<?xml version="1.0" encoding="UTF-8"?>
<!DOCTYPE article PUBLIC "-//NLM//DTD JATS (Z39.96) Journal Publishing DTD v1.3 20210610//EN" "JATS-journalpublishing1-3.dtd">
<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-2021-6-4-320-327</article-id><article-id custom-type="elpub" pub-id-type="custom">meat-196</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>Comparative proteomic study of pig muscle proteins during growth and development of an animal</article-title><trans-title-group xml:lang="ru"><trans-title></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="western" xml:lang="en"><surname>Akhremko</surname><given-names>A. G.</given-names></name></name-alternatives><bio xml:lang="en"><p>Anastasiya G. Akhremko, junior researcher, Experimental clinic-laboratory «Biologically active substances of an animal origin»</p><p>26, Talalikhina str., 109316, Moscow, Russia</p><p>Ph.: +7–495–676–95–11(128)</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/0000-0003-2219-5964</contrib-id><name-alternatives><name name-style="western" xml:lang="en"><surname>Vetrova</surname><given-names>E. S.</given-names></name></name-alternatives><bio xml:lang="en"><p>Evgeniya S. Vetrova, senior laboratory assistant, Experimental clinic-laboratory «Biologically active substances of an animal origin»</p><p>26, Talalikhina str., 109316, Moscow, Russia</p><p>Ph.: +7–915–027–83–89</p></bio><email xlink:type="simple">jozefina-veter@yandex.ru</email><xref ref-type="aff" rid="aff-1"/></contrib></contrib-group><aff xml:lang="en" id="aff-1"><institution>V. M. Gorbatov Federal Research Center for Food Systems</institution><country>Russian Federation</country></aff><pub-date pub-type="collection"><year>2021</year></pub-date><pub-date pub-type="epub"><day>02</day><month>01</month><year>2022</year></pub-date><volume>6</volume><issue>4</issue><fpage>320</fpage><lpage>327</lpage><permissions><copyright-statement>Copyright &amp;#x00A9; Akhremko A.G., Vetrova E.S., 2022</copyright-statement><copyright-year>2022</copyright-year><copyright-holder xml:lang="ru">Akhremko A.G., Vetrova E.S.</copyright-holder><copyright-holder xml:lang="en">Akhremko A.G., Vetrova E.S.</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/196">https://www.meatjournal.ru/jour/article/view/196</self-uri><abstract><p>The production of high-quality pork is closely related to the growth and development of muscle tissue. The present article provides a comparative proteomic research of l. dorsi, b. femoris, m. brachiocephalicus during the pigs’ growth and development (at age of 60 days and 180 days). This work was supported by data of electrophoretic methods: one-dimensional electrophoresis according to Laemmli with densitometric assessment in the ImageJ software and two-dimensional electrophoresis according to O’Farrell method with its further processing on the software ImageMaster. The mass spectrometric identification was conducted with the help of the high-performance liquid chromatography (HPLC) system connected to a mass spectrometer; further the data were interpreted by search algorithm Andromeda. When comparing frequency diagrams of one-dimensional electrophoregrams of all three muscle tissues of weaned pigs, the greatest difference was observed for the muscle sample l. dorsi. Comparison of diagrams of muscle tissue samples taken for mature pigs showed a great similarity of all three studied muscles samples. Within the framework of the research, the Fold indicator was calculated. The exceeding its value by more than 2 units is generally considered to be a statistically significant difference. When analyzing two-dimensional electrophoretograms of weaned pigs’ muscles, 18 protein fractions were revealed with Fold &gt; 2. When examining the muscle tissue of mature pigs, 15 of those proteins were found; the differences were mostly detected in the minor protein fractions. The mass spectrometric analysis of the cut bands with well-pronounced differences from the onedimensional electrophoretogram revealed 214 proteins involved to a greater extent in cellular and metabolic processes, physical activity and localization. Growth and development protein — semaphorin‑6B (96.78 kDa) — was revealed in muscle tissue of l. dorsi, a. Also in l. dorsi and b. femoris the growth and development proteins were found: cadherin‑13 (78.23 kDa), cadherin‑7 (87.01 kDa), the F‑actin-cap protein beta subunit (30.66 kDa), and two uncharacterized proteins at 65.60 kDa and 63.88 kDa.