title: Purification and biochemical properties of glutathione S-transferase from Lactuca sativa.
abstract: A glutathione S-transferase (GST) from Lactuca sativa was purified to electrophoretic homogeneity approximately 403-fold with a 9.6% activity yield by DEAE-Sephacel and glutathione (GSH)-Sepharose column chromatography. The molecular weight of the enzyme was determined to be approximately 23,000 by SDS-polyacrylamide gel electrophoresis and 48,000 by gel chromatography, indicating a homodimeric structure. The activity of the enzyme was significantly inhibited by ShexylGSH and S-(2,4-dinitrophenyl) glutathione. The enzyme displayed activity towards 1-chloro-2,4-dinitrobenzene, a general GST substrate and high activities towards ethacrynic acid. It also exhibited glutathione peroxidase activity toward cumene hydroperoxide.
authors.affiliation: Department of Chemistry, College of Natural Sciences, Chung-Ang University, Dongjak-ku, Seoul 156-756, Korea.
authors.forename: Hee-Joong
authors.initials: HJ
authors.lastname: Park
authors.forename: Hyun-Young
authors.initials: HY
authors.lastname: Cho
authors.forename: Kwang-Hoon
authors.initials: KH
authors.lastname: Kong
mesh_terms: D004791:Enzyme Inhibitors / Q000494:pharmacology; D004795:Enzyme Stability; D005982:Glutathione Transferase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D018545:Lactuca / Q000201:enzymology*; D008970:Molecular Weight; D013379:Substrate Specificity
chemical_list: D004791:Enzyme Inhibitors; D005982:Glutathione Transferase