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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="en"><front><journal-meta><journal-id journal-id-type="publisher-id">meat</journal-id><journal-title-group><journal-title xml:lang="en">Theory and practice of meat processing</journal-title><trans-title-group xml:lang="ru"><trans-title>Теория и практика переработки мяса</trans-title></trans-title-group></journal-title-group><issn pub-type="ppub">2414-438X</issn><issn pub-type="epub">2414-441X</issn><publisher><publisher-name>ФГБНУ «Федеральный научный центр пищевых систем им. В.М. Горбатова» РАН</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="doi">10.21323/2414-438X-2022-7-1-35-41</article-id><article-id custom-type="elpub" pub-id-type="custom">meat-208</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>Статьи</subject></subj-group></article-categories><title-group><article-title>Comparison of the proteomic profile of pork byproducts during their storage</article-title><trans-title-group xml:lang="ru"><trans-title>Comparison of the proteomic profile of pork byproducts during their storage</trans-title></trans-title-group></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-0211-8171</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Akhremko</surname><given-names>A. G.</given-names></name><name name-style="western" xml:lang="en"><surname>Akhremko</surname><given-names>A. G.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Moscow</p></bio><bio xml:lang="en"><p>Anastasia G. Akhremko, Junior Researcher, Experimental-clinical research laboratory of bioactive substances of animal origin</p><p>26, Talalikhina str., 109316, Moscow</p><p>Tel.: +7–915–237–94–97</p></bio><email xlink:type="simple">a.ahremko@fncps.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0001-7625-3838</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Nasonova</surname><given-names>V. V.</given-names></name><name name-style="western" xml:lang="en"><surname>Nasonova</surname><given-names>V. V.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Moscow</p></bio><bio xml:lang="en"><p>Victoria V. Nasonova, Candidate of technical sciences, Head of Department of Applied Scientific and Technological Development</p><p>26, Talalikhina str., 109316, Moscow</p><p>Tel.: +7–495–676–95–11 (307)</p></bio><email xlink:type="simple">v.nasonova@fncps.ru</email><xref ref-type="aff" rid="aff-1"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0003-4544-4433</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Spirina</surname><given-names>M. E.</given-names></name><name name-style="western" xml:lang="en"><surname>Spirina</surname><given-names>M. E.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Moscow</p></bio><bio xml:lang="en"><p>Maria E. Spirina, bachelor</p><p>49, Timiryazevskaya str., 49, 127550, Moscow</p><p>Tel.: + 7–977–541–27–97</p></bio><email xlink:type="simple">mspirina88@gmail.com</email><xref ref-type="aff" rid="aff-2"/></contrib><contrib contrib-type="author" corresp="yes"><contrib-id contrib-id-type="orcid">https://orcid.org/0000-0002-6876-8847</contrib-id><name-alternatives><name name-style="eastern" xml:lang="ru"><surname>Godswill</surname><given-names>N. N.</given-names></name><name name-style="western" xml:lang="en"><surname>Godswill</surname><given-names>N. N.