PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15040847-3 2004 Erythrocytes exposed to tBHP also show an increase in mean corpuscular volume and a remarkable formation of methemoglobin (met-Hb) without any appearance of hemichromes that form Heinz bodies. tert-Butylhydroperoxide 24-28 hemoglobin subunit gamma 2 Homo sapiens 108-121 18971612-7 2008 RESULTS: When treated with tBHP, the deformability of erythrocytes was decreased (P<0.01) and methemoglobin (metHb) formation and mean corpuscular volume (MCV) of erythrocytes were increased (P<0.01, P<0.05) compared to those of the untreated control cells. tert-Butylhydroperoxide 27-31 hemoglobin subunit gamma 2 Homo sapiens 97-110 18702879-7 2008 The oxidative action induced by TBHP was observed in erythrocytes AA<AS<SS, by the increase in the content of Heinz bodies, methemoglobin, hemolysis, GSH depletion and lowering activities of the enzymes G6-PD and GR. tert-Butylhydroperoxide 32-36 hemoglobin subunit gamma 2 Homo sapiens 130-143 18702879-8 2008 The protective actions of the vitamins C and E for the oxidative stress induced by TBHP were observed for the erythrocytes in the lowering Heinz bodies, methemoglobin, hemolysis, and partial recovery of GSH more efficiently in AS and SS erythrocytes. tert-Butylhydroperoxide 83-87 hemoglobin subunit gamma 2 Homo sapiens 153-166 17115906-7 2006 By mixing either methemoglobin or human blood with tert-butyl hydroperoxide, we found that this technique can detect OR- generated in vitro. tert-Butylhydroperoxide 51-75 hemoglobin subunit gamma 2 Homo sapiens 17-30 8241252-6 1993 Incubation of RBCs with tBHP also resulted in decreased oxyhemoglobin, increased methemoglobin and increased thiobarbituric acid reactive substances (TBARS). tert-Butylhydroperoxide 24-28 hemoglobin subunit gamma 2 Homo sapiens 81-94 8917415-4 1996 The interaction of t-BHP with hemoglobin (Hb) and methemoglobin (MetHb) caused the production of superoxide (O2-) and hydrogen peroxide (H2O2). tert-Butylhydroperoxide 19-24 hemoglobin subunit gamma 2 Homo sapiens 50-63 8917415-4 1996 The interaction of t-BHP with hemoglobin (Hb) and methemoglobin (MetHb) caused the production of superoxide (O2-) and hydrogen peroxide (H2O2). tert-Butylhydroperoxide 19-24 hemoglobin subunit gamma 2 Homo sapiens 65-70 8917415-5 1996 The differential direct effect of t-BHP on Hb and MetHb was investigated by taking their spectra in the presence or absence of cytochrome C. tert-Butylhydroperoxide 34-39 hemoglobin subunit gamma 2 Homo sapiens 50-55 3718986-2 1986 Exposure of human erythrocytes to t-butyl hydroperoxide (0.5-1.0 mM) results in oxidation of glutathione, formation of malonyldialdehyde, and oxidation of hemoglobin to methemoglobin. tert-Butylhydroperoxide 34-55 hemoglobin subunit gamma 2 Homo sapiens 169-182 3718986-6 1986 In cells pre-treated with NaNO2 to convert hemoglobin to methemoglobin, t-butyl hydroperoxide reduces [9,10-3H]oleic acid incorporation into phosphatidylcholine by erythrocytes but does not stimulate [9,10-3H]oleic acid incorporation into phosphatidylethanolamine. tert-Butylhydroperoxide 72-93 hemoglobin subunit gamma 2 Homo sapiens 57-70 3995035-3 1985 As increased hemoglobin oxidation occurred in the erythrocytes, membrane lipid peroxidation diminished, suggesting a protective role for methemoglobin in t-butyl hydroperoxide-induced lipid peroxidation. tert-Butylhydroperoxide 154-175 hemoglobin subunit gamma 2 Homo sapiens 137-150