PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
235320-2	1975	We measured lipoprotein lipase activity in dried defatted preparations of rat lung using doubly labeled chylomicron triglyceride as substrate.	Triglycerides	116-128	lipoprotein lipase	Rattus norvegicus	12-30	
235320-4	1975	Lungs from fed rats hydrolyzed chylomicron triglyceride at a rate of 13.00 mumoles/g per h; the activity rate was unchanged by fasting 8-72 h. Heparin infusion into isolated lungs caused immediate release of lipoprotein lipase to the venous effluent.	chylomicron triglyceride	31-55	lipoprotein lipase	Rattus norvegicus	208-226	
235320-4	1975	Lungs from fed rats hydrolyzed chylomicron triglyceride at a rate of 13.00 mumoles/g per h; the activity rate was unchanged by fasting 8-72 h. Heparin infusion into isolated lungs caused immediate release of lipoprotein lipase to the venous effluent.	Heparin	143-150	lipoprotein lipase	Rattus norvegicus	208-226	
235320-6	1975	Since the ability to remove blood triglyceride is directly related to the level of lipoprotein lipase activity, these findings indicate that the lung is one of the few tissues able to remove efficiently blood triglyceride during fasting.	Triglycerides	34-46	lipoprotein lipase	Rattus norvegicus	83-101	
235320-6	1975	Since the ability to remove blood triglyceride is directly related to the level of lipoprotein lipase activity, these findings indicate that the lung is one of the few tissues able to remove efficiently blood triglyceride during fasting.	Triglycerides	209-221	lipoprotein lipase	Rattus norvegicus	83-101