Peroxide-Induced Oxidative Modification of Hemoglobin

A. D. Vasilyeva, L. V. Yurina, A. E. Bugrova, M. I. Indeykina, D. Y. Azarova, A. V. Bychkova, K. I. Akzhigitova, A. S. Kononikhin, E. N. Nikolaev, M. A. Rosenfeld

    Research output: Contribution to journalArticlepeer-review

    1 Citation (Scopus)


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

    Original languageEnglish
    Pages (from-to)197-200
    Number of pages4
    JournalDoklady Biochemistry and Biophysics
    Issue number1
    Publication statusPublished - 1 May 2019


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