Abstract
The damage to blood coagulation factor XIII (FXIII) at different stages of its enzymatic activation under the action of various physiological amounts of hypochlorite ion was studied. The results obtained by HPLC-MS/MS, SDS-PAGE, and colorimetry showed that, during the conversion of FXIII to FXIIIa, the vulnerability of FXIII to hypochlorite-induced oxidation increased. FXIII oxidized with 150 μM hypochlorite completely retained its enzymatic activity inherent to the intact protein, whereas FXIIIa treated with 50 μM hypochlorite showed sharply reduced enzymatic activity. It was shown that a number of methionine and cysteine residues on the catalytic subunit can perform antioxidant function; additionally, the regulatory subunits of FXIII-B contribute to the antioxidant protection of the catalytic center of the FXIII-A subunit, which, together with the tight packing of the tetrameric structure of the FXIII proenzyme, are the three factors that provide high protein resistance to the oxidizing agent.
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ACKNOWLEDGMENTS
In this study, we used 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).
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Translated by M. Batrukova
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Vasilyeva, A.D., Yurina, L.V., Bugrova, A.E. et al. The Nature of Resistance of the Coagulation Factor XIII Structure to Hypochlorite-Induced Oxidation. Dokl Biochem Biophys 495, 276–281 (2020). https://doi.org/10.1134/S1607672920050117
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DOI: https://doi.org/10.1134/S1607672920050117