Differentiation between acetylcholinesterase and the organophosphate-inhibited form using antibodies and the correlation of antibody recognition with reactivation mechanism and rate.

Two types of polyclonal antibodies were generated from (a) a decapeptide sequence that includes the active site serine of acetylcholinesterase (anti-AChE10S) and (b) the identical decapeptide sequence phosphorylated at the active site serine of acetylcholinesterase (anti-AChE10SP). The anti-AChE10S antiserum was found to specifically recognize native, control, and vehicle-treated recombinant mouse AChE (rMoAChE) but did not recognize rMoAChE that was phosphorylated by the four organophosphate (OP) compounds tested. Conversely the anti-AChE10SP antiserum recognized phosphoserine rMoAChE that resulted from reaction with phosphorous oxychloride (POCl3) but did not recognize native or vehicle-treated rMoAChE.

Examination of cross-antigenicity of acetylcholinesterase and butyrylcholinesterase using anti-acetylcholinesterase antibodies.

Acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) share a high degree of homology and overlap in several biochemical properties. This study aimed to compare and contrast the antigenic reactivity of AChE and BuChE with several polyclonal antibodies. We have performed a detailed analysis of AChE and BuChE enzymatic activities with different substrates and different inhibitors.