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Clinical Chemistry 42: 19-23, 1996;
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Clinical Chemistry, Vol 42, 19-23, Copyright © 1996 by American Association for Clinical Chemistry

Monoclonal antibodies against a C-terminal peptide of human brain acetylcholinesterase distinguish between erythrocyte and brain acetylcholinesterases

N Boschetti, U Brodbeck, SP Jensen, C Koch and B Norgaard-Pedersen
Institute of Biochemistry and Molecular Biology, University of Bern, Switzerland.

Monoclonal antibodies (mAbs) were raised against a peptide of the 10 C- terminal amino acids of human brain acetylcholinesterase (AChE): H-Tyr- Ser-Lys-Gln-Asp-Arg-Cys-Ser-Asp-Leu-OH. Two positive clones (mAbs 190-1 and 190-2) were selected and tested for their ability to distinguish between mammalian brain and erythrocyte AChEs. In a solid-phase enzyme antigen immunoassay as well as by Western- and dot-blot analysis, both antibodies showed clear binding to AChE from human and bovine brain but not to AChE from erythrocytes. MAbs 190-1 and 190-2 reacted with neither AChE from electric eel nor butyrylcholinesterase from human serum. Both antibodies were used in a quantitative assay for AChE in amniotic fluids, where AChE activity could be found only in samples from open neural tube-defect pregnancies, but not in fluids from normal pregnancies or in artificially blood-contaminated samples.




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Copyright © 1996 by the American Association for Clinical Chemistry.