</given-names></name></name-alternatives><bio xml:lang="ru"><p>Yaounde</p></bio><bio xml:lang="en"><p>Ntsomboh N. Godswill, Doctor, PhD, Senior Lecturer, Department of Plant Biology, Faculty of Science; Head of the Department of Agricultural Biotechnology; Member </p><p>P.O. Box 812, Yaounde</p><p>Tel.: +237-679-941-910</p></bio><email xlink:type="simple">ntsomboh.godswill@facsciences-uy1.cm</email><xref ref-type="aff" rid="aff-3"/></contrib></contrib-group><aff-alternatives id="aff-1"><aff xml:lang="ru"><institution>V.M. Gorbatov Federal Research Center for Food Systems</institution><country>Россия</country></aff><aff xml:lang="en"><institution>V.M. Gorbatov Federal Research Center for Food Systems</institution><country>Russian Federation</country></aff></aff-alternatives><aff-alternatives id="aff-2"><aff xml:lang="ru"><institution>Russian State Agrarian University — Moscow Timiryazev Agricultural Academy</institution><country>Россия</country></aff><aff xml:lang="en"><institution>Russian State Agrarian University — Moscow Timiryazev Agricultural Academy</institution><country>Russian Federation</country></aff></aff-alternatives><aff-alternatives id="aff-3"><aff xml:lang="ru"><institution>University Yaounde I; FINISTECH; Cameroon Academy of Young Scientists</institution><country>Камерун</country></aff><aff xml:lang="en"><institution>University Yaounde I; FINISTECH; Cameroon Academy of Young Scientists</institution><country>Cameroon</country></aff></aff-alternatives><pub-date pub-type="collection"><year>2022</year></pub-date><pub-date pub-type="epub"><day>12</day><month>04</month><year>2022</year></pub-date><volume>7</volume><issue>1</issue><fpage>35</fpage><lpage>41</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Akhremko A.G., Nasonova V.V., Spirina M.E., Godswill N.N., 2022</copyright-statement><copyright-year>2022</copyright-year><copyright-holder xml:lang="ru">Akhremko A.G., Nasonova V.V., Spirina M.E., Godswill N.N.</copyright-holder><copyright-holder xml:lang="en">Akhremko A.G., Nasonova V.V., Spirina M.E., Godswill N.N.</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://www.meatjournal.ru/jour/article/view/208">https://www.meatjournal.ru/jour/article/view/208</self-uri><abstract><p>In this article, the proteomic profiles of pork by-products (snout, tongue, liver, kidney, spleen) were studied by comparative method on the first day and the fifth day of their storage. Two-dimensional electrophoresis according to O’Farrell was used for the aims of this article, while the results were further processed in ImageMaster software. Proteomic maps of by-products showed clear changes in protein composition after visualization and images analysis. There was a decrease and increase in manifestation intensity of some proteins. The study of the obtained electrophoregrams with the help of references resources allowed identifying various compounds in the by-products. 9 protein fractions with various intensity of manifestation were found on the day 1st and 5th. On the 1st day the following substances were intensively manifested: in the liver — glutathione peroxidase 4 (22.3 kDa), LEAP-2 (8.8 kDa); in the kidneys — quinone oxidoreductase (34.9 kDa); in the spleen — glycoprotein CD59 (13.7 kDa), in the patch — protein flint (49.07 kDa). It is noted that these proteins play their role in stopping certain processes in cells, like oxidation, microbial activity, and accumulation of toxic substances. These processes can worsen the quality of raw materials, and further lead to spoilage of the food product. On the 5th day of storage the highest intensity of manifestation of glyceraldehyde-3-phosphate dehydrogenase (35.8 kDa) in the liver was observed; superoxide dismutase [Cu-Zn] (15.8 kDa) was noted in the kidneys, colony-stimulating factor (16.2 kDa) was observed in the spleen and glutaredoxin –1 (11.8 kDa) in the tongue. In its turn, on the fifth day these chemical processes manifested themselves more intensely, as the fatty acids and glucose broke down. To obtain more accurate results, the proteins were compared by their volume. Among the identified fractions the highest expression was observed in LEAP 2 (8.8 kDa) on the first day, and in glyceraldehyde-3-phosphate dehydrogenase (35.8 kDa) on the fifth day. The least change in the intensity of manifestation was noted for superoxide dismutase [Cu-Zn] (15.8 kDa), which volume increased during storage by 13% for 5 days. The analysis of the obtained electrophoregrams allowed identifying various compounds, tracing the changes in the qualitative composition of protein in by-products during various periods of their storage. The obtained data demonstrate the transformation of protein molecules during storage, which makes it possible to determine the changes and quality of the food products.