| Autor: |
Vasilyeva AD; N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 117977, Russia., Bychkova AV; N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 117977, Russia., Bugrova AE; N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 117977, Russia., Indeykina MI; N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 117977, Russia., Chikunova AP; N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 117977, Russia., Leonova VB; N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 117977, Russia., Kostanova EA; N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 117977, Russia., Biryukova MI; N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 117977, Russia., Konstantinova ML; N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 117977, Russia., Kononikhin AS; N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 117977, Russia.; N.M. Emanuel Energy Problems of Chemical Physics, Russian Academy of Sciences, Moscow, 117334, Russia.; Moscow Institute of Physics and Technology (State University), Dolgoprudny, Moscow region, 141700, Russia., Nikolaev EN; N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 117977, Russia.; N.M. Emanuel Energy Problems of Chemical Physics, Russian Academy of Sciences, Moscow, 117334, Russia.; Skolkovo Institute of Science and Technology, Skolkovo, Moscow oblast, 143025, Russia., Rosenfeld MA; N.M. Emanuel Institute of Biochemical Physics, Russian Academy of Sciences, Moscow, 117977, Russia. markrosenfeld@rambler.ru. |
| Abstrakt: |
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. |
