Epitopes recognized by anti-reduced and alkylated acetylcholinesterase antibodies

Peptides of the reduced and alkylated acetylcholinesterase (RA-AChE) from the electric organ of Torpediniformes Torpedo torpedo subjected to bromo-cynogen (CNBr) cleavage or/and peptic digestion conserved well the antigen-antibody reactivity with anti-RA-AChE monoclonal antibodies E9, F6, and F12, whereas peptides produced by CNBr and tryptic treatments lost all the reactivity. Periodate oxidation of the RA-AChE or glycopeptidase digestion of the CNBr cleaved RA-AChE did not change the antigen-antibody reactivity. It implied that the epitopes recognized by the 3 anti-RA-AChE monoclonal antibodies are all peptide determinants rather than carbohydrate determinants.