Peroxide-induced oxidative modification of hemoglobin

Abstract

The oxidative modification of human hemoglobin Hb treated with ydrogen peroxide was investigated. The method of mass spectrometry were detected oxidized amino acid residues of the hemoglobin molecule: αTrp14, αTyr24, αArg31, αMet32, αTyr42, αHis45, αHis72, αMet76, αPro77, αLys90, αCys104, αTyr140, βHis2, βTrp15, βTrp37, βMet55, βCys93, βCys112, βTyr130, βLys144, βHis146. The antioxidant potential of the Hb molecule in the intracellular space and when it enters the blood plasma is discussed.