PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3190453-9	1988	[4] the other type inhibitors showing positive cooperativity for erythrocyte AChE: tetraethylammonium and ethyltrimethylammonium.	Tetraethylammonium	83-101	acetylcholinesterase (Cartwright blood group)	Homo sapiens	77-81	
435550-1	1979	Data are presented in favour of the regulatory role of AChE in passive transmembrane transfer of anions: 1) gradual inhibition of the enzyme with proserin brings about the change of the transport activation energy and irregular shift of temperature in the salient point on Arrhenius curves; 2) complexing of different AChE inhibitors (succinyl cholinechlorine, tetraethyl ammonium, tetramethyl ammonium, d-tubocurarin, proserin) results in the change of transport velocity.	Tetraethylammonium	361-380	acetylcholinesterase (Cartwright blood group)	Homo sapiens	55-59	
5125850-0	1971	The influence of tetraethylammonium ion on the reaction between acetylcholinesterase and selected inhibitors.	Tetraethylammonium	17-35	acetylcholinesterase (Cartwright blood group)	Homo sapiens	64-84	
204352-2	1978	In order to elucidate some features of the mechanism of the acceleration of methanesulfonylation of acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) with cationic accelerators, the methanesulfonylation of this enzyme by high concentrations of methanesulfonylfluoride, in the absence and presence of accelerators decamethonium and tetraethylammonium, was studied.	Tetraethylammonium	340-358	acetylcholinesterase (Cartwright blood group)	Homo sapiens	100-120