Pm. Brophy et al., GLUTATHIONE S-TRANSFERASES FROM THE GASTROINTESTINAL NEMATODE HELIGMOSOMOIDES-POLYGYRUS AND MAMMALIAN LIVER COMPARED, Comparative biochemistry and physiology. B. Comparative biochemistry, 109(4), 1994, pp. 585-592
Glutathione S-transferases have been partially characterised from the
gastrointestinal nematode Heligmosomoides polygyrus. Two major subunit
families were purified (24 and 23 kDa) with N-terminal homology to th
e mammalian Alpha family. Four dimeric forms of GST were purified from
the nematode by glutathione-affinity chromatography, two major enzyme
s (pI 8.1, 5.0) and two minor forms (pI 5.8, 5.3). The purified GST po
ol could neutralize model and lipid peroxides via peroxidase activity
but not peroxidation derived reactive carbonyls via glutathione transf
erase activity. Antisera raised to the pooled nematode GSTs appeared t
o recognize other Strongylida GSTs more strongly on Western blotting c
ompared to mammalian GSTs.