1. Proteomic analysis of contaminants in recombinant membrane hemeproteins expressed in E. coli and isolated by metal affinity chromatography / A. V. Yantsevich [et al.] // Applied Biochemistry and Microbiology. – 2017. – Vol. 53, N 2. – P. 173–186. https://doi.org/10.1134/s000368381702017x

2. Пермяков, Е. А. Металлсвязывающие белки: структура, свойства, функции / Е. А. Пермяков. – М., 2012. – 544 с.

3. Baker, H. M. Lactoferrin and iron: structural and dynamic aspects of binding and release / H. M. Baker, E. N. Baker // BioMetals. – 2004. – Vol. 17, N 3. – P. 209–216. https://doi.org/10.1023/b:biom.0000027694.40260.70

4. Борзенкова, Н. В. Лактоферрин: физико-химические свойства, биологические функции, системы доставки, лекарственные препараты и биологически активные добавки (обзор) / Н. В. Борзенкова, Н. Г. Балабушевич, Н. И. Ларионова // Биофармацевт. журн. – 2010. – Т. 2, № 3. – С. 3–19.

5. Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins / M.-H. Metz-Boutigue [et al.] // European Journal of Biochemistry. – 1984. – Vol. 145, N 3. – P. 659–676. https://doi.org/10.1111/j.1432-1033.1984.tb08607.x

6. Baker, E. N. A structural framework for understanding the multifunctional character of lactoferrin / E. N. Baker, H. M. Baker // Biochimie. – 2009. – Vol. 91, N 1. – P. 3–10. https://doi.org/10.1016/j.biochi.2008.05.006

7. Ward, P. P. Cooperative interactions between the amino- and carboxyl-terminal lobes contribute to the unique ironbinding stability of lactoferrin / P. P. Ward, X. Zhou, O. M. Conneely // Journal of Biological Chemistry. Protein Chemistry and Structure. – 1996. – Vol. 271, N 22. – P. 12790–12794. https://doi.org/10.1074/jbc.271.22.12790

8. Production of human lactoferrin in animal milk / I. L. Goldman [et al.] // Biochemistry and Cell Biology. – 2012. – Vol. 90, N 3. – P. 513–519. https://doi.org/10.1139/o11-088

9. Получение рекомбинантного лактоферрина человека из молока коз-продуцентов и его физиологические эффекты / В. С. Лукашевич [и др.] // Докл. Нац. акад. наук Беларуси. – 2016. – Т. 60, № 1. – С. 72–81.

10. Семенов, Д. А. Новые иммуноаналитические системы на основе рекомбинантного лактоферрина человека / Д. А. Семенов, И. И. Вашкевич, О. В. Свиридов // Докл. Нац. акад. наук Беларуси. – 2021. – Т. 65, № 3. – С. 290–302. https://doi.org/10.29235/1561-8323-2021-65-3-290-302

11. A high-throughput method for the quantification of iron saturation in lactoferrin preparations / G. Majka [et al.] // Analytical and Bioanalytical Chemistry. – 2013. – Vol. 405, N 15. – P. 5191–5200. https://doi.org/10.1007/s00216-013-6943-9

12. Edelhoch, H. Spectroscopic determination of tryptophan and tyrosine in proteins / H. Edelhoch // Biochemistry. – 1967. – Vol. 6, N 7. – P. 1948–1954. https://doi.org/10.1021/bi00859a010

13. Characterization of recombinant human lactoferrin secreted in milk of transgenic mice / J. H. Nuijens [et al.] // Journal of Biological Chemistry. Protein Chemistry and Structure. – 1997. – Vol. 272, N 13. – P. 8802–8807. https://doi.org/10.1074/jbc.272.13.8802

14. Studies of the structure of multiferric ion-bound lactoferrin: a new antianemic edible material / F. Hu [et al.] // International Dairy Journal. – 2008. – Vol. 18, N 10–11. – P. 1051–1056. https://doi.org/10.1016/j.idairyj.2008.05.003

15. Luk, C. K. Study of the nature of the metal-binding sites and estimate of the distance between the metal-binding sites in transferrin using trivalent lanthanide ions as fluorescent probes / C. K. Luk // Biochemistry. – 1971. – Vol. 10, N 15. – P. 2838–2843. https://doi.org/10.1021/bi00791a006

16. Abdollahi, S. Application of circularly polarized luminescence spectroscopy to Tb(III) and Eu(III) complexes of transferrins / S. Abdollahi, W. R. Harris, J. P. Riehl // Journal of Physical Chemistry. – 1996. – Vol. 100, N 5. – P. 1950–1956. https://doi.org/10.1021/jp952044d

17. Interactions of whey proteins with metal ions / A. Rodzik [et al.] // International Journal of Molecular Sciences. – 2020. – Vol. 21, N 6. – Art. 2156. https://doi.org/10.3390/ijms21062156

18. Lehrer, S. S. Fluorescence and absorption studies of the binding of copper and iron to transferrin / S. S. Lehrer //Journal of Biological Chemistry. – 1969. – Vol. 244, N 13. – P. 3613–3617. https://doi.org/10.1016/s0021-9258(18)83413-5

19. Horrocks, W. D. Lanthanide ion luminescence probes of the structure of biological macromolecules / W. D. Horrocks, D. R. Sudnick // Accounts of Chemical Research. – 1981. – Vol. 14, N 12. – P. 384–392. https://doi.org/10.1021/ar00072a004

20. Europium as a label in time-resolved immunofluorometric assays / I. Hemmilä [et al.] // Analytical Biochemistry. – 1984. – Vol. 137, N 2. – P. 335–343. https://doi.org/10.1016/0003-2697(84)90095-2

21. Yang, B. Binding constants for terbium (III) with chicken apoovotransferrin / B. Yang, Y. Li // Chemical Research in Chinese Universities. – 2001. – Vol. 17, N 1. – P. 6–13.