ISOLATION AND PURIFICATION OF GLUTATHIONE S-TRANSFERASEFROM RAT LIVER

Abstract

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 DEAECellulose,
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.