  • Temel Y, Taysi MŞ. 2019. The effect of mercury chloride and boric acid on rat erythrocyte enzymes. Biological Trace Element Research, 191(1):177-182
  • Temel Y, Bozkuş T, Karagözoğlu Y, Çiftci M. 2017a. Glutatyon redüktaz (GR) enziminin japon bıldırcın (Coturnix coturnix japanica) eritrositlerinden saflaştırılması ve karakterizasyonu Journal of the Institute of Science and Technology, 7(3): 143-150.
  • Temel Y, Ciftci M, Akkoyun HT, Akkoyun M. 2017b. Effect of astaxanthin and aluminum chloride on erythrocyte G6PD and 6PGD enzyme activities in vivo and on erythrocyte G6PD in vitro in rats. Journal of biochemical and molecular toxicology 31(10): e21954.
  • Temel Y, Kocyigit UM. 2017. Purification of glucose-6-phosphate dehydrogenase from rat (Rattus norvegicus) erythrocytes and inhibition effects of some metal ions on enzyme activity. Journal of biochemical and molecular toxicology 31(9)): e21927.
  • Temel Y, Ayna A, Hamdi Shafeeq I, Ciftci M. 2020. In vitro effects of some antibiotics on glucose-6-phosphate dehydrogenase from rat (Rattus norvegicus) erythrocyte. Drug and chemical toxicology, 43(2): 219-223.
  • Toribio F, Martínez-Lara E, Pascual P, López-Barea J. 1996. Methods for purification of glutathione peroxide and related enzymes. Journal of Chromatography B: Biomedical Applications, 684(1–2): 77–97.
  • Türkan F, Huyut Z, Demir Y, Ertaş F, Beydemir Ş. 2019. The effects of some cephalosporins on acetylcholinesterase and glutathione S-transferase: an in vivo and in vitro study. Archives of Physiology and Biochemistry, 125(3): 235–243.
  • Türkan F, Huyut Z, Taslimi P, Huyut MT, Gülçin İ. 2020. Investigation of the effects of cephalosporin antibiotics on glutathione S-transferase activity in different tissues of rats in vivo conditions in order to drug development research. Drug and Chemical Toxicology, 43(4): 423–428.
  • Ulusu G. 2005. Purification and characterization of glutathione reductase from sheep liver. Turkish Journal of Veterinary & Animal Sciences, 29(5): 1109-1117.
  • Wang J, Yi J. 2008. Cancer cell killing via ROS: To increase or decrease, that is a question. Cancer Biology and Therapy, 7(12): 1875–1884.
  • Zaric Y, Yerlikaya E, Demirdag R. 2019. Purification, Characterization of Glutathione S-Transferase from the Gill Tissue of Lake Van Fish and Inhibition Effects of Some Metal Ions and Pesticides. Fresenius Environmental Bulletin. 28: 9004-9010.

Glutathione S-transferase: Purification and Characterization from Sheep Spleen Tissue

Year 2022, Volume: 12 Issue: 4, 2352 - 2363, 01.12.2022
https://doi.org/10.21597/jist.1150868

Abstract

In this study, glutathione S-transferase (GST; EC 2.5.1.18), which is the important enzyme of the glutathione antioxidant system, which is the main intracellular antioxidant system, was purified in three steps from sheep spleen tissue; using homogenate preparation, ammonium sulfate precipitation method and affinity chromatography (glutathione-agarose) with a specific activity value of 3.67 EU mg-1, 122.3 protein fold and 3.73% yield. SDS-PAGE method was used to determine the purity level and to determine the natural molecular mass of subunits of the GST enzyme, purified from sheep spleen tissue. The molecular mass of the subunits of the sheep spleen tissue GST enzyme was calculated as approximately 26.36 kDa. In the studies carried out for the characterization of the GST enzyme purified from sheep spleen tissue; optimum pH, K-phosphate buffer pH=8.0, optimum ionic strength, K-phosphate buffer 1.0 M, stable pH, K-phosphate buffer pH = 7.0 and optimum temperature 60 oC. Lineweaver-Burk graphs were used in kinetic studies to determine the KM and Vmax values of the GST enzyme purified from sheep spleen tissue. In the kinetic studies carried out for reduced glutathione (GSH) and 1-chloro-2,4-dinitrobenzene (CDNB), which are the substrates of the GST Enzyme; for GSH the KM value 0.629 mM, the Vmax value 0.056 EU mL-1, for CDNB the KM value 0.321 mM, and the Vmax value 0.129 EU mL-1 were determined.