</p></abstract><trans-abstract xml:lang="ru"><p>In this article, the proteomic profiles of pork by-products (snout, tongue, liver, kidney, spleen) were studied by comparative method on the first day and the fifth day of their storage. Two-dimensional electrophoresis according to O’Farrell was used for the aims of this article, while the results were further processed in ImageMaster software. Proteomic maps of by-products showed clear changes in protein composition after visualization and images analysis. There was a decrease and increase in manifestation intensity of some proteins. The study of the obtained electrophoregrams with the help of references resources allowed identifying various compounds in the by-products. 9 protein fractions with various intensity of manifestation were found on the day 1st and 5th. On the 1st day the following substances were intensively manifested: in the liver — glutathione peroxidase 4 (22.3 kDa), LEAP-2 (8.8 kDa); in the kidneys — quinone oxidoreductase (34.9 kDa); in the spleen — glycoprotein CD59 (13.7 kDa), in the patch — protein flint (49.07 kDa). It is noted that these proteins play their role in stopping certain processes in cells, like oxidation, microbial activity, and accumulation of toxic substances. These processes can worsen the quality of raw materials, and further lead to spoilage of the food product. On the 5th day of storage the highest intensity of manifestation of glyceraldehyde-3-phosphate dehydrogenase (35.8 kDa) in the liver was observed; superoxide dismutase [Cu-Zn] (15.8 kDa) was noted in the kidneys, colony-stimulating factor (16.2 kDa) was observed in the spleen and glutaredoxin –1 (11.8 kDa) in the tongue. In its turn, on the fifth day these chemical processes manifested themselves more intensely, as the fatty acids and glucose broke down. To obtain more accurate results, the proteins were compared by their volume. Among the identified fractions the highest expression was observed in LEAP 2 (8.8 kDa) on the first day, and in glyceraldehyde-3-phosphate dehydrogenase (35.8 kDa) on the fifth day. The least change in the intensity of manifestation was noted for superoxide dismutase [Cu-Zn] (15.8 kDa), which volume increased during storage by 13% for 5 days. The analysis of the obtained electrophoregrams allowed identifying various compounds, tracing the changes in the qualitative composition of protein in by-products during various periods of their storage. The obtained data demonstrate the transformation of protein molecules during storage, which makes it possible to determine the changes and quality of the food products.</p></trans-abstract><kwd-group xml:lang="ru"><kwd>by-products</kwd><kwd>pork</kwd><kwd>2-DE</kwd><kwd>proteomics</kwd><kwd>by-products proteins</kwd><kwd>liver</kwd><kwd>kidneys</kwd></kwd-group><kwd-group xml:lang="en"><kwd>by-products</kwd><kwd>pork</kwd><kwd>2-DE</kwd><kwd>proteomics</kwd><kwd>by-products proteins</kwd><kwd>liver</kwd><kwd>kidneys</kwd></kwd-group><funding-group><funding-statement xml:lang="en">The article was published as part of the research topic No. FNEN-2019–0008 of the state assignment of the V. M. Gorbatov Federal Research Center for Food Systems of RAS.