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.
Wang
Y X
YX
Institute of Pharmacology and Toxicology, Academy of Military Medical Sciences, Beijing, China.
Xin
Y B
YB
Sun
M J
MJ
D000110:Acetylcholinesterase / Q000187:drug effects / Q000276:immunology* / Q000302:isolation & purification; D000478:Alkylation; D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D003488:Cyanogen Bromide / Q000494:pharmacology; D004557:Electric Organ / Q000737:chemistry*; D000939:Epitopes; D010084:Oxidation-Reduction; D010434:Pepsin A / Q000494:pharmacology; D010446:Peptide Fragments / Q000276:immunology; D014101:Torpedo; D014357:Trypsin / Q000494:pharmacology
D000911:Antibodies, Monoclonal; D000939:Epitopes; D010446:Peptide Fragments; D000110:Acetylcholinesterase; D014357:Trypsin; D010434:Pepsin A; D003488:Cyanogen Bromide