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Peptidasic Activities Associated with Acetylcholinesterase Are Due to Contaminating Enzymes
Author(s) -
Checler Frédéric,
Vincent JeanPierre
Publication year - 1989
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1989.tb11793.x
Subject(s) - acetylcholinesterase , neurotensin , enzyme , chemistry , biochemistry , immunoprecipitation , neuropeptide , dissociation (chemistry) , hydrolysis , monoclonal antibody , microbiology and biotechnology , biology , antibody , gene , organic chemistry , immunology , receptor
The esterasic and peptidasic activities of two different sources of acetylcholinesterase purified from electric eel were examined. Hydrolyses of leucine‐enkephalin and neurotensin indicated that both sources exhibited exopepti‐dasic and tryptic‐like activities. However, the enzyme preparation which appeared 10‐fold enriched with regard to the esterasic activity was found to display a 50‐ and 185‐fold lower tryptic‐like and exopeptidasic function, respectively. This lack of parallelism in the enrichment of the various activities seemed to indicate that they were not co‐purified. Immunoprecipitation experiments performed with monoclonal antibodies directed towards the catalytic subunit of globular or asymmetric forms of electric eel acetylcholinesterase allowed the physical dissociation of esterasic and peptidasic functions and therefore confirmed that the ability of acetylcholinesterase to hydrolyze various neuropeptides was likely due to contaminating peptidases.