</funding-statement></funding-group></article-meta></front><back><ref-list><title>References</title><ref id="cit1"><label>1</label><citation-alternatives><mixed-citation xml:lang="ru">Nasonova, V.V. (2018). Perspective ways the use of byproducts. Theory and practice of meat processing, 3(3), 64-73. https://doi.org/10.21323/2414-438X-2018-3-3-64-73 (In Russian)</mixed-citation><mixed-citation xml:lang="en">Nasonova, V.V. (2018). Perspective ways the use of byproducts. Theory and practice of meat processing, 3(3), 64-73. https://doi.org/10.21323/2414-438X-2018-3-3-64-73 (In Russian)</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Kabulov B., Kassymov S., Moldabayeva Zh., Rebezov M., Zinina O., Chernyshenko Yu. et al. (2020). Developing the formulation and method of production of meat frankfurters with protein supplement from meat by-products. EurAsian Journal of BioSciences, 14(1), 213-218.</mixed-citation><mixed-citation xml:lang="en">Kabulov B., Kassymov S., Moldabayeva Zh., Rebezov M., Zinina O., Chernyshenko Yu. et al. (2020). Developing the formulation and method of production of meat frankfurters with protein supplement from meat by-products. EurAsian Journal of BioSciences, 14(1), 213-218.</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Babicz, M., Kropiwiec, K., Szyndler-Nedza, M., Skrzypczak, E. (2018). The physicochemical properties of by-product from Puławska gilts in relation to carcass meatiness. Annals of Animal Science, 18(1), 239-249. https://doi.org/10.1515/aoas-2017-0018</mixed-citation><mixed-citation xml:lang="en">Babicz, M., Kropiwiec, K., Szyndler-Nedza, M., Skrzypczak, E. (2018). The physicochemical properties of by-product from Puławska gilts in relation to carcass meatiness. Annals of Animal Science, 18(1), 239-249. https://doi.org/10.1515/aoas-2017-0018</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Biel, W., Czerniawska-Piątkowska, E., Kowalczyk, A. (2019). By-product Chemical Composition from Veal, Beef, and Lamb Maintained in Organic Production Systems. Animals, 9(8), Article 489. https://doi.org/10.3390/ani9080489</mixed-citation><mixed-citation xml:lang="en">Biel, W., Czerniawska-Piątkowska, E., Kowalczyk, A. (2019). By-product Chemical Composition from Veal, Beef, and Lamb Maintained in Organic Production Systems. Animals, 9(8), Article 489. https://doi.org/10.3390/ani9080489</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Alao, B. O., Falowo, A. B., Chulayo, A., Muchenje, V. (2017). The potential of animal by-products in food systems: Production, prospects and challenges. Sustainability, 9(7), Article 1089. https://doi.org/10.3390/su9071089</mixed-citation><mixed-citation xml:lang="en">Alao, B. O., Falowo, A. B., Chulayo, A., Muchenje, V. (2017). The potential of animal by-products in food systems: Production, prospects and challenges. Sustainability, 9(7), Article 1089. https://doi.org/10.3390/su9071089</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Babicz, M., Kasprzyk, A., Kropiwiec-Domańska, K. (2018). Influence of the sex and type of tissue on the basic chemical composition and the content of minerals in the sirloin and by-product of fattener pigs. Canadian Journal of Animal Science, 99(2), 343- 348. https://doi.org/10.1139/cjas-2018-0085</mixed-citation><mixed-citation xml:lang="en">Babicz, M., Kasprzyk, A., Kropiwiec-Domańska, K. (2018). Influence of the sex and type of tissue on the basic chemical composition and the content of minerals in the sirloin and by-product of fattener pigs. Canadian Journal of Animal Science, 99(2), 343- 348. https://doi.org/10.1139/cjas-2018-0085</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Abdilova, G., Rebezov, M., Nesterenko, A., Safronov, S., Knysh, I., Ivanova, I. et al. (2021). Characteristics of meat by-products: nutritional and biological value. International Journal of Modern Agriculture, 10(2), 3895-3904.