Purification and characterization of glutathione S-transferase from sugarcane leaves
1991
Singhal, S.S. | Tiwari, N.K. | Ahmad, H. | Srivastava, S.K. | Awasthi, Y.C.
Glutathione S-transferase has been purified from leaves of sugarcane using (NH4)2SO4 fractionation, isoelectric focusing, Sephadex G-100 gel filtration, DEAE cellulose ion-exchange chromatography, and affinity chromatography over GSH-linked to epoxy-activated Sepharose 6B. The enzyme has a pI value of 4.7 and consists of two subunits having Mr values of ca 22500 and 24000. N-Terminal amino acid sequence analysis of both the subunits indicates a high degree of homology between these two subunits. Both subunits also have primary structure homologies with the corn GST subunits characterized previously. Kinetic properties of the enzyme are described and compared with other plant glutathione S-transferases. Similar to human GST isoenzymes, sugarcane leaf GST is also inhibited by the herbicides 2,4-dichlorophenoxyacetate, 2,4,5-trichlorophenoxyacetate, and chenodeoxycholate.
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