Proteomic identification of glutathione S-transferases from the model nematode Caenorhabditis elegans

Andy Tait, James R. Jefferies, John Barrett, Peter M. Brophy, Arjan Johannes van Rossum

Research output: Contribution to journalArticlepeer-review

28 Citations (SciVal)

Abstract

Glutathione affinity chromatography and two-dimensional electrophoresis (2-DE) were used to purify glutathione binding proteins from Caenorhabditis elegans. All proteins identified after peptide mass fingerprinting using matrix-assisted laser desorption/ionization-time of flight were found to belong to the glutathione S-transferase (GST) superfamily. From the 26 individual spots identified, 12 different GSTs were isolated. Of these, five were found on the gel only once, whilst the remaining seven were represented by 21 separate spots. Most of the GSTs identified were of the nematode specific class, however, three Alpha class GSTs, a Pi and a Sigma class GST were also isolated.
Original languageEnglish
Pages (from-to)1463-1468
Number of pages6
JournalProteomics
Volume1
Issue number11
DOIs
Publication statusPublished - 21 Nov 2001

Keywords

  • Glutathione S-transferase
  • Affinity chromatography
  • Matrix-assisted laser desorption
  • ionization-time of flight
  • Two-dimensional electrophoresis

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