Purified glutathione S-transferases from parasites as candidate protective antigens.
Glutathione S-transferase (GST) activity was detected in larvae of the Australian sheep blowfly Lucilia cuprina, and in the nematode Haemonchus contortus. A specific inhibitor of the enzyme was shown to affect survival of both species of parasite in vitro. GST from both parasites has been purified and partially characterized. Antisera raised to the purified enzymes were shown to inhibit the enzyme activity in vitro. However, the antisera had no effect on the survival of either parasite.
Sharp
P J
PJ
Biotech Australia Pty. Ltd, Roseville, New South Wales, Australia.
Smith
D R
DR
Bach
W
W
Wagland
B M
BM
Cobon
G S
GS
D000595:Amino Acid Sequence; D000818:Animals; D004175:Diptera / Q000201:enzymology*; D005982:Glutathione Transferase / Q000032:analysis* / Q000037:antagonists & inhibitors / Q000737:chemistry; D006189:Haemonchus / Q000201:enzymology*; D007106:Immune Sera / Q000276:immunology; D008969:Molecular Sequence Data; D013448:Sulfobromophthalein / Q000494:pharmacology
D007106:Immune Sera; D013448:Sulfobromophthalein; D005982:Glutathione Transferase