PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3603728-1	1987	A commercial preparation of water-soluble acetylcholinesterase from horse red cells has been purified to a specific activity of 2380 U/mg of protein (a 1660-fold purification) by a twofold affinity chromatography on the known sorbent of Sepharose-p-[NH-(CH2)5-C(O)NH(CH2)5C(O)NH-]-C6H4-N+(CH3)3 X Br- at pH 7.5.	Sepharose	237-246	acetylcholinesterase	Equus caballus	42-62	
6501251-4	1984	Bovine erythrocyte acetylcholinesterase released by PI-specific phospholipase C was purified by column chromatography on DEAE-cellulose, affinity gel and Sepharose 6B, to a homogeneous state, as indicated by polyacrylamide gel electrophoresis, with a recovery of 39%.	Sepharose	154-163	acetylcholinesterase	Equus caballus	19-39	
6501251-7	1984	On elution from the Sepharose 6B column, Triton X-100-solubilized acetylcholinesterase was eluted at the void volume while the enzyme obtained by further treatment with PI-specific phospholipase C was eluted in the region corresponding to M.W.	Sepharose	20-29	acetylcholinesterase	Equus caballus	66-86