PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8478079-1	1993	Enzymatically active and inactive (diisopropylfluorophosphate-treated) cathepsin G exerted antibacterial action in vitro against Staphylococcus aureus, whereas only enzymatically active cathepsin G displayed bactericidal action against Pseudomonas aeruginosa.	Isoflurophate	35-61	cathepsin G	Homo sapiens	71-82	
1658173-7	1991	Enzyme-inhibitor complexes were stable in sodium dodecyl sulfate at 100 degrees C but were dissociated by hydrolysis in ammonium hydroxide (1.5 mol/L) at 37 degrees C. Formation of each complex was prevented by pretreatment of elastase or cathepsin G with diisopropylfluorophosphate, indicating that the inhibitor binds to the active site of the enzyme.	Isoflurophate	256-282	cathepsin G	Homo sapiens	239-250	
3316266-10	1987	After inhibition of elastase, the residual activity was inhibited by diisopropylfluorophosphate; thus, it was due to a serine protease(s) such as cathepsin G.	Isoflurophate	69-95	cathepsin G	Homo sapiens	146-157