</mixed-citation><mixed-citation xml:lang="en">Abdilova, G., Rebezov, M., Nesterenko, A., Safronov, S., Knysh, I., Ivanova, I. et al. (2021). Characteristics of meat by-products: nutritional and biological value. International Journal of Modern Agriculture, 10(2), 3895-3904.</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Kupaeva, N.V., Kotenkova, Е.А. (2019). Analysis of the antioxidant capacity of farm animal raw materials. Vsyo o myase, 5, 34-37. https://doi.org/10.21323/2071-2499-2019-5-34-37 (In Russian)</mixed-citation><mixed-citation xml:lang="en">Kupaeva, N.V., Kotenkova, Е.А. (2019). Analysis of the antioxidant capacity of farm animal raw materials. Vsyo o myase, 5, 34-37. https://doi.org/10.21323/2071-2499-2019-5-34-37 (In Russian)</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Kotenkova, E. A., Kupaeva, N. V. (2020). Assessment of the antioxidant potential of some porcine by-products from slaughter. Food Industry, 7, 34-40. https://doi.org/10.24411/0235-2486-2020-10073 (In Russian)</mixed-citation><mixed-citation xml:lang="en">Kotenkova, E. A., Kupaeva, N. V. (2020). Assessment of the antioxidant potential of some porcine by-products from slaughter. Food Industry, 7, 34-40. https://doi.org/10.24411/0235-2486-2020-10073 (In Russian)</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Аkhremko, A., Vasilevskaya, E., Fedulova, L. (2020). Adaptation of two-dimensional electrophoresis for muscule tissue analysis. Potravinarstvo Slovak Journal of Food Sciences, 14(1), 595- 601. https://doi.org/10.5219/1380</mixed-citation><mixed-citation xml:lang="en">Аkhremko, A., Vasilevskaya, E., Fedulova, L. (2020). Adaptation of two-dimensional electrophoresis for muscule tissue analysis. Potravinarstvo Slovak Journal of Food Sciences, 14(1), 595- 601. https://doi.org/10.5219/1380</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Banerjee, R., Maheswarappa, N.B., Mohan, K., Biswas, S., Batabyal, S. (2022). Proteomic technologies and their application for ensuring meat quality, safety and Authenticity. Current Proteomics, 19(2), 128-141. https://doi.org/10.2174/1570164618666210114113306</mixed-citation><mixed-citation xml:lang="en">Banerjee, R., Maheswarappa, N.B., Mohan, K., Biswas, S., Batabyal, S. (2022). Proteomic technologies and their application for ensuring meat quality, safety and Authenticity. Current Proteomics, 19(2), 128-141. https://doi.org/10.2174/1570164618666210114113306</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Chernukha, I.M., Akhremko, A.G. (2018). Application of proteomic tools: the autolytic changes of pork muscular tissue. Theory and Practice of Meat Processing, 3(4), 32-37. https://doi.org/10.21323/2414-438X-2018-3-4-32-37 (In Russian)</mixed-citation><mixed-citation xml:lang="en">Chernukha, I.M., Akhremko, A.G. (2018). Application of proteomic tools: the autolytic changes of pork muscular tissue. Theory and Practice of Meat Processing, 3(4), 32-37. https://doi.org/10.21323/2414-438X-2018-3-4-32-37 (In Russian)</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Zamaratskaia, G., Li, S. (2017). Proteomics in meat science — current status and future perspective. Theory and Practice of Meat Processing, 2(1), 18-26. https://doi.org/10.21323/2414-438X-2017-2-1-18-26 (In Russian)</mixed-citation><mixed-citation xml:lang="en">Zamaratskaia, G., Li, S. (2017). Proteomics in meat science — current status and future perspective. Theory and Practice of Meat Processing, 2(1), 18-26. https://doi.org/10.21323/2414-438X-2017-2-1-18-26 (In Russian)</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Aryuzina, M.A., Vetrova, E.S. (2021). Application of two-dimensional electrophoresis in the study of blood plasma of biomodels. Food Systems, 4(3S), 8-11. https://doi.org/10.21323/2618-9771-2021-4-3S-8-11 (In Russian)</mixed-citation><mixed-citation xml:lang="en">Aryuzina, M.A., Vetrova, E.S. (2021). Application of