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Doklady Biochemistry and Biophysics

, Volume 488, Issue 1, pp 332–337 | Cite as

Hypochlorite-Induced Damage of Plasminogen Molecules: Structural-Functional Disturbance

  • A. D. VasilyevaEmail author
  • L. V. Yurina
  • A. N. Shchegolikhin
  • A. E. Bugrova
  • T. S. Konstantinova
  • M. I. Indeykina
  • A. S. Kononikhin
  • E. N. Nikolaev
  • M. A. Rosenfeld
BIOCHEMISTRY, BIOPHYSICS, AND MOLECULAR BIOLOGY

Abstract

Plasminogen, the precursor of plasmin, is a serine protease that plays a fundamental role in the intravascular thrombolysis. For the first time, by using high-resolution mass spectrometry, data on the oxidative modifications of the plasminogen molecule under induced oxidation were obtained. The FTIR data show that, under oxidation on the protein, its secondary structure also undergoes the rearrangements. The high tolerance of plasminogen to oxidation can be due to both the closed conformation and the ability of some Met residues to serve as ROS trap.

Notes

ACKNOWLEDGMENTS

This study was performed using the equipment of the Core Facility of the Emanuel Institute of Biochemical Physics, Russian Academy of Sciences.

FUNDING

Mass spectrometric data were obtained with the support of the Russian Science Foundation (project no. 16-14-00181).

COMPLIANCE WITH ETHICAL STANDARDS

Conflict of interests. The authors declare that they have no conflict of interest.

Statement of compliance with standards of research involving humans as subjects. All procedures performed in studies involving human participants were in accordance with the ethical standards of the institutional and/or national research committee and with the 1964 Helsinki Declaration and its later amendments or comparable ethical standards. Informed consent was obtained from all individual participants involved in the study.

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Copyright information

© Pleiades Publishing, Ltd. 2019

Authors and Affiliations

  • A. D. Vasilyeva
    • 1
    Email author
  • L. V. Yurina
    • 1
  • A. N. Shchegolikhin
    • 1
  • A. E. Bugrova
    • 1
  • T. S. Konstantinova
    • 1
  • M. I. Indeykina
    • 1
    • 3
  • A. S. Kononikhin
    • 2
    • 4
  • E. N. Nikolaev
    • 4
  • M. A. Rosenfeld
    • 1
  1. 1.Emanuel Institute of Biochemical Physics, Russian Academy of SciencesMoscowRussia
  2. 2.Talrose Institute for Energy Problems of Chemical Physics, Semenov Federal Center of Chemical Physics, Russian Academy of SciencesMoscowRussia
  3. 3.Moscow Institute of Physics and Technology (State University)DolgoprudnyiRussia
  4. 4.Skolkovo Institute of Science and TechnologySkolkovoRussia

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