Sheep were immunised against Haemonchus contortus with an integral membrane glycoprotein complex isolated from the intestines of the parasite as antigen. This antigen has been termed Haemonchus galactose-containing glycoprotein complex. Sodium dodecyl sulphate (SDS) polyacrylamide gel analysis has shown that it is composed of several polypeptides but so far these have proved refractory to separation when in the native state. However when dissociated by SDS, it was found to be as efficacious as in its native state, although it was less consistently protective when tested after being dissociated and reduced. An attempt was therefore made to identify the protective ingredient(s) of the dissociated complex by testing its major polypeptides individually after they had been separated on SDS polyacrylamide gels under non-reducing conditions. Partial protection was induced by protein bands with molecular weights of about 200 kD and less than 50 kD, but none of the individual fractions tested was as efficacious as the unseparated complex, suggesting that either more than one component was essential for a consistent effect or that the separation technique had damaged crucial protective epitopes.