PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1696509-5	1990	AFP was fractionated by three different chromatographic/electrophoretic methods: E2 affinity chromatography, preparative polyacrylamide-gel electrophoresis (PAGE), and high-performance liquid chromatography (HPLC); and one immunoaffinity method: gel-entrapped antibody filtration (GAF).	polyacrylamide	121-135	alpha fetoprotein	Mus musculus	0-3	
2428091-3	1986	AFP was isolated from Nya:NYLAR mouse amniotic fluid (MAF) by polyacrylamide gel electrophoresis plus Blue Sepharose affinity chromatography (PAGE/BS), and by affinity chromatographies employing immobilized E2 and rabbit anti-AFP.	polyacrylamide	62-76	alpha fetoprotein	Mus musculus	0-3	
2464688-2	1989	Mouse AFP was isolated from amniotic fluid and purified by polyacrylamide gel electrophoresis followed by Blue Sepharose chromatography.	polyacrylamide	59-73	alpha fetoprotein	Mus musculus	6-9	
46267-3	1975	Polyacrylamide gel analysis showed that dialyzed MAF was composed of three major protein components, transferrin, albumin, and alpha-fetoprotein (AFP).	polyacrylamide	0-14	alpha fetoprotein	Mus musculus	146-149	
66068-3	1977	Polyacrylamide slab gel electrophoresis, extended agarose electrophoresis and immunoelectrophoresis demonstrated that mouse hepatoma alpha-fetoprotein migrated at pH 8.6 as a rapid alpha1, or postalbumin globulin.	polyacrylamide	0-14	alpha fetoprotein	Mus musculus	133-150