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.

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