Hypochlorite-Induced Oxidative Modification of Fibrinogen


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Oxidation of fibrinogen with hypochlorite inhibited the fibrin network self-assembly even at the lowest concentration of the oxidant. The analysis of the results of protein electrophoresis at this hypochlorite concentration showed the absence of fragmentation of the protein and covalent cross-linking of its chains. The study of the areas responsible for the conversion of fibrinogen into fibrin by mass spectrometry showed that they are not subject to oxidative damage. However, we identified oxidized amino acid residues, which could affect the protofibril aggregation.

作者简介

L. Yurina

Emanuel Institute of Biochemical Physics, Russian Academy of Sciences

编辑信件的主要联系方式.
Email: lyu.yurina@gmail.com
俄罗斯联邦, Moscow, 119334

A. Vasilyeva

Emanuel Institute of Biochemical Physics, Russian Academy of Sciences

Email: lyu.yurina@gmail.com
俄罗斯联邦, Moscow, 119334

A. Bugrova

Emanuel Institute of Biochemical Physics, Russian Academy of Sciences

Email: lyu.yurina@gmail.com
俄罗斯联邦, Moscow, 119334

M. Indeykina

Emanuel Institute of Biochemical Physics, Russian Academy of Sciences; Moscow Institute of Physics and Technology

Email: lyu.yurina@gmail.com
俄罗斯联邦, Moscow, 119334; Dolgoprudnyi, Moscow oblast, 141701

A. Kononikhin

Emanuel Institute of Biochemical Physics, Russian Academy of Sciences; Moscow Institute of Physics and Technology; Tal’roze Institute for Energy Problems of Chemical Physics, Russian Academy of Sciences

Email: lyu.yurina@gmail.com
俄罗斯联邦, Moscow, 119334; Dolgoprudnyi, Moscow oblast, 141701; Moscow, 119334

E. Nikolaev

Emanuel Institute of Biochemical Physics, Russian Academy of Sciences; Tal’roze Institute for Energy Problems of Chemical Physics, Russian Academy of Sciences; Skolkovo Institute of Science and Technology

Email: lyu.yurina@gmail.com
俄罗斯联邦, Moscow, 119334; Moscow, 119334; Skolkovo, Moscow oblast, 143025

M. Rosenfeld

Emanuel Institute of Biochemical Physics, Russian Academy of Sciences

Email: lyu.yurina@gmail.com
俄罗斯联邦, Moscow, 119334

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