</p></abstract><kwd-group xml:lang="en"><kwd>two-dimensional electrophoresis</kwd><kwd>muscle proteins</kwd><kwd>2-DE</kwd><kwd>ontogenesis</kwd><kwd>proteomics</kwd></kwd-group><funding-group><funding-statement xml:lang="en">The research was carried out with the support of the Russian Foundation for Basic Research, project number 19–316–90056</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">Xiaobo, Z., Xiaowei, H., Povey, M. (2016). Non-invasive sensing for food reassurance. Analyst, 141(5), 1587–1610. https://doi.org/10.1039/c5an02152a</mixed-citation><mixed-citation xml:lang="en">Xiaobo, Z., Xiaowei, H., Povey, M. (2016). Non-invasive sensing for food reassurance. Analyst, 141(5), 1587–1610. https://doi.org/10.1039/c5an02152a</mixed-citation></citation-alternatives></ref><ref id="cit2"><label>2</label><citation-alternatives><mixed-citation xml:lang="ru">Chernukha, I., Fedulova, L., Vasilevskaya, E., Kulikovskii, A., Kupaeva, N., Kotenkova, E. (2021). Antioxidant effect of ethanolic onion (Allium cepa) husk extract in ageing rats. Saudi Journal of Biological Sciences, 28(5), 2877–2885. https://doi.org/10.1016/j.sjbs.2021.02.020</mixed-citation><mixed-citation xml:lang="en">Chernukha, I., Fedulova, L., Vasilevskaya, E., Kulikovskii, A., Kupaeva, N., Kotenkova, E. (2021). Antioxidant effect of ethanolic onion (Allium cepa) husk extract in ageing rats. Saudi Journal of Biological Sciences, 28(5), 2877–2885. https://doi.org/10.1016/j.sjbs.2021.02.020</mixed-citation></citation-alternatives></ref><ref id="cit3"><label>3</label><citation-alternatives><mixed-citation xml:lang="ru">Vasilevskaya, E.R., Fedulova, L.V., Chernukha, I.M., Kotenkova, E.A., Fokina, A.I. (2021). Effects of tissue-specific biomolecules on piglets after-weaning period. Veterinary World, 14(1), 168–175. https://doi.org/10.14202/vetworld.2021.168–175</mixed-citation><mixed-citation xml:lang="en">Vasilevskaya, E.R., Fedulova, L.V., Chernukha, I.M., Kotenkova, E.A., Fokina, A.I. (2021). Effects of tissue-specific biomolecules on piglets after-weaning period. Veterinary World, 14(1), 168–175. https://doi.org/10.14202/vetworld.2021.168–175</mixed-citation></citation-alternatives></ref><ref id="cit4"><label>4</label><citation-alternatives><mixed-citation xml:lang="ru">Lonergan, S.M., Huff-Lonergan, E., Rowe, L.J., Kuhlers, D.L., Jungst, S.B. (2001). Selection for lean growth efficiency in Duroc pigs influences pork quality. Journal of Animal Science, 79(8), 2075–2085. https://doi.org/10.2527/2001.7982075x</mixed-citation><mixed-citation xml:lang="en">Lonergan, S.M., Huff-Lonergan, E., Rowe, L.J., Kuhlers, D.L., Jungst, S.B. (2001). Selection for lean growth efficiency in Duroc pigs influences pork quality. Journal of Animal Science, 79(8), 2075–2085. https://doi.org/10.2527/2001.7982075x</mixed-citation></citation-alternatives></ref><ref id="cit5"><label>5</label><citation-alternatives><mixed-citation xml:lang="ru">Kim, Y.H.B., Warner, R.D., Rosenvold, K. (2014). Influence of high pre-rigor temperature and fast pH fall on muscle proteins and meat quality: a review. Animal Production Science, 54(4), 375–395. https://doi.org/10.1071/AN13329</mixed-citation><mixed-citation xml:lang="en">Kim, Y.H.B., Warner, R.D., Rosenvold, K. (2014). Influence of high pre-rigor temperature and fast pH fall on muscle proteins and meat quality: a review. Animal Production Science, 54(4), 375–395. https://doi.org/10.1071/AN13329</mixed-citation></citation-alternatives></ref><ref id="cit6"><label>6</label><citation-alternatives><mixed-citation xml:lang="ru">Lonergan, S.M., Stalder, K.J., Huff-Lonergan, E., Knight, T.J., Goodwin, R.N., Prusa, K.J. et