PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2542309-5	1989	Both loss of iron binding capacity and transferrin iodination by either the myeloperoxidase system or activated neutrophils were blocked by azide or catalase.	Iron	13-17	myeloperoxidase	Homo sapiens	76-91	
2542309-0	1989	Inactivation of transferrin iron binding capacity by the neutrophil myeloperoxidase system.	Iron	28-32	myeloperoxidase	Homo sapiens	68-83	
2542309-7	1989	The kinetics of changes in iron binding capacity and iodination closely paralleled one another, exhibiting t1/2 values of less than 1 min for the myeloperoxidase-H2O2 system, 3-4 min for the myeloperoxidase-glucose oxidase system, and 8 min for the neutrophil system.	Iron	27-31	myeloperoxidase	Homo sapiens	146-161	
2542309-7	1989	The kinetics of changes in iron binding capacity and iodination closely paralleled one another, exhibiting t1/2 values of less than 1 min for the myeloperoxidase-H2O2 system, 3-4 min for the myeloperoxidase-glucose oxidase system, and 8 min for the neutrophil system.	Iron	27-31	myeloperoxidase	Homo sapiens	191-206	
2542309-8	1989	That the occupied binding site is protected from the myeloperoxidase system was suggested by 1) a failure to mobilize iron from iron-loaded transferrin, 2) an inverse correlation between initial iron saturation and myeloperoxidase-mediated loss of iron binding capacity, and 3) decreased myeloperoxidase-mediated iodination of iron-loaded versus apotransferrin.	Iron	118-122	myeloperoxidase	Homo sapiens	53-68	
2542309-8	1989	That the occupied binding site is protected from the myeloperoxidase system was suggested by 1) a failure to mobilize iron from iron-loaded transferrin, 2) an inverse correlation between initial iron saturation and myeloperoxidase-mediated loss of iron binding capacity, and 3) decreased myeloperoxidase-mediated iodination of iron-loaded versus apotransferrin.	Iron	118-122	myeloperoxidase	Homo sapiens	215-230	
2542309-8	1989	That the occupied binding site is protected from the myeloperoxidase system was suggested by 1) a failure to mobilize iron from iron-loaded transferrin, 2) an inverse correlation between initial iron saturation and myeloperoxidase-mediated loss of iron binding capacity, and 3) decreased myeloperoxidase-mediated iodination of iron-loaded versus apotransferrin.	Iron	118-122	myeloperoxidase	Homo sapiens	215-230	
2542309-8	1989	That the occupied binding site is protected from the myeloperoxidase system was suggested by 1) a failure to mobilize iron from iron-loaded transferrin, 2) an inverse correlation between initial iron saturation and myeloperoxidase-mediated loss of iron binding capacity, and 3) decreased myeloperoxidase-mediated iodination of iron-loaded versus apotransferrin.	Iron	128-132	myeloperoxidase	Homo sapiens	53-68	
2542309-8	1989	That the occupied binding site is protected from the myeloperoxidase system was suggested by 1) a failure to mobilize iron from iron-loaded transferrin, 2) an inverse correlation between initial iron saturation and myeloperoxidase-mediated loss of iron binding capacity, and 3) decreased myeloperoxidase-mediated iodination of iron-loaded versus apotransferrin.	Iron	128-132	myeloperoxidase	Homo sapiens	215-230	
2542309-8	1989	That the occupied binding site is protected from the myeloperoxidase system was suggested by 1) a failure to mobilize iron from iron-loaded transferrin, 2) an inverse correlation between initial iron saturation and myeloperoxidase-mediated loss of iron binding capacity, and 3) decreased myeloperoxidase-mediated iodination of iron-loaded versus apotransferrin.	Iron	128-132	myeloperoxidase	Homo sapiens	215-230	
2542309-8	1989	That the occupied binding site is protected from the myeloperoxidase system was suggested by 1) a failure to mobilize iron from iron-loaded transferrin, 2) an inverse correlation between initial iron saturation and myeloperoxidase-mediated loss of iron binding capacity, and 3) decreased myeloperoxidase-mediated iodination of iron-loaded versus apotransferrin.	Iron	128-132	myeloperoxidase	Homo sapiens	53-68	
2542309-8	1989	That the occupied binding site is protected from the myeloperoxidase system was suggested by 1) a failure to mobilize iron from iron-loaded transferrin, 2) an inverse correlation between initial iron saturation and myeloperoxidase-mediated loss of iron binding capacity, and 3) decreased myeloperoxidase-mediated iodination of iron-loaded versus apotransferrin.	Iron	128-132	myeloperoxidase	Homo sapiens	215-230	
2542309-8	1989	That the occupied binding site is protected from the myeloperoxidase system was suggested by 1) a failure to mobilize iron from iron-loaded transferrin, 2) an inverse correlation between initial iron saturation and myeloperoxidase-mediated loss of iron binding capacity, and 3) decreased myeloperoxidase-mediated iodination of iron-loaded versus apotransferrin.	Iron	128-132	myeloperoxidase	Homo sapiens	215-230	
2542309-8	1989	That the occupied binding site is protected from the myeloperoxidase system was suggested by 1) a failure to mobilize iron from iron-loaded transferrin, 2) an inverse correlation between initial iron saturation and myeloperoxidase-mediated loss of iron binding capacity, and 3) decreased myeloperoxidase-mediated iodination of iron-loaded versus apotransferrin.	Iron	128-132	myeloperoxidase	Homo sapiens	53-68	
2542309-8	1989	That the occupied binding site is protected from the myeloperoxidase system was suggested by 1) a failure to mobilize iron from iron-loaded transferrin, 2) an inverse correlation between initial iron saturation and myeloperoxidase-mediated loss of iron binding capacity, and 3) decreased myeloperoxidase-mediated iodination of iron-loaded versus apotransferrin.	Iron	128-132	myeloperoxidase	Homo sapiens	215-230	
2542309-8	1989	That the occupied binding site is protected from the myeloperoxidase system was suggested by 1) a failure to mobilize iron from iron-loaded transferrin, 2) an inverse correlation between initial iron saturation and myeloperoxidase-mediated loss of iron binding capacity, and 3) decreased myeloperoxidase-mediated iodination of iron-loaded versus apotransferrin.	Iron	128-132	myeloperoxidase	Homo sapiens	215-230	
2542309-8	1989	That the occupied binding site is protected from the myeloperoxidase system was suggested by 1) a failure to mobilize iron from iron-loaded transferrin, 2) an inverse correlation between initial iron saturation and myeloperoxidase-mediated loss of iron binding capacity, and 3) decreased myeloperoxidase-mediated iodination of iron-loaded versus apotransferrin.	Iron	128-132	myeloperoxidase	Homo sapiens	53-68	
2542309-8	1989	That the occupied binding site is protected from the myeloperoxidase system was suggested by 1) a failure to mobilize iron from iron-loaded transferrin, 2) an inverse correlation between initial iron saturation and myeloperoxidase-mediated loss of iron binding capacity, and 3) decreased myeloperoxidase-mediated iodination of iron-loaded versus apotransferrin.	Iron	128-132	myeloperoxidase	Homo sapiens	215-230	
2542309-8	1989	That the occupied binding site is protected from the myeloperoxidase system was suggested by 1) a failure to mobilize iron from iron-loaded transferrin, 2) an inverse correlation between initial iron saturation and myeloperoxidase-mediated loss of iron binding capacity, and 3) decreased myeloperoxidase-mediated iodination of iron-loaded versus apotransferrin.	Iron	128-132	myeloperoxidase	Homo sapiens	215-230	
2542309-9	1989	Since as little as 1 atom of iodide bound per molecule of transferrin was associated with substantial losses in iron binding capacity, there appears to be a high specificity of myeloperoxidase-catalyzed iodination for residues at or near the iron binding sites.	Iron	112-116	myeloperoxidase	Homo sapiens	177-192	
2542309-9	1989	Since as little as 1 atom of iodide bound per molecule of transferrin was associated with substantial losses in iron binding capacity, there appears to be a high specificity of myeloperoxidase-catalyzed iodination for residues at or near the iron binding sites.	Iron	242-246	myeloperoxidase	Homo sapiens	177-192	
2542309-11	1989	These observations document the ability of neutrophils to inactivate transferrin iron binding capacity via the secretion of myeloperoxidase, formation of H2O2, and subsequent myeloperoxidase-catalyzed iodination.	Iron	81-85	myeloperoxidase	Homo sapiens	124-139	
2542309-11	1989	These observations document the ability of neutrophils to inactivate transferrin iron binding capacity via the secretion of myeloperoxidase, formation of H2O2, and subsequent myeloperoxidase-catalyzed iodination.	Iron	81-85	myeloperoxidase	Homo sapiens	175-190