PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24271910-3	1982	The results show that, singly or in combination, bicarbonate, orthophosphate, citrate, apo-transferrin, and/or albumin have less than one-tenth of the ability to enhance the oxidation of Fe(II) compared to the serum enzyme, ceruloplasmin.	ammonium ferrous sulfate	187-193	ceruloplasmin	Homo sapiens	224-237	
24271910-5	1982	Whereas ceruloplasmin produces a 4:1 ratio of Fe(II) oxidized to oxygen utilized, the non-enzymic components yield a 2:1 or 3.09:1 ratio.	ammonium ferrous sulfate	46-52	ceruloplasmin	Homo sapiens	8-21	
24271910-6	1982	These data support the role of ceruloplasmin as an antioxidant that prevents the formation of the intermediate active oxygen species O 2 (-)   and H2O 2 ( ) through the Fe(II) auto-oxidation reaction.A hitherto unrecognized factor in the control of nonenzymic oxidation of Fe(II) was serum albumin.	ammonium ferrous sulfate	169-175	ceruloplasmin	Homo sapiens	31-44	
24271910-6	1982	These data support the role of ceruloplasmin as an antioxidant that prevents the formation of the intermediate active oxygen species O 2 (-)   and H2O 2 ( ) through the Fe(II) auto-oxidation reaction.A hitherto unrecognized factor in the control of nonenzymic oxidation of Fe(II) was serum albumin.	ammonium ferrous sulfate	273-279	ceruloplasmin	Homo sapiens	31-44	
24271910-8	1982	The addition of ceruloplasmin effected up to a 44 x increase in the rate of Fe(II) oxidation and Fe(III)-transferrin formation even in the presence of 0.60 mM albumin.	ammonium ferrous sulfate	76-82	ceruloplasmin	Homo sapiens	16-29