References

  • AAdem S, Ciftci M. 2012. 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): 1–4.
  • Akkemik E, Şentürk M, Özgeriş FB, Taşer P, Çiftci M. 2011. In vitro eff ects of some drugs on human erythrocyte glutathione reductase 41(2): 235–241.
  • Akkemik E, Taser P, Bayindir A, Budak H, Ciftci M. 2012a. Purification and characterization of glutathione S-transferase from turkey liver and inhibition effects of. Environmental Toxicology and Pharmacology 34(3): 888–894.
  • Akkemik E, Taser P, Bayindir A, Budak H, Ciftci M. 2012b. Purification and characterization of glutathione S-transferase from turkey liver and inhibition effects of some metal ions on enzyme activity. Environmental Toxicology and Pharmacology 34(3): 888–894.
  • Aksoy M, Ozaslan MS, Kufrevioglu OI. 2016. Purification of glutathione S-transferase from Van Lake fish (Chalcalburnus tarichii Pallas) muscle and investigation of some metal ions effect on enzyme activity. Journal of Enzyme Inhibition and Medicinal Chemistry 31(4): 546–550.
  • Aybek H, Temel Y, Ahmed BM, Ağca CA, Çiftci M. 2020. Deciphering of The Effect of Chemotherapeutic Agents on Human Glutathione S-Transferase Enzyme and MCF-7 Cell Line. Protein and Peptide Letters 27(9): 888–894.
  • Balcı N, Türkan F, Şakiroğlu H, Aygün A, Şen F. 2019. Purification and characterization of glutathione S-transferase from blueberry fruits (Vaccinium arctostaphylos L.) and investigated of some pesticide inhibition effects on enzyme activity. Heliyon, 5(4): e01422.
  • Balcı N, Şakiroğlu H, Türkan F, Bursal E. 2021. In vitro and in silico enzyme inhibition effects of some metal ions and compounds on glutathione S-transferase enzyme purified from Vaccinium arctostapylous L. Journal of Biomolecular Structure and Dynamics, 1-7.
  • Balendiran GK, Dabur R, Fraser D. 2004. The role of glutathione in cancer. Cell Biochemistry and Function, 22(6): 343–352.
  • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical biochemistry 72(1-2): 248-254.
  • Çetin A, Bursal E, Türkan F. 2021. 2-methylindole analogs as cholinesterases and glutathione S-transferase inhibitors: Synthesis, biological evaluation, molecular docking, and pharmacokinetic studies. Arabian Journal of Chemistry, 14(12): 103449.
  • De Koning AJ, De Koning CB, De Koning PD. 2005. Antioxidants. Handbook of food science, Technology, and Engineering - 4 : 1653–1662.
  • Demirdag R, Yerlikaya E, Kufrevioglu O.I, Gundogdu C. 2013. Purification of glutathione S-transferase isoenzymes from tumour and nontumour human stomach and inhibitory effects of some heavy metals on enzymes activities. Journal of Enzyme Inhibition and Medicinal Chemistry, 28(5): 911-915.
  • Gülçin I. 2010. Antioxidant properties of resveratrol: A structure-activity insight. Innovative Food Science and Emerging Technologies, 11(1): 210–218.
  • Gülçin I. 2012. Antioxidant activity of food constituents: An overview. Archives of Toxicology, 86(3): 345–391.
  • Gülçin İ, Taslimi P, Aygün A, Sadeghian N, Bastem E, Kufrevioglu OI, Şen F. 2018. Antidiabetic and antiparasitic potentials: Inhibition effects of some natural antioxidant compounds on α-glycosidase, α-amylase and human glutathione S-transferase enzymes. International Journal of Biological Macromolecules, 119: 741–746.
  • Orhan H, Şahin G. 1995.Glutatyon S-Transferazların klinik ve toksikolojik önemi. Türkiye Klinikleri Tıp Bilimleri, 15: 303-15.
  • Habig WH, Pabst MJ, Jakoby WB. 1974. Glutathione S-transferases: the first enzymatic step in mercapturic acid formation. Journal of biological Chemistry 249(22): 7130-7139.
  • Karaman M, Temel Y, Bayindir S. (2020). Inhibition effect of rhodanines containing benzene moieties on pentose phosphate pathway enzymes and molecular docking. Journal of Molecular Structure, 1220: 128700.
  • Kopustinskiene DM, Jakstas V, Savickas A, Bernatoniene J. 2020. Flavonoids as anticancer agents. Nutrients, 12(2): 1–25.
  • Kuchibhotla P, Rao BD. 1995. A methodology for fast scheduling of partitioned systolic algorithms. Journal of VLSI Signal Processing, 10(2): 111–126.
  • Laemmli UK. 1970. 1970 Nature Publishing Group. Nature Publishing Group, 228, 1979.
  • Liao S, Williams-Ashman HG. 1964. Glutathione reductase. Enzyme, 13(1955): 888–894.
  • Lineweaver H, Burk D. 1934. The Determination of enzyme dissociation constants. Journal of the American Chemical Society, 56(3): 658–666.
