PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11692726-1	2001	Changes were studied in processes of peroxide oxidation of lipid (LPO), such as neutral lipids and phospholipids, as related to the levels of hemoglobin (Hb) and its derivatives, methemoglobin (Met-Hb) and carboxyhemoglobin (CO-Hb) in erythrocytes and blood plasma of 33 patients with iron-deficiency anemia (IDA).	Peroxides	37-45	hemoglobin subunit gamma 2	Homo sapiens	179-192	
11692726-3	2001	Increase in the level of Met-Hb is accompanied by an accumulation in erythrocytes of Schiff bases as the final products of phospholipids peroxidation (r = 0.586, P = 0.004), CO-Hb-substrates of LPO (r = 0.425, P = 0.049), primary (r = 0.453, P = 0.04) and secondary (r = 0.438, P = 0.048) molecular products of peroxide oxidation of neutral lipids.	Peroxides	311-319	hemoglobin subunit gamma 2	Homo sapiens	25-31	
1312811-4	1992	The major cytotoxic radical species generated in the mixtures of various peroxides and heme iron, especially methemoglobin, metmyoglobin, or hemin, was the alkyl peroxyl radical (ROO.).	Peroxides	73-82	hemoglobin subunit gamma 2	Homo sapiens	109-122	
3697367-5	1986	These compounds, but not the other amines given above, inhibited the peroxide compound formation from methemoglobin and hydrogen peroxide.	Peroxides	69-77	hemoglobin subunit gamma 2	Homo sapiens	102-115	
5831949-0	1965	[Effect of peroxide forming cytostatics on the methemoglobin and glutathione content of normal and akatalatic erythrocytes].	Peroxides	11-19	hemoglobin subunit gamma 2	Homo sapiens	47-60	
19178454-2	2009	In the presence of peroxides, deoxyhemoglobin and methemoglobin can produce free radicals and induce lipid peroxidation.	Peroxides	19-28	hemoglobin subunit gamma 2	Homo sapiens	50-63	
19868866-6	1924	At a somewhat later time in the logarithmic period of the culture peroxide was demonstrable and, simultaneously with the appearance of this substance, the substrate acquired the ability to change catalase-free crystalline hemoglobin to methemoglobin.	Peroxides	66-74	hemoglobin subunit gamma 2	Homo sapiens	236-249	
15892615-4	2005	The product of the oxidation (presumably NO2*) directly oxidizes oxyhemoglobin to methemoglobin-peroxide complex without hydrogen peroxide release into the environment.	Peroxides	96-104	hemoglobin subunit gamma 2	Homo sapiens	82-95