Hemoglobin oxidation

NP Niké Posta
ÉC Éva Csősz
MO Melinda Oros
DP Dávid Pethő
LP László Potor
GK Gergő Kalló
ZH Zoltán Hendrik
KS Katalin Éva Sikura
GM Gábor Méhes
CT Csaba Tóth
JP József Posta
GB György Balla
JB József Balla
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Hemoglobin (10 µmol/L) was oxidized with H2O2 (40 µmol/L) at room temperature for 30 min. To assess the effect of haptoglobin on the fragmentation of hemoglobin, hemoglobin was incubated with haptoglobin (Hp 1-1, 330-12, Lee BioSolutions, 10 µmol/L) and then exposed to H2O2 (40 µmol/L) at room temperature. The oxidized products were concentrated with an Amicon Ultra-0.5 centrifugal filter unit with an Ultracel-10 membrane (UFC501096, Merck KGaA, Darmstadt, Germany). The concentrated fraction (containing 30 µg of protein) was subjected to SDS-PAGE (NW04120BOX, NuPAGE Bis-Tris Precast Gel, Thermo Scientific).

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