PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1461372-4	1992	Labeling DS-AChE with 3-(trifluoromethyl)-3-(m-(125I)-iodophenyl) diazirine ([125I]TID) revealed, by polyacrylamide gel electrophoresis under reducing conditions, one single band of 69 kD apparent molecular mass.	3-(trifluoromethyl)-3-(m-(125i)-iodophenyl) diazirine	22-75	acetylcholinesterase	Rattus norvegicus	12-16	
1461372-4	1992	Labeling DS-AChE with 3-(trifluoromethyl)-3-(m-(125I)-iodophenyl) diazirine ([125I]TID) revealed, by polyacrylamide gel electrophoresis under reducing conditions, one single band of 69 kD apparent molecular mass.	polyacrylamide	101-115	acetylcholinesterase	Rattus norvegicus	12-16	
1461372-7	1992	These results are compatible with the existence of a hydrophobic segment present both on salt-soluble and detergent-soluble 11 S AChE as well as on the minor forms 4 S and 7 S. This segment is not linked to the catalytic subunits by disulfide bounds in contrast to the 20 kD non-catalytic subunit described by Inestrosa et al.	Salts	89-93	acetylcholinesterase	Rattus norvegicus	129-133	
1461372-7	1992	These results are compatible with the existence of a hydrophobic segment present both on salt-soluble and detergent-soluble 11 S AChE as well as on the minor forms 4 S and 7 S. This segment is not linked to the catalytic subunits by disulfide bounds in contrast to the 20 kD non-catalytic subunit described by Inestrosa et al.	Disulfides	233-242	acetylcholinesterase	Rattus norvegicus	129-133