PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6534126-0	1984	The effect of myoglobin concentration on muscle cell PO2 gradients.	PO-2	53-56	myoglobin	Homo sapiens	14-23	
3215851-1	1988	The aim of this paper was to measure the binding of CO to myoglobin and hemoglobin at various PO2 values.	PO-2	94-97	myoglobin	Homo sapiens	58-67	
3215851-3	1988	The results indicate that a significant proportion of CO is released by hemoglobin and binds myoglobin at low PO2 values (approximately 2-3 Torr), in qualitative agreement with the predictions of a previous computer simulation of the "in vivo" system.	PO-2	110-113	myoglobin	Homo sapiens	93-102	
16421206-1	2006	Myoglobin (Mb) has a purported role in facilitating O2 diffusion in tissue, especially as cellular PO2 drops or the respiration demand increases.	PO-2	99-102	myoglobin	Homo sapiens	0-9	
16421206-1	2006	Myoglobin (Mb) has a purported role in facilitating O2 diffusion in tissue, especially as cellular PO2 drops or the respiration demand increases.	PO-2	99-102	myoglobin	Homo sapiens	11-13	
10401602-3	1999	The degree to which the decrease in pH and the freeing of copper ions, as well as the variations in pO2 associated with ischemia and reperfusion increase the rates of such myoglobin reactions has been investigated.	PO-2	100-103	myoglobin	Homo sapiens	172-181