Anionic subsite of active center of Torpedo acetylcholinesterase constructs a part of its conformational epitope
Abstract
AIM: To study the structure-activity relationship of Torpedo acetylcholinesterase
(AChE) and explore whether the anionic subsite of the active center is a
constituent of the conformational epitope of enzyme.
METHODS: Using ELISA and enzyme inhibition test to examine the effect of
1-methyl-2-hydroxyiminomethylpyridium chloride (2-PAM), an anionic subsite probe
of AChE, on the immunoreactivity between Torpedo AChE and its monoclonal antibody
(McAb) 3F3.
RESULTS: McAb 3F3 did not react with 2-PAM-AChE complex. 2-PAM decreased the
inhibitory rate of McAb 3F3 on AChE in a concentration-dependent fashion, but did
not dissociate the McAb 3F3-AChE complex.
CONCLUSION: Anionic subsite of the active center of Torpedo AChE constructs a
part of its conformational epitope.
Keywords:
(AChE) and explore whether the anionic subsite of the active center is a
constituent of the conformational epitope of enzyme.
METHODS: Using ELISA and enzyme inhibition test to examine the effect of
1-methyl-2-hydroxyiminomethylpyridium chloride (2-PAM), an anionic subsite probe
of AChE, on the immunoreactivity between Torpedo AChE and its monoclonal antibody
(McAb) 3F3.
RESULTS: McAb 3F3 did not react with 2-PAM-AChE complex. 2-PAM decreased the
inhibitory rate of McAb 3F3 on AChE in a concentration-dependent fashion, but did
not dissociate the McAb 3F3-AChE complex.
CONCLUSION: Anionic subsite of the active center of Torpedo AChE constructs a
part of its conformational epitope.