Peroxide-Induced Damage to Plasminogen Molecules

A. D. Vasilyeva, V. S. Ivanov, L. V. Yurina, M. I. Indeykina, A. E. Bugrova, A. S. Kononikhin, E. N. Nikolaev, M. A. Rosenfeld

Research output: Contribution to journalArticlepeer-review


Abstract: Plasminogen is a zymogenic form of plasmin, an enzyme that plays a fundamental role in the dissolution of fibrin clots as well as in many other physiological processes. For the first time, by the method of gas chromatography–mass spectrometry, post-translational modifications in the primary structure of plasminogen treated with physiologically relevant amounts of hydrogen peroxide were identified. It was found that methionine and tryptophan residues located in different structural regions of plasminogen served as targets of the oxidant. Plasminogen oxidation caused a dose-dependent effect in decreasing the fibrinogenolytic activity of plasmin evidenced by the formation of fibrinogen degradation products. The possible antioxidant role of methionines in the oxidative modification of plasminogen is discussed.

Original languageEnglish
Pages (from-to)419-423
Number of pages5
JournalDoklady Biochemistry and Biophysics
Issue number1
Publication statusPublished - Nov 2021


  • antioxidant methionines
  • electrophoresis
  • hydrogen peroxide
  • mass spectrometry
  • oxidation
  • oxidation sites
  • plasminogen/plasmin


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