Glutathione binding proteins in the gastrointestinal nematode Heligmosomoides polygyrus.
A glutathione-affinity matrix was used to identify glutathione-dependent protein(s) in somatic extracts of the nematode Heligmosomoides polygyrus. Polypeptides of 70-80 kDa were retained by the affinity matrix following the elution of H. polygyrus glutathione S-transferases by 5 mM glutathione. The 70-80-kDa polypeptides were subsequently eluted from the matrix by the addition of 20 mM glutathione and these polypeptides did not show glutathione S-transferase activity. The high-affinity H. polygyrus glutathione-binding proteins may be related to the uncharacterized purification hindering factors previously demonstrated during the isolation of glutathione S-transferases in several other helminths.
Brophy
P M
PM
Pharmacy Department, School of Applied Sciences, De Montfort University, Leicester, United Kingdom.
Ben-Smith
A
A
Behnke
J M
JM
Brown
A
A
Pritchard
D I
DI
D000818:Animals; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005978:Glutathione / Q000378:metabolism*; D005982:Glutathione Transferase / Q000302:isolation & purification; D015801:Helminth Proteins / Q000737:chemistry / Q000378:metabolism*; D007526:Isoelectric Point; D009351:Nematospiroides dubius / Q000737:chemistry* / Q000378:metabolism
D015801:Helminth Proteins; D005982:Glutathione Transferase; D005978:Glutathione