  • Loscalzo J, Freedman J. 1986. Purification and characterization of human platelet glutathione-S- transferase. Blood 67(6): 1595–1599.
  • Özaslan MS, Demir Y, Aksoy M., Küfrevioğlu ÖI, Beydemir Ş. 2018. Inhibition effects of pesticides on glutathione-S-transferase enzyme activity of Van Lake fish liver. Journal of Biochemical and Molecular Toxicology, 32(9): e22196
  • Özaslan MS, Demir Y, Aslan HE, Beydemir Ş, Küfrevioğlu Öİ. 2018. Evaluation of chalcones as inhibitors of glutathione S-transferase. Journal of Biochemical and Molecular Toxicology, 32(5): 1–6.
  • Pljesa-Ercegovac M, Savic-Radojevic A, Matic M, Coric V, Djukic T, Radic T, Simic T. 2018. Glutathione transferases: Potential targets to overcome chemoresistance in solid tumors. International Journal of Molecular Sciences, 19(12): 3785
  • Shahıdı F. 2015.Fereidoon (ed.). Handbook of antioxidants for food preservation. Woodhead Publishing.
  • Sayın Y. 2022. Kaz Karaciğer Dokusundan Glutatyon S-Transferaz Enziminin Saflaştırılması, Karakterizasyonu ve Bazı Kimyasalların Enzim Aktivitesi Üzerine Etkilerinin İncelenmesi, Ağrı İbrahim Çeçen Üniversitesi Fen Bilimleri Enstitüsü Kimya Ana Bilim Dalı, Yüksek Lisans Tezi (Basılmış).
  • Taysi MŞ, Temel Y. 2021. Glutathione S-transferase: Purification and characterization from quail (Coturnix coturnix japonica) liver and the impact of some metal ions on enzyme activity. BioNanoScience, 11(1): 91–98.
  • Temel Y, Koçyigit UM, Taysı MŞ, Gökalp F, Gürdere MB, Budak Y, Çiftci M. 2018. 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. Journal of biochemical and molecular toxicology, 32(3): e22034.
  • Temel Y, Kufrevioǧlu ÖI, Çiftci M. 2017. Investigation of the effects of purification and characterization of turkey (Meleagris gallopavo) liver mitochondrial thioredoxin reductase enzyme and some metal ions on enzyme activity. Turkish Journal of Chemistry, 41(1):48-60
  • Temel Y, Taysi MŞ. 2019. The effect of mercury chloride and boric acid on rat erythrocyte enzymes. Biological Trace Element Research, 191(1):177-182
  • Temel Y, Bozkuş T, Karagözoğlu Y, Çiftci M. 2017a. Glutatyon redüktaz (GR) enziminin japon bıldırcın (Coturnix coturnix japanica) eritrositlerinden saflaştırılması ve karakterizasyonu Journal of the Institute of Science and Technology, 7(3): 143-150.
  • Temel Y, Ciftci M, Akkoyun HT, Akkoyun M. 2017b. Effect of astaxanthin and aluminum chloride on erythrocyte G6PD and 6PGD enzyme activities in vivo and on erythrocyte G6PD in vitro in rats. Journal of biochemical and molecular toxicology 31(10): e21954.
  • Temel Y, Kocyigit UM. 2017. Purification of glucose-6-phosphate dehydrogenase from rat (Rattus norvegicus) erythrocytes and inhibition effects of some metal ions on enzyme activity. Journal of biochemical and molecular toxicology 31(9)): e21927.
  • Temel Y, Ayna A, Hamdi Shafeeq I, Ciftci M. 2020. In vitro effects of some antibiotics on glucose-6-phosphate dehydrogenase from rat (Rattus norvegicus) erythrocyte. Drug and chemical toxicology, 43(2): 219-223.
  • Toribio F, Martínez-Lara E, Pascual P, López-Barea J. 1996. Methods for purification of glutathione peroxide and related enzymes. Journal of Chromatography B: Biomedical Applications, 684(1–2): 77–97.
  • Türkan F, Huyut Z, Demir Y, Ertaş F, Beydemir Ş. 2019. The effects of some cephalosporins on acetylcholinesterase and glutathione S-transferase: an in vivo and in vitro study. Archives of Physiology and Biochemistry, 125(3): 235–243.
  • Türkan F, Huyut Z, Taslimi P, Huyut MT, Gülçin İ. 2020. Investigation of the effects of cephalosporin antibiotics on glutathione S-transferase activity in different tissues of rats in vivo conditions in order to drug development research. Drug and Chemical Toxicology, 43(4): 423–428.
  • Ulusu G. 2005. Purification and characterization of glutathione reductase from sheep liver. Turkish Journal of Veterinary & Animal Sciences, 29(5): 1109-1117.
  • Wang J, Yi J. 2008. Cancer cell killing via ROS: To increase or decrease, that is a question. Cancer Biology and Therapy, 7(12): 1875–1884.
  • Zaric Y, Yerlikaya E, Demirdag R. 2019. Purification, Characterization of Glutathione S-Transferase from the Gill Tissue of Lake Van Fish and Inhibition Effects of Some Metal Ions and Pesticides. Fresenius Environmental Bulletin. 28: 9004-9010.
There are 44 citations in total.

