ISOLATION AND PURIFICATION OF GLUTATHIONE S-TRANSFERASE FROM RAT LIVER

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.