Wheat glutathione S-transferase: Purification and properties

G. Williamson, M. C. Beverley

Research output: Contribution to journalArticleResearchpeer-review

Abstract

Glutathione S-transferase (EC 2.5.1 .18) is present in wheat flour (0·07 mg enzyme/g flour). It was purified by hydrophobic interaction chromatography on phenyl Sepharose CL-4B and affinity chromatography on S-hexylglutathione Sepharose 6B. The enzyme is a homodimer with subunit molecular weight of 27500 and an isoelectric point of 5·9. It conjugated glutathione (Km = 0·37 mm) with 1-chloro2,4-dinitrobenzene with a specific activity of 30μmol/min/mg protein. Linoleic acid hydroperoxides were reduced, with a specific activity of 60 nmol/min/mg protein for the 9-hydroperoxy-trans- 10,cis-l2-octadecadienoic acid isomer. The possible contribution of glutathione S-transferase to the baking properties of wheat is discussed.

Original languageEnglish
Pages (from-to)155-163
Number of pages9
JournalJournal of Cereal Science
Volume8
Issue number2
DOIs
Publication statusPublished - 1 Jan 1988
Externally publishedYes

Keywords

  • 1-chloro-2,4-dinitrobenzene
  • 13-hydroperoxy-cis-9,trans-1 1-octadecadienoic acid
  • 13c,t-HPO
  • 9-hydroperoxy-trans- 10,cis-12-octadecadienoic acid
  • 9c,t-HPO
  • CDNB
  • GSH
  • GSSG
  • oxidised glutathione
  • polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate
  • reduced glutathione
  • SDS-PAGE

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