Details

Primary Language Turkish
Subjects Chemical Engineering
Journal Section Kimya / Chemistry
Authors

Fatih Yüksel 0000-0003-0022-4170

Yusuf Temel 0000-0001-8148-3718

Early Pub Date November 25, 2022
Publication Date December 1, 2022
Submission Date July 29, 2022
Acceptance Date October 8, 2022
Published in Issue Year 2022 Volume: 12 Issue: 4

Cite

APA Yüksel, F., & Temel, Y. (2022). Glutatyon S-transferaz: Koyun Dalak Dokusundan Saflaştırılması ve Karakterizasyonu. Journal of the Institute of Science and Technology, 12(4), 2352-2363. https://doi.org/10.21597/jist.1150868
AMA Yüksel F, Temel Y. Glutatyon S-transferaz: Koyun Dalak Dokusundan Saflaştırılması ve Karakterizasyonu. J. Inst. Sci. and Tech. December 2022;12(4):2352-2363. doi:10.21597/jist.1150868
Chicago Yüksel, Fatih, and Yusuf Temel. “Glutatyon S-Transferaz: Koyun Dalak Dokusundan Saflaştırılması Ve Karakterizasyonu”. Journal of the Institute of Science and Technology 12, no. 4 (December 2022): 2352-63. https://doi.org/10.21597/jist.1150868.
EndNote Yüksel F, Temel Y (December 1, 2022) Glutatyon S-transferaz: Koyun Dalak Dokusundan Saflaştırılması ve Karakterizasyonu. Journal of the Institute of Science and Technology 12 4 2352–2363.
IEEE F. Yüksel and Y. Temel, “Glutatyon S-transferaz: Koyun Dalak Dokusundan Saflaştırılması ve Karakterizasyonu”, J. Inst. Sci. and Tech., vol. 12, no. 4, pp. 2352–2363, 2022, doi: 10.21597/jist.1150868.
ISNAD Yüksel, Fatih - Temel, Yusuf. “Glutatyon S-Transferaz: Koyun Dalak Dokusundan Saflaştırılması Ve Karakterizasyonu”. Journal of the Institute of Science and Technology 12/4 (December 2022), 2352-2363. https://doi.org/10.21597/jist.1150868.
JAMA Yüksel F, Temel Y. Glutatyon S-transferaz: Koyun Dalak Dokusundan Saflaştırılması ve Karakterizasyonu. J. Inst. Sci. and Tech. 2022;12:2352–2363.
MLA Yüksel, Fatih and Yusuf Temel. “Glutatyon S-Transferaz: Koyun Dalak Dokusundan Saflaştırılması Ve Karakterizasyonu”. Journal of the Institute of Science and Technology, vol. 12, no. 4, 2022, pp. 2352-63, doi:10.21597/jist.1150868.
Vancouver Yüksel F, Temel Y. Glutatyon S-transferaz: Koyun Dalak Dokusundan Saflaştırılması ve Karakterizasyonu. J. Inst. Sci. and Tech. 2022;12(4):2352-63.