al. (2007). Influence of lipid content on pork sensory quality within pH classification. Journal of Animal Science, 85(4), 1074–1079. https://doi.org/10.2527/jas.2006–413</mixed-citation><mixed-citation xml:lang="en">Lonergan, S.M., Stalder, K.J., Huff-Lonergan, E., Knight, T.J., Goodwin, R.N., Prusa, K.J. et al. (2007). Influence of lipid content on pork sensory quality within pH classification. Journal of Animal Science, 85(4), 1074–1079. https://doi.org/10.2527/jas.2006–413</mixed-citation></citation-alternatives></ref><ref id="cit7"><label>7</label><citation-alternatives><mixed-citation xml:lang="ru">Wheeler, T.L., Shackelford, S.D., Koohmaraie, M. (2000). Variation in proteolysis, sarcomere length, collagen content, and tenderness among major pork muscles. Journal of Animal Science, 78(4), 958–965. https://doi.org/10.2527/2000.784958x</mixed-citation><mixed-citation xml:lang="en">Wheeler, T.L., Shackelford, S.D., Koohmaraie, M. (2000). Variation in proteolysis, sarcomere length, collagen content, and tenderness among major pork muscles. Journal of Animal Science, 78(4), 958–965. https://doi.org/10.2527/2000.784958x</mixed-citation></citation-alternatives></ref><ref id="cit8"><label>8</label><citation-alternatives><mixed-citation xml:lang="ru">Lametsch, R., Roepstorff, P., Bendixen, E. (2002). Identification of protein degradation during post-mortem storage of pig meat. Journal of Agricultural and Food Chemistry, 50(20), 5508–5512. https://doi.org/10.1021/jf025555n</mixed-citation><mixed-citation xml:lang="en">Lametsch, R., Roepstorff, P., Bendixen, E. (2002). Identification of protein degradation during post-mortem storage of pig meat. Journal of Agricultural and Food Chemistry, 50(20), 5508–5512. https://doi.org/10.1021/jf025555n</mixed-citation></citation-alternatives></ref><ref id="cit9"><label>9</label><citation-alternatives><mixed-citation xml:lang="ru">Huff Lonergan, E., Zhang, W., Lonergan, S.M. (2010). Biochemistry of postmortem muscle — Lessons on mechanisms of meat tenderization. Meat Science, 86(1), 184–195. https://doi.org/10.1016/j.meatsci.2010.05.004</mixed-citation><mixed-citation xml:lang="en">Huff Lonergan, E., Zhang, W., Lonergan, S.M. (2010). Biochemistry of postmortem muscle — Lessons on mechanisms of meat tenderization. Meat Science, 86(1), 184–195. https://doi.org/10.1016/j.meatsci.2010.05.004</mixed-citation></citation-alternatives></ref><ref id="cit10"><label>10</label><citation-alternatives><mixed-citation xml:lang="ru">Jia, X., Veiseth-Kent, E., Grove, H., Kuziora, P., Aass, L., Hildrum, K.I. et al. (2009). Peroxiredoxin‑6 A potential protein marker for meat tenderness in bovine longissimus thoracis muscle. Journal of Animal Science, 87(7), 2391–2399. https://doi.org/10.2527/jas.2009–1792</mixed-citation><mixed-citation xml:lang="en">Jia, X., Veiseth-Kent, E., Grove, H., Kuziora, P., Aass, L., Hildrum, K.I. et al. (2009). Peroxiredoxin‑6 A potential protein marker for meat tenderness in bovine longissimus thoracis muscle. Journal of Animal Science, 87(7), 2391–2399. https://doi.org/10.2527/jas.2009–1792</mixed-citation></citation-alternatives></ref><ref id="cit11"><label>11</label><citation-alternatives><mixed-citation xml:lang="ru">Lametsch, R., Karlsson, A., Rosenvold, K., Andersen, H.J., Roepstorff, P., Bendixen, E. (2003). Postmortem proteome changes of porcine muscle related to tenderness. Journal of Agricultural and Food Chemistry, 51(24), 6992–6997. https://doi.org/10.1021/jf034083p</mixed-citation><mixed-citation xml:lang="en">Lametsch, R., Karlsson, A., Rosenvold, K., Andersen, H.J., Roepstorff, P., Bendixen, E. (2003). Postmortem proteome changes of porcine muscle related to tenderness. Journal of Agricultural and Food Chemistry, 51(24), 6992–6997. https://doi.org/10.1021/jf034083p</mixed-citation></citation-alternatives></ref><ref id="cit12"><label>12</label><citation-alternatives><mixed-citation xml:lang="ru">Gagaoua, M., Terlouw, E.M.C., Micol, D., Hocquette, J.F., Moloney, A.P., Nuernberg, K. et al. (2016). Sensory quality of