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<article article-type="research-article" dtd-version="1.3" xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xml:lang="ru"><front><journal-meta><journal-id journal-id-type="publisher-id">dan</journal-id><journal-title-group><journal-title xml:lang="ru">Доклады Национальной академии наук Беларуси</journal-title><trans-title-group xml:lang="en"><trans-title>Doklady of the National Academy of Sciences of Belarus</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">1561-8323</issn><issn pub-type="epub">2524-2431</issn><publisher><publisher-name>The Republican Unitary Enterprise Publishing House "Belaruskaya Navuka"</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.29235/1561-8323-2022-66-1-43-54</article-id><article-id custom-type="elpub" pub-id-type="custom">dan-1037</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="ru"><subject>ХИМИЯ</subject></subj-group><subj-group subj-group-type="section-heading" xml:lang="en"><subject>CHEMISTRY</subject></subj-group></article-categories><title-group><article-title>Некоторые металлсвязывающие свойства рекомбинантного лактоферрина человека из молока трансгенных коз</article-title><trans-title-group xml:lang="en"><trans-title>Some metal binding properties of recombinant human lactoferrin from the milk of transgenic goats</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Семенов</surname><given-names>Д. А.</given-names></name><name name-style="western" xml:lang="en"><surname>Semenov</surname><given-names>D. A.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Семенов Дмитрий Александрович – научный сотрудник.</p><p>Ул. Купревича, 5/2, 220141, Минск</p></bio><bio xml:lang="en"><p>Semenov Dmitry A. – Researcher.</p><p>5/2, Kuprevich Str., 220141, Minsk</p></bio><email xlink:type="simple">dsemenov@iboch.by</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Куприенко</surname><given-names>О. С.</given-names></name><name name-style="western" xml:lang="en"><surname>Kuprienko</surname><given-names>O. S.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Куприенко Ольга Сергеевна – кандидат химических наук, старший научный сотрудник.</p><p>Ул. Купревича, 5/2, 220141, Минск</p></bio><bio xml:lang="en"><p>Kuprienko Olga S. – Ph. D. (Chemistry), Senior Researcher.</p><p>5/2, Kuprevich Str., 220141, Minsk</p></bio><email xlink:type="simple">kuprienko@iboch.by</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Вашкевич</surname><given-names>И. И.</given-names></name><name name-style="western" xml:lang="en"><surname>Vashkevich</surname><given-names>I. I.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Вашкевич Ирина Игнатьевна – кандидат химических наук, ведущий научный сотрудник.</p><p>Ул. Купревича, 5/2, 220141, Минск</p></bio><bio xml:lang="en"><p>Vashkevich Irina I. – Ph. D. (Chemistry), Leading Researcher.</p><p>5/2, Kuprevich Str., 220141, Minsk</p></bio><email xlink:type="simple">vashkevich@iboch.by</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Свиридов</surname><given-names>О. В.</given-names></name><name name-style="western" xml:lang="en"><surname>Sviridov</surname><given-names>O. V.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Свиридов Олег Васильевич – доктор химических наук, заведующий лабораторией.</p><p>Ул. Купревича, 5/2, 220141, Минск</p></bio><bio xml:lang="en"><p>Sviridov Oleg V. – D. Sc. (Chemistry), Head of the Laboratory.</p><p>5/2, Kuprevich Str., 220141, Minsk</p></bio><email xlink:type="simple">sviridov@iboch.by</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus</institution></aff><aff xml:lang="en"><institution>Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus</institution></aff></aff-alternatives><pub-date pub-type="collection"><year>2022</year></pub-date><pub-date pub-type="epub"><day>09</day><month>03</month><year>2022</year></pub-date><volume>66</volume><issue>1</issue><fpage>43</fpage><lpage>54</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Семенов Д.А., Куприенко О.С., Вашкевич И.И., Свиридов О.В., 2022</copyright-statement><copyright-year>2022</copyright-year><copyright-holder xml:lang="ru">Семенов Д.А., Куприенко О.С., Вашкевич И.И., Свиридов О.В.</copyright-holder><copyright-holder xml:lang="en">Semenov D.A., Kuprienko O.S., Vashkevich I.I., Sviridov O.V.</copyright-holder><license xml:lang="ru" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>Данная работа распространяется под лицензией Creative Commons Attribution 4.0.