PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24632343-2	2014	In contrast to plant peroxidases, like horseradish peroxidase (HRP), the mammalian counterparts myeloperoxidase (MPO) and lactoperoxidase (LPO) are rapidly and irreversibly inactivated by chlorite in the micromolar concentration range.	chlorite	188-196	myeloperoxidase	Homo sapiens	96-111	
24632343-2	2014	In contrast to plant peroxidases, like horseradish peroxidase (HRP), the mammalian counterparts myeloperoxidase (MPO) and lactoperoxidase (LPO) are rapidly and irreversibly inactivated by chlorite in the micromolar concentration range.	chlorite	188-196	myeloperoxidase	Homo sapiens	113-116	
24632343-3	2014	Chlorite acts as efficient one-electron donor for Compound I and Compound II of MPO and LPO and reacts with the corresponding ferric resting states in a biphasic manner.	chlorite	0-8	myeloperoxidase	Homo sapiens	80-83	
24632343-4	2014	The first (rapid) phase is shown to correspond to the formation of a MPO-chlorite high-spin complex, whereas during the second (slower) phase degradation of the prosthetic group was observed.	chlorite	73-81	myeloperoxidase	Homo sapiens	69-72