Proteomic identification of glutathione S-transferases from the model nematode Caenorhabditis elegans.
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.
van Rossum
A J
AJ
Institute of Biological Sciences, University of Wales, Aberystwyth, Ceredigion, UK. ajv@aber.ac.uk
Brophy
P M
PM
Tait
A
A
Barrett
J
J
Jefferies
J R
JR
D000818:Animals; D017173:Caenorhabditis elegans / Q000201:enzymology*; D002845:Chromatography / Q000379:methods; D019992:Databases as Topic; D005982:Glutathione Transferase / Q000737:chemistry* / Q000378:metabolism; D010802:Phylogeny; D011506:Proteins / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
D011506:Proteins; D005982:Glutathione Transferase