</license-p></license><license xml:lang="en" license-type="creative-commons-attribution" xlink:href="https://creativecommons.org/licenses/by/4.0/" xlink:type="simple"><license-p>This work is licensed under a Creative Commons Attribution 4.0 License.</license-p></license></permissions><self-uri xlink:href="https://doklady.belnauka.by/jour/article/view/1037">https://doklady.belnauka.by/jour/article/view/1037</self-uri><abstract><p>Методами спектрофотометрии, флуоресцентной спектроскопии и масс-спектрометрии показано, что человеческий рекомбинантный лактоферрин (рчЛФ), выделенный из молока трансгенных коз, способен связывать ионы железа и европия. Получены апо-форма рчЛФ, а также комплексы этого белка с Fe3+ и Eu3+, в которых степень насыщения рчЛФ металлом соответственно составила 76 и 22 %. Предложен способ регистрации общего или высвободившегося лантанида в системе, содержащей комплекс рчЛФ–Eu3+, при кислом или нейтральном значении рН и высоких или низких концентрациях хелатирующих агентов по интенсивности времяразрешенной флуоресценции.</p></abstract><trans-abstract xml:lang="en"><p>In this research, the ability of pure recombinant human lactoferrin (rhLF), originated from the milk of transgenic goats, to bind ferric and europium ions has been shown by the methods of spectrophotometry, fluorescent spectroscopy, and inductively coupled plasma mass spectrometry. The apo-form of rhLF and its complexes with Fe3+ or Eu3+ saturated in 76 or 22 %, respectively, were obtained. A method for detection of total or released (“free”) lanthanide at acidic or neutral pH and high or low concentrations of chelating agents by time-resolved fluorescence was proposed.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>рекомбинантный лактоферрин человека</kwd><kwd>связывание ионов железа и европия</kwd></kwd-group><kwd-group xml:lang="en"><kwd>recombinant human lactoferrin</kwd><kwd>ferric and europium ions binding</kwd></kwd-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Yantsevich A. V., Dzichenka Ya. V., Ivanchik A. V., Shapiro M. A., Trawkina M., Shkel T. V., Gilep A. A., Sergeev G. V., Usanov S. A. Proteomic analysis of contaminants in recombinant membrane hemeproteins expressed in E. coli and isolated by metal affinity chromatography. Applied Biochemistry and Microbiology, 2017, vol. 53, no. 2, pp. 173–186. https://doi.org/10.1134/s000368381702017x</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Пермяков, Е. А. Металлсвязывающие белки: структура, свойства, функции / Е. А. Пермяков. – М., 2012. – 544 с.</mixed-citation><mixed-citation xml:lang="en">Permyakov E. A. Metal binding proteins: structure, properties, functions. Moscow, 2012. 544 p. (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Baker H. M., Baker E. N. Lactoferrin and iron: structural and dynamic aspects of binding and release. BioMetals, 2004, vol. 17, no. 3, pp. 209–216. https://doi.org/10.1023/b:biom.0000027694.40260.70</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">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.</mixed-citation><mixed-citation xml:lang="en">Borzenkova N. V., Balabushevich N. G., Larionova N. I. Lactoferrin: physical and chemical properties, biological functions, delivery systems, pharmaceutical and nutraceutical preparations (review). Biofarmatsevticheskii zhurnal = Biopharmaceutical Journal, 2010, vol. 2, no. 3, pp. 3–19 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Metz-Boutigue M.-H., Jollès J., Mazurier J., Schoentgen F., Legrand D., Spik G., Montreuil J., Jollès P. Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins. European Journal of Biochemistry, 1984, vol. 145, no. 3, pp. 659–676. https://doi.org/10.1111/j.1432-1033.1984.tb08607.x</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Baker E. N., Baker H. M. A structural framework for understanding the multifunctional character of lactoferrin. Biochimie, 2009, vol. 91, no. 1, pp. 3–10. https://doi.org/10.1016/j.biochi.2008.05.006</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Ward P. P., Zhou X., Conneely O. M. Cooperative interactions between the amino- and carboxyl-terminal lobes contribute to the unique iron-binding stability of lactoferrin. Journal of Biological Chemistry. Protein Chemistry and Structure, 1996, vol. 271, no. 22, pp. 12790–12794. https://doi.org/10.1074/jbc.271.22.12790</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Goldman I. L., Georgieva S. G., Gurskiy Ya. G., Krasnov A. N., Deykin A. V., Popov A. N., Ermolkevich T. G., Budzevich A. I., Chernousov A. D., Sadchikova E. R. Production of human lactoferrin in animal milk. Biochemistry and Cell Biology, 2012, vol. 90, no. 3, pp. 513–519. https://doi.org/10.1139/o11-088</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">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.</mixed-citation><mixed-citation xml:lang="en">Lukashevich V. S., Budzevich A. I., Semak I. V., Kuznetsova V. N., Malyushkova E. V., Pyzh A. E., Novakovskaya S. A., Rudnichenko J. A., Popkov N. A., Ivashkevich O. A., Zalutsky I. V. Production of recombinant human lactoferrin from the milk of goat-producers and its physiological effects. Doklady Natsional’noi akademii nauk Belarusi = Doklady of the National Academy of Sciences of Belarus, 2016, vol. 60, no. 1, pp. 72–81 (in Russian).</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Semenov D. A., Vashkevich I. I., Sviridov O. V. New immunoassay systems based on recombinant human lactoferrin. Doklady Natsional’noi akademii nauk Belarusi = Doklady of the National Academy of Sciences of Belarus, 2021, vol. 65, no. 3, pp. 290–302 (in Russian). https://doi.org/10.29235/1561-8323-2021-65-3-290-302</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Majka G., Śpiewak K., Kurpiewska K., Heczko P., Stochel G., Strus M., Brindell M. A high-throughput method for the quantification of iron saturation in lactoferrin preparations. Analytical and Bioanalytical Chemistry, 2013, vol. 405, no. 15, pp. 5191–5200. https://doi.org/10.1007/s00216-013-6943-9</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry, 1967, vol. 6, no. 7, pp. 1948–1954. https://doi.org/10.1021/bi00859a010</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Nuijens J. H., van Berkel P. H. C., Geerts M. E. J., Hartevelt P. P., de Boer H. A., van Veen H. A., Pieper F. R. Characterization of recombinant human lactoferrin secreted in milk of transgenic mice. Journal of Biological Chemistry. Protein Chemistry and Structure, 1997, vol. 272, no. 13, pp. 8802–8807. https://doi.org/10.1074/jbc.272.13.8802</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Hu F., Pan F., Sawano Y., Makino T., Kakehi Y., Komiyama M., Kawakami H., Tanokura M. Studies of the structure of multiferric ion-bound lactoferrin: a new antianemic edible material. International Dairy Journal, 2008, vol. 18, no. 10–11, pp. 1051–1056. https://doi.org/10.1016/j.idairyj.2008.05.003</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">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. Biochemistry, 1971, vol. 10, no. 15, pp. 2838–2843. https://doi.org/10.1021/bi00791a006</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Abdollahi S., Harris W. R., Riehl J. P. Application of circularly polarized luminescence spectroscopy to Tb(III) and Eu(III) complexes of transferrins. Journal of Physical Chemistry, 1996, vol. 100, no. 5, pp. 1950–1956. https://doi.org/10.1021/jp952044d</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Rodzik A., Pomastowski P., Sagandykova G. N., Buszewski B. Interactions of whey proteins with metal ions. International Journal of Molecular Sciences, 2020, vol. 21, no. 6, art. 2156. https://doi.org/10.3390/ijms21062156</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Lehrer S. S. Fluorescence and absorption studies of the binding of copper and iron to transferrin. Journal of Biological Chemistry, 1969, vol. 244, no. 13, pp. 3613–3617. https://doi.org/10.1016/s0021-9258(18)83413-5</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Horrocks W. D., Sudnick D. R. Lanthanide ion luminescence probes of the structure of biological macromolecules. Accounts of Chemical Research, 1981, vol. 14, no. 12, pp. 384–392. https://doi.org/10.1021/ar00072a004</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">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</mixed-citation><mixed-citation xml:lang="en">Hemmilä I., Dakubu S., Mukkala V.-M., Siitari H., Lövgren T. Europium as a label in time-resolved immunofluorometric assays. Analytical Biochemistry, 1984, vol. 137, no. 2, pp. 335–343. https://doi.org/10.1016/0003-2697(84)90095-2</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">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.</mixed-citation><mixed-citation xml:lang="en">Yang B., Li Y. Binding constants for terbium (III) with chicken apoovotransferrin. Chemical Research in Chinese Universities, 2001, vol. 17, no. 1, pp. 6–13.</mixed-citation></citation-alternatives></ref></ref-list><fn-group><fn fn-type="conflict"><p>The authors declare that there are no conflicts of interest present.</p></fn></fn-group></back></article>
