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A conformation‐dependent monoclonal antibody against active chicken acetylcholinesterase
Author(s) -
Chatel Jean-Marc,
Vallette François-Marie,
Massoulié Jean,
Grassi Jacques
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80027-r
Subject(s) - monoclonal antibody , chemistry , trypsin , acetylcholinesterase , enzyme , biochemistry , microbiology and biotechnology , chymotrypsin , antibody , peptide , active site , biology , immunology
We show that the C‐131 monoclonal antibody, directed against chicken AChE, recognizes active chicken AChE, but not the SDS‐denatured or heat‐inactivated protein. Previous results indicated that C‐131 only binds to the active enzyme, and not to inactive molecules which also occur in the embryonic chicken brain. In contrast with C‐131, other monoclonal antibodies obtained in the same series, such as C‐6 and C‐54, also recognize denatured or inactive AChE. It is noteworthy that these antibodies all seem to react with a trypsin‐sensitive peptide which is present in chicken but not in mammalian or Torpedo AChE, whereas the C‐131 antibody binds trypsin‐modified as well as intact molecules. These results show that C‐131 is highly conformation‐dependent, specific for active AChE. They confirm our previous conclusion that active and inactive molecules arise from different folding processes.