Abstract
By using the mass-spectrometry method, the oxidative modifications of the fibrinogen Aα, Bβ, and γ polypeptide chains induced by its oxidation have been studied. The αC-region has been proven to be the most vulnerable target for the oxidizer (ozone) as compared with the other structural elements of the Aα chain. The Bβ chain mapping shows that the oxidative sites are localized within all the structural elements of the chain in which the β-nodule exhibits high susceptibility to oxidation. The γ chains are the least vulnerable to the oxidizer action. The results obtained demonstrate convincingly that the self-assembly centers dealing with interactions of knob “A”: hole “a” are not involved in oxidative modification. It is concluded that the numerous oxidative sites revealed are mainly responsible for inhibiting lateral aggregation of protofibrils. The part of amino acid residues subjected to oxidation is supposed to carry out the antioxidant function.
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Original Russian Text © A.V. Bychkova, A.D. Vasilyeva, A.E. Bugrova, M.I. Indeykina, A.S. Kononikhin, E.N. Nikolaev, M.L. Konstantinova, M.A. Rosenfeld, 2017, published in Doklady Akademii Nauk, 2017, Vol. 474, No. 2, pp. 238–242.
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Bychkova, A.V., Vasilyeva, A.D., Bugrova, A.E. et al. Oxidation-induced modification of the fibrinogen polypeptide chains. Dokl Biochem Biophys 474, 173–177 (2017). https://doi.org/10.1134/S1607672917030115
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DOI: https://doi.org/10.1134/S1607672917030115