meat from eight different types of cattle in relation with their biochemical characteristics. Journal of Integrative Agriculture, 15(7), 1550–1563. https://doi.org/10.1016/S2095–3119(16)61340–0</mixed-citation><mixed-citation xml:lang="en">Gagaoua, M., Terlouw, E.M.C., Micol, D., Hocquette, J.F., Moloney, A.P., Nuernberg, K. et al. (2016). Sensory quality of meat from eight different types of cattle in relation with their biochemical characteristics. Journal of Integrative Agriculture, 15(7), 1550–1563. https://doi.org/10.1016/S2095–3119(16)61340–0</mixed-citation></citation-alternatives></ref><ref id="cit13"><label>13</label><citation-alternatives><mixed-citation xml:lang="ru">Ouali, A., Gagaoua, M., Boudida, Y., Becila, S., Boudjellal, A., Herrera-Mendez, C.H.et al. (2013). Biomarkers of meat tenderness: present knowledge and perspectives in regards to our current understanding of the mechanisms involved. Meat Science, 95(4), 854–870. https://doi.org/10.1016/j.meatsci.2013.05.010</mixed-citation><mixed-citation xml:lang="en">Ouali, A., Gagaoua, M., Boudida, Y., Becila, S., Boudjellal, A., Herrera-Mendez, C.H.et al. (2013). Biomarkers of meat tenderness: present knowledge and perspectives in regards to our current understanding of the mechanisms involved. Meat Science, 95(4), 854–870. https://doi.org/10.1016/j.meatsci.2013.05.010</mixed-citation></citation-alternatives></ref><ref id="cit14"><label>14</label><citation-alternatives><mixed-citation xml:lang="ru">Carlson, K.B., Prusa, K.J., Fedler, C.A., Steadham, E.M., Huff- Lonergan, E., Lonergan, S.M. (2017). Proteomic features linked to tenderness of aged pork loins. Journal of Animal Science, 95(6), 2533–2546. https://doi.org/10.2527/jas2016.1122</mixed-citation><mixed-citation xml:lang="en">Carlson, K.B., Prusa, K.J., Fedler, C.A., Steadham, E.M., Huff- Lonergan, E., Lonergan, S.M. (2017). Proteomic features linked to tenderness of aged pork loins. Journal of Animal Science, 95(6), 2533–2546. https://doi.org/10.2527/jas2016.1122</mixed-citation></citation-alternatives></ref><ref id="cit15"><label>15</label><citation-alternatives><mixed-citation xml:lang="ru">Zhang, R., Ross, A.B., Yoo, M.J., Farouk, M.M. (2021). Use of Rapid Evaporative Ionisation Mass Spectrometry fingerprinting to determine the metabolic changes to dry-aged lean beef due to different ageing regimes. Meat Science, 181, Article 108438. https://doi.org/10.1016/j.meatsci.2021.108438</mixed-citation><mixed-citation xml:lang="en">Zhang, R., Ross, A.B., Yoo, M.J., Farouk, M.M. (2021). Use of Rapid Evaporative Ionisation Mass Spectrometry fingerprinting to determine the metabolic changes to dry-aged lean beef due to different ageing regimes. Meat Science, 181, Article 108438. https://doi.org/10.1016/j.meatsci.2021.108438</mixed-citation></citation-alternatives></ref><ref id="cit16"><label>16</label><citation-alternatives><mixed-citation xml:lang="ru">Trivedi, D.K., Hollywood, K.A., Rattray, N.J.W., Ward, H., Greenwood, J., Ellis, D.I. et al. (2016). Meat, the metabolites: an integrated metabolite profiling and lipidomics approach for the detection of the adulteration of beef with pork. Analyst, 141(7), 2155–2164. https://doi.org/10.1039/c6an00108d</mixed-citation><mixed-citation xml:lang="en">Trivedi, D.K., Hollywood, K.A., Rattray, N.J.W., Ward, H., Greenwood, J., Ellis, D.I. et al. (2016). Meat, the metabolites: an integrated metabolite profiling and lipidomics approach for the detection of the adulteration of beef with pork. Analyst, 141(7), 2155–2164. https://doi.org/10.1039/c6an00108d</mixed-citation></citation-alternatives></ref><ref id="cit17"><label>17</label><citation-alternatives><mixed-citation xml:lang="ru">Piasentier, E., Valusso, R., Camin, F., Versini, G. (2003). Stable isotope ratio analysis for authentication of lamb meat. Meat science, 64(3), 239–247. https://doi.org/10.1016/S0309–1740(02)00183–3</mixed-citation><mixed-citation xml:lang="en">Piasentier, E., Valusso, R., Camin, F., Versini, G. (2003). Stable isotope ratio analysis for authentication of lamb meