title: Separation of glutathione transferase subunits from Proteus vulgaris by two-dimensional gel electrophoresis.
abstract: Cytosolic glutathione transferases of Proteus vulgaris were purified by affinity chromatography and characterized by two-dimensional gel electrophoresis. Four different subunits were identified, and each subunit contained a different molecular mass, ranging from 26.2 kDa to 28.5 kDa; a different pI value, ranging from 8.2 to 9.4; and a different amount of protein fraction, ranging from 10% to 56%. All four subunits existed as basic proteins (pI > 7.0). From these results, we concluded that multiple forms of glutathione transferase enzymes existed in Proteus vulgaris, and four different glutathione transferase subunits were separated by 2-D gel electrophoresis.
authors: Department of Environmental Engineering and Science, Feng Chia University, P.O. Box 25-223, Taichung 407, Taiwan.
authors: Giaming
authors: G
authors: Hong
authors: Yi-Chih
authors: YC
authors: Chien
authors: Cheng-I
authors: CI
authors: Chien
mesh_terms: D002846:Chromatography, Affinity / Q000379:methods; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods; D005982:Glutathione Transferase / Q000737:chemistry*; D007526:Isoelectric Point; D008970:Molecular Weight; D021122:Protein Subunits / Q000032:analysis / Q000302:isolation & purification*; D011514:Proteus vulgaris / Q000201:enzymology*
chemical_list: D021122:Protein Subunits; D005982:Glutathione Transferase