DIFFERENTIAL INTERACTION OF THE MONOCLONAL-ANTIBODY AE-1 WITH ACETYLCHOLINESTERASE OLIGOMERS AND MONOMERS FROM RABBIT MUSCLE MICROSOMES, HUMAN BRAIN AND FETAL BOVINE SERUM
C. Floresflores et al., DIFFERENTIAL INTERACTION OF THE MONOCLONAL-ANTIBODY AE-1 WITH ACETYLCHOLINESTERASE OLIGOMERS AND MONOMERS FROM RABBIT MUSCLE MICROSOMES, HUMAN BRAIN AND FETAL BOVINE SERUM, Neuroscience letters, 239(2-3), 1997, pp. 101-104
The monoclonal antibody AE-I raised against acetylcholinesterase (AChE
) from human erythrocytes (HE) is shown to react with active asymmetri
c and tetrameric AChE components from rabbit muscle microsomes (RMM),
and with tetrameric forms from human brain (HE) or fetal bovine serum
(FBS). However, it failed to bind to AChE monomers from RMM or HE. The
results of Western blot revealed that the determinant for AE-I consis
ted of a conformational domain, not a primary sequence region, in the
AChE subunit. The antibody recognized HE monomers and FBS dimers, but
not FBS monomers. The formation of labile immunocomplexes between AE-1
and AChE subunits may explain the lack of interaction between the ant
ibody and the monomers from non-erythrocyte sources. (C) 1997 Elsevier
Science Ireland Ltd.