DIVERGENCE AND CONSERVATION OF EPITOPES IN INTERMEDIATE-SIZE SECRETORY PROTEINS FROM 3 SPECIES OF CHIRONOMUS

1. Affinity-purified antibodies against chemically synthesized peptides were used in immunoblotting experiments to search for common epitopes in intermediate size secretory proteins from Chironomus tentans, Chironomus pallidivittatus and Chironomus thummi. 2. Anti-peptide antibodies against C tentans 140 kDa and 195 kDa secretory proteins (sp140 and sp195, respectively) failed to react with secretory proteins from the other two species. 3. Antibodies against an 18-residue peptide from a 185 kDa secretory protein (sp 185) in C. tentans reacted equally with spl 85 in C. pallidivittatus and a 220 kDa secretory protein (sp220) in C. thummi. 4. The amino acid compositions of sp185 and sp220 are similar, particularly in their high cysteine content (17-24%). 5. We conclude that sp185 and sp220 may be structurally related proteins.