two-dimensional electrophoresis in the study of blood plasma of biomodels. Food Systems, 4(3S), 8-11. https://doi.org/10.21323/2618-9771-2021-4-3S-8-11 (In Russian)</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Ahremko, A.G. (2019). Application of two-dimensional electrophoresis method for assessing meat products composition on model stuffing example. Vsyo o myase, 3, 46-48. https://doi.org/10.21323/2071-2499-2019-3-46-48 (In Russian)</mixed-citation><mixed-citation xml:lang="en">Ahremko, A.G. (2019). Application of two-dimensional electrophoresis method for assessing meat products composition on model stuffing example. Vsyo o myase, 3, 46-48. https://doi.org/10.21323/2071-2499-2019-3-46-48 (In Russian)</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Akhremko, A. G., Vetrova, E. S. (2021). Comparative proteomic study of pig muscle proteins during growth and development of an animal. Theory and Practice of Meat Processing, 6(4), 320-327. https://doi.org/10.21323/2414-438X-2021-6-4-320-327</mixed-citation><mixed-citation xml:lang="en">Akhremko, A. G., Vetrova, E. S. (2021). Comparative proteomic study of pig muscle proteins during growth and development of an animal. Theory and Practice of Meat Processing, 6(4), 320-327. https://doi.org/10.21323/2414-438X-2021-6-4-320-327</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Data base “UniProt”. Retrieved from https://www.uniprot.org/. Accessed December 23, 2021</mixed-citation><mixed-citation xml:lang="en">Data base “UniProt”. Retrieved from https://www.uniprot.org/. Accessed December 23, 2021</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Cozza, G., Rossetto, M., Bosello-Travain, V., Maiorino, M., Roveri, A., Toppo, S. et al. (2017). Glutathione peroxidase 4-catalyzed reduction of lipid hydroperoxides in membranes: the polar head of membrane phospholipids binds the enzyme and addresses the fatty acid hydroperoxide group toward the redox center. Free Radical Biology and Medicine, 112, 1-11. https://doi.org/10.1016/j.freeradbiomed.2017.07.010</mixed-citation><mixed-citation xml:lang="en">Cozza, G., Rossetto, M., Bosello-Travain, V., Maiorino, M., Roveri, A., Toppo, S. et al. (2017). Glutathione peroxidase 4-catalyzed reduction of lipid hydroperoxides in membranes: the polar head of membrane phospholipids binds the enzyme and addresses the fatty acid hydroperoxide group toward the redox center. Free Radical Biology and Medicine, 112, 1-11. https://doi.org/10.1016/j.freeradbiomed.2017.07.010</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Hong, Y., Truong, A. D., Lee, J., Lee, K., Kim, G. -B., Heo, K. -N. et al. (2019). Identification of duck liver-expressed antimicrobial peptide 2 and characterization of its bactericidal activity. AsianAustralasian Journal of Animal Sciences, 32(7), 1052-1061. https://doi.org/10.5713/ajas.18.0571</mixed-citation><mixed-citation xml:lang="en">Hong, Y., Truong, A. D., Lee, J., Lee, K., Kim, G. -B., Heo, K. -N. et al. (2019). Identification of duck liver-expressed antimicrobial peptide 2 and characterization of its bactericidal activity. AsianAustralasian Journal of Animal Sciences, 32(7), 1052-1061. https://doi.org/10.5713/ajas.18.0571</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Pey, A. L., Megarity, C. F., Timson, D. J. (2019). NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just enough mobility, in just the right places. Bioscience Reports, 39(1), Article BSR20180459. https://doi.org/10.1042/BSR20180459</mixed-citation><mixed-citation xml:lang="en">Pey, A. L., Megarity, C. F., Timson, D. J. (2019). NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just enough mobility, in just the right places. Bioscience Reports, 39(1), Article BSR20180459. https://doi.org/10.1042/BSR20180459</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Das, N., Anand, D., Biswas, B., Kumari, D., Gandhi, M. (2019). The membrane complement regulatory protein CD59 and its association with rheumatoid arthritis and systemic lupus erythematosus. Current Medicine Research and Practice, 9(5), 182-188. https://doi.org/10.1016/j.cmrp.2019.07.013</mixed-citation><mixed-citation xml:lang="en">Das, N., Anand, D., Biswas, B., Kumari, D., Gandhi, M. (2019). The membrane complement regulatory protein CD59 and its association with rheumatoid arthritis and systemic lupus erythematosus. Current Medicine Research and Practice, 9(5), 182-188. https://doi.org/10.1016/j.cmrp.2019.07.013</mixed-citation></citation-alternatives></ref><ref id="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Sumia, I., Pierani, A., Causeret, F. (2019). Kremen1-induced cell death is regulated by homo-and heterodimerization. Cell Death Discovery, 5(1), Article 91. https://doi.org/10.1038/s41420-019-0175-5</mixed-citation><mixed-citation xml:lang="en">Sumia, I., Pierani, A., Causeret, F. (2019). Kremen1-induced cell death is regulated by homo-and heterodimerization. Cell Death Discovery, 5(1), Article 91. https://doi.org/10.1038/s41420-019-0175-5</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Sirover, M. A. (2021). The role of posttranslational modification in moonlighting glyceraldehyde-3-phosphate dehydrogenase structure and function. Amino Acids, 53(4), 507-515. https://doi.org/10.1007/s00726-021-02959-z</mixed-citation><mixed-citation xml:lang="en">Sirover, M. A. (2021). The role of posttranslational modification in moonlighting glyceraldehyde-3-phosphate dehydrogenase structure and function. Amino Acids, 53(4), 507-515. https://doi.org/10.1007/s00726-021-02959-z</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Bakavayev, S., Chetrit, N., Zvagelsky, T., Mansour, R., Vyazmensky, M., Barak, Z. et al. (2019). Cu/Zn-superoxide dismutase and wild-type like fALS SOD1 mutants produce cytotoxic quantities of H 2O2 via cysteine-dependent redox short-circuit. Scientific Reports, 9(1), Article 10826. https://doi.org/10.1038/s41598-019-47326-x</mixed-citation><mixed-citation xml:lang="en">Bakavayev, S., Chetrit, N., Zvagelsky, T., Mansour, R., Vyazmensky, M., Barak, Z. et al. (2019). Cu/Zn-superoxide dismutase and wild-type like fALS SOD1 mutants produce cytotoxic quantities of H 2O2 via cysteine-dependent redox short-circuit. Scientific Reports, 9(1), Article 10826. https://doi.org/10.1038/s41598-019-47326-x</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Wessendarp, M., Watanabe-Chailland, M., Liu, S., Stankiewicz, T., Ma, Y., Kasam, R.K. et al. (2022). Role of GM-CSF in regulating metabolism and mitochondrial functions critical to macrophage proliferation. Mitochondrion, 62, 85-101. https://doi.org/10.1101/2021.02.10.430444</mixed-citation><mixed-citation xml:lang="en">Wessendarp, M., Watanabe-Chailland, M., Liu, S., Stankiewicz, T., Ma, Y., Kasam, R.K. et al. (2022). Role of GM-CSF in regulating metabolism and mitochondrial functions critical to macrophage proliferation. Mitochondrion, 62, 85-101. https://doi.org/10.1101/2021.02.10.430444</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Burns, M., Rizvi, S.H.M., Tsukahara, Y., Pimentel, D. R. Luptak, I., Hamburg N. M. et al. (2020). Role of glutaredoxin-1 and glutathionylation in cardiovascular diseases. International Journal of Molecular Sciences, 21(18), 1-17, Article 6803. https://doi.org/10.3390/ijms21186803</mixed-citation><mixed-citation xml:lang="en">Burns, M., Rizvi, S.H.M., Tsukahara, Y., Pimentel, D. R. Luptak, I., Hamburg N. M. et al. (2020). Role of glutaredoxin-1 and glutathionylation in cardiovascular diseases. International Journal of Molecular Sciences, 21(18), 1-17, Article 6803. https://doi.org/10.3390/ijms21186803</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>
