Purification and biochemical properties of glutathione S-transferase from Lactuca sativa.
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.
Park
Hee-Joong
HJ
Department of Chemistry, College of Natural Sciences, Chung-Ang University, Dongjak-ku, Seoul 156-756, Korea.
Cho
Hyun-Young
HY
Kong
Kwang-Hoon
KH
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
D004791:Enzyme Inhibitors; D005982:Glutathione Transferase