Modification of the catalytic subunit of plasma fibrin-stabilizing factor under induced oxidation

A. D. Vasilyeva, A. V. Bychkova, A. E. Bugrova, M. I. Indeykina, A. P. Chikunova, V. B. Leonova, E. A. Kostanova, M. I. Biryukova, M. L. Konstantinova, A. S. Kononikhin, E. N. Nikolaev, M. A. Rosenfeld

    Research output: Contribution to journalArticlepeer-review

    5 Citations (Scopus)


    For the first time, by using mass-spectrometry method, the oxidation-mediated modification of the catalytic FXIII-A subunit of plasma fibrin-stabilizing factor, pFXIII, has been studied. The oxidative sites were identified to belong to all structural elements of the catalytic subunit: the β-sandwich (Tyr104, Tyr117, and Cys153), the catalytic core domain (Met160, Trp165, Met266, Cys328, Asp352, Pro387, Arg409, Cys410, Tyr442, Met475, Met476, Tyr482, and Met500), the β-barrel 1 (Met596), and the β-barrel 2 (Met647, Pro676, Trp692, Cys696, and Met710), which correspond to 3.9%, 1.11%, 0.7%, and 3.2%, respectively, of oxidative modifications as compared to the detectable amounts of amino acid residues in each of the structural domains. Lack of information on some parts of the molecule may be associated with the spatial unavailability of residues, complicating analysis of the molecule. The absence of oxidative sites localized within crucial areas of the structural domains may be brought about by both the spatial inaccessibility of the oxidant to amino acid residues in the zymogen and the screening effect of the regulatory FXIII-B subunit.

    Original languageEnglish
    Pages (from-to)40-43
    Number of pages4
    JournalDoklady Biochemistry and Biophysics
    Issue number1
    Publication statusPublished - 1 Jan 2017


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