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생화학분자생물학회 (Korean Society for Biochemistry and Molecular Biology)
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Purification and Biochemical Properties of Glutathione S-Transferase from Lactuca sativa

  • Park, Hee-Joong (Department of Chemistry, College of Natural Sciences, Chung-Ang University) ;
  • Cho, Hyun-Young (Department of Chemistry, College of Natural Sciences, Chung-Ang University) ;
  • Kong, Kwang-Hoon (Department of Chemistry, College of Natural Sciences, Chung-Ang University)
  • 발행 : 2005.03.31
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초록

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 S-hexylGSH 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.

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참고문헌

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