PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2847800-1	1988	Chlorination of monochlorodimedon is routinely used to measure the production of hypochlorous acid catalysed by myeloperoxidase from H2O2 and Cl-.	Hypochlorous Acid	81-98	myeloperoxidase	Homo sapiens	112-127	
2847800-6	1988	Both the amount of hypochlorous acid formed during the burst phase, and the steady-state rate of hypochlorous acid production, increased with increasing concentrations of myeloperoxidase and with decreasing concentrations of monochlorodimedon.	Hypochlorous Acid	19-36	myeloperoxidase	Homo sapiens	171-186	
2847800-6	1988	Both the amount of hypochlorous acid formed during the burst phase, and the steady-state rate of hypochlorous acid production, increased with increasing concentrations of myeloperoxidase and with decreasing concentrations of monochlorodimedon.	Hypochlorous Acid	97-114	myeloperoxidase	Homo sapiens	171-186	
2847800-8	1988	From these results, and the ability of myeloperoxidase to slowly peroxidase monochlorodimedon in the absence of Cl-, we propose that the reaction of monochlorodimedon with the myeloperoxidase/H2O2/Cl- system involves a major pathway due to hypochlorous acid-dependent chlorination and a minor peroxidative pathway.	Hypochlorous Acid	240-257	myeloperoxidase	Homo sapiens	39-54	
2847800-8	1988	From these results, and the ability of myeloperoxidase to slowly peroxidase monochlorodimedon in the absence of Cl-, we propose that the reaction of monochlorodimedon with the myeloperoxidase/H2O2/Cl- system involves a major pathway due to hypochlorous acid-dependent chlorination and a minor peroxidative pathway.	Hypochlorous Acid	240-257	myeloperoxidase	Homo sapiens	176-191	
2847800-13	1988	We suggest, therefore, that in vivo the rate of turnover of compound II may determine the rate of myeloperoxidase-dependent production of hypochlorous acid by stimulated neutrophils.	Hypochlorous Acid	138-155	myeloperoxidase	Homo sapiens	98-113