PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3144917-3	1988	Arachidonic acid (bound to fatty acid-free human serum albumin) added to serum-free medium caused a concentration-dependent increase in the production of prostacyclin by myometrial cells.	Epoprostenol	154-166	albumin	Homo sapiens	49-62	
2478194-0	1989	Characterization of the interaction between prostacyclin and human serum albumin using a fluorescent analogue, 2,6-dichloro-4-aminophenol iloprost.	Epoprostenol	44-56	albumin	Homo sapiens	67-80	
1764464-13	1991	These findings indicate that albumin plays a major role in protecting PGI2 activity and regulating its availability for platelet PGI2 receptors.	Epoprostenol	70-74	albumin	Homo sapiens	29-36	
1764464-0	1991	Regulation of PGI2 activity by serum proteins: serum albumin but not high density lipoprotein is the PGI2 binding and stabilizing protein in human blood.	Epoprostenol	14-18	albumin	Homo sapiens	53-60	
1764464-0	1991	Regulation of PGI2 activity by serum proteins: serum albumin but not high density lipoprotein is the PGI2 binding and stabilizing protein in human blood.	Epoprostenol	101-105	albumin	Homo sapiens	53-60	
1764464-1	1991	Although previous studies have shown that serum albumin binds PGI2 and protects it from rapid degradation, it remains debatable whether it is physiologically important due to its low binding affinity for PGI2.	Epoprostenol	62-66	albumin	Homo sapiens	48-55	
1764464-11	1991	To determine whether physiological concentrations of albumin influence PGI2 binding to platelet receptors, we measured PGI2 binding to platelet membrane in the absence and presence of albumin.	Epoprostenol	71-75	albumin	Homo sapiens	53-60	
1764464-12	1991	Albumin at 40 mg/ml increased the KD of PGI2 binding to the receptors by 2-3 fold.	Epoprostenol	40-44	albumin	Homo sapiens	0-7