1. Baker, E. N. Lactoferrin: Molecular structure, binding properties and dynamics of lactoferrin / E. N. Baker, H. M. Baker // Cellular and Molecular Life Sciences. – 2005. – Vol. 62, N 22. – P. 2531–2539. https://doi.org/10.1007/s00018-005-5368-9

2. Lactoferrin: a modulator of immune and inflammatory responses/ D. Legrand [et al.] // Cellular and Molecular Life Sciences. – 2005. – Vol. 62, N 22. – P. 2549–2559. https://doi.org/10.1007/s00018-005-5370-2

3. Recombinant human lactoferrin modulates neutrophil degranulation and H2O2 production via increase of intracellular free calcium ion concentration and tyrosine phosphorylation/ D. Grigorieva [et al.] // XIII Intern. Conf. on Lactoferrin Struc., Func. & Appl. – Rome, 2017. – P. 49.

4. Halliwell, B. Hydrogen peroxide in the human body / B. Halliwell, M. V. Clement, L. H. Long // FEBS Letters. – 2000. – Vol. 486, N 1. – P. 10–13. https://doi.org/10.1016/s0014-5793(00)02197-9

5. Doing the unexpected: proteins involved in hydrogen peroxide perception/ J. Hancock [et al.]// J. of Exp. Botany. – 2006. – Vol. 57, N 8. – P. 1711–1718. https://doi.org/10.1093/jxb/erj180

6. Watson, A. J. M. Characterisation of oxidative injury to an intestinal cell line (HT-29) by hydrogen peroxide / A. J. M. Watson, J. N. Askew, G. I. Sandle // Gut. – 1994. – Vol. 35, N 11. – P. 1575–1581. https://doi.org/10.1136/gut.35.11.1575

7. Arnhold, J. Redox properties of myeloperoxidase / J. Arnhold, P. G. Furtmüller, C. Obinger // Redox Report. – 2003. – Vol. 8, N 4. – P. 179–186. https://doi.org/10.1179/135100003225002664

8. Панасенко, О. М. Хлорноватистая кислота как предшественник свободных радикалов в живых системах / О. М. Панасенко, И. В. Горудко, А. В. Соколов // Успехи биол. хим. – 2013. – № 53. – С. 195–244.

9. Davies, M. J. Protein oxidation and peroxidation / M. J. Davies // Biochem. J. – 2016. – Vol. 473, N 7. – P. 805–825. https://doi.org/10.1042/bj20151227

10. Pattison, D. I. Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds / D. I. Pattison, M. J. Davies // Chem. Res. Toxicol. – 2001. – Vol. 14, N 10. – P. 1453–1464. https://doi.org/10.1021/tx0155451

11. Bhattacharya, M. Studying protein misfolding and aggregation by fluorescence spectroscopy / M. Bhattacharya, S. Mukhopadhyay // Reviews in Fluorescence 2015. – Baltimore, 2016. – Ch. 1. – P. 1–28. https://doi.org/10.1007/978-3-319-24609-3_1

12. Lakowicz, J. R. Principles of fluorescence spectroscopy / J. R. Lakowicz. – Baltimore, 2006. – Ch. 16. – P. 530–578.

13. Veen, B. S. Myeloperoxidase: molecular mechanism s of action and their relevance to human health and disease / B. S. van der Veen, M. P. J. de Winther, P. Heeringa // Antiox. and redox signaling. – 2009. – Vol. 11, N 11. – P. 2899–2937. https://doi.org/10.1089/ars.2009.2538

14. Structural response of human serum albumin to oxidation: biological buffer to local formation of hypochlorite / A. Del Giudice [et al.] // The J. of Phys. Chem. – 2016. – Vol. 120, N 48. – P. 12261–12271. https://doi.org/10.1021/acs.jpcb.6b08601

15. Petrônio, M. S. Effects of oxidation of lysozyme by hypohalous acids and haloamines on enzymatic activity and aggregation / M. S. Petrônio, V. F. Ximenes // Biochim. et Biophys. acta. – 2012. – Vol. 1824, N 10. – P. 1090–1096. https://doi.org/10.1016/j.bbapap.2012.06.013