PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
62424-6	1976	These results confirm the molecular and functional heterogeneity of rat AFP and suggest that the carbohydrate moiety of the protein may have a role in estrogen-AFP interactions.	Carbohydrates	97-109	alpha-fetoprotein	Rattus norvegicus	72-75	
1720412-3	1991	Carbohydrate-free rat AFP was electrophoretically homogeneous.	Carbohydrates	0-12	alpha-fetoprotein	Rattus norvegicus	22-25	
6197305-0	1983	Structure determination of the carbohydrate chains of rat alpha-fetoprotein.	Carbohydrates	31-43	alpha-fetoprotein	Rattus norvegicus	58-75	
6197305-3	1983	Based on methylation analysis and high-resolution 1H-NMR spectroscopy of the re-N-acetylated hydrazinolysates, the carbohydrate structures of the two ConA-molecular variants of alpha-fetoprotein were established.	Carbohydrates	115-127	alpha-fetoprotein	Rattus norvegicus	177-194	
6162639-6	1981	Moreover it was demonstrated that each alpha 1-fetoprotein variant contained either two glycans 1a or two glycans 2a, not randomly, but a pair of the identical carbohydrate chains at the two glycosylation sites.	Carbohydrates	160-172	alpha-fetoprotein	Rattus norvegicus	39-58	
65808-7	1977	These results confirm the molecular and functional heterogeneity of rat AFT and suggest that the carbohydrate moiety of the protein may have a role in estrogen-AFP interactions.	Carbohydrates	97-109	alpha-fetoprotein	Rattus norvegicus	160-163	
62424-6	1976	These results confirm the molecular and functional heterogeneity of rat AFP and suggest that the carbohydrate moiety of the protein may have a role in estrogen-AFP interactions.	Carbohydrates	97-109	alpha-fetoprotein	Rattus norvegicus	160-163