Glutathione S-transferase: Purification and Characterization from Quail (Coturnix coturnix japonica) Liver and the Impact of Some Metal Ions on Enzyme Activity

Author:

Taysi Mehmet ŞerifORCID,Temel YusufORCID

Funder

Bingöl Üniversitesi

Publisher

Springer Science and Business Media LLC

Subject

Biomedical Engineering,Bioengineering

Reference46 articles.

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2. Temel, Y., Koçyigit, U. M., Taysı, M. Ş., Gökalp, F., Gürdere, M. B., Budak, Y., Gulcin, I., & 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.

3. Sheehan, D., Meade, G., Foley, V. M., & Dowd, C. A. (2001). Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. The Biochemical Journal, 360(1), 1–16.

4. Autrup, H. (2000). Genetic polymorphism in human xenobiotica metabolizing enzymes as susceptibility factors in toxic response. Mutation Research, 464(1), 65–76.

5. Işik, M., Demir, Y., Kirici, M., Demir, R., Şimşek, F., & Beydemir, Ş. (2015). Changes in the anti-oxidant system in adult epilepsy patients receiving anti-epileptic drugs. Archives of Physiology and Biochemistry, 121, 97–102.

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