Separation of glutathione transferase subunits from Proteus vulgaris by two-dimensional gel electrophoresis.
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.
Hong
Giaming
G
Department of Environmental Engineering and Science, Feng Chia University, P.O. Box 25-223, Taichung 407, Taiwan.
Chien
Yi-Chih
YC
Chien
Cheng-I
CI
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*
D021122:Protein Subunits; D005982:Glutathione Transferase