PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
603347-1	1977	Two kinetic evidences revealed that two cholinesterase forms are present in rat brain homogenate and involved in the hydrolysis of acetylthiocholine.	Acetylthiocholine	131-148	butyrylcholinesterase	Rattus norvegicus	40-54	
18096154-3	2008	Competition assays with the substrate acetylthiocholine showed a concentration-dependent reduction in rat brain cholinesterase Vmax without changes in apparent Km.	Acetylthiocholine	38-55	butyrylcholinesterase	Rattus norvegicus	112-126	
12110369-9	2002	Wild-type rat BChE had an 8- to 9-fold higher K(m) for the positively charged substrates butyrylthiocholine, acetylthiocholine, propionylthiocholine, benzoylcholine, and cocaine compared with wild-type human BChE.	Acetylthiocholine	109-126	butyrylcholinesterase	Rattus norvegicus	14-18