Title of article
ISOLATION AND PURIFICATION OF GLUTATHIONE S-TRANSFERASE FROM RAT LIVER
Author/Authors
Al-Jumaily, Essam F. A. Baghdad University - Biotechnology Institute - Biotechnology Department Genetic Engineering, Iraq , Ameen, Zahraa F. Baghdad University - Biotechnology Institute - Biotechnology Department Genetic Engineering, Iraq , Jassim, Ayad H. Al-Nahrain University - Science College - Chemistry Department, Iraq
From page
137
To page
144
Abstract
Glutathione S-transferase (EC 2.5.1.18) was purified to homogeneity from rat liver. The enzyme was initially separated by a preparative anion exchange chromatographic step using DEAE-Cellulose, then cation exchange chromatographic CM-Cellulose was used, followed by subsequent chromatography on Sephacryl S-200, the enzyme was purified about 419.88 fold with an 56.43% yield. The purified enzyme had a specific activity of 1250x10^-3 unit/mg protein, indicated that the enzyme is momoner of Mr (50000) Daltons SDS gel electrophoresis studies.
Keywords
Glutathione , S , transferase , isolation, purification, molecule weight, rat liver.
Journal title
Al-Nahrain Journal Of Science
Journal title
Al-Nahrain Journal Of Science
Record number
2644337
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