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Anionic subsite of active center of Torpedo acetylcholinesterase constructs a part of its conformational epitope

   
@article{APS6973,
	author = {Feng-Hua Fu and Yan-Bin Xin and Feng-Zhen Li and Han Zhang and Man-Ji Sun},
	title = {Anionic subsite of active center of Torpedo acetylcholinesterase constructs a part of its conformational epitope},
	journal = {Acta Pharmacologica Sinica},
	volume = {18},
	number = {5},
	year = {2016},
	keywords = {},
	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.},
	issn = {1745-7254},	url = {http://www.chinaphar.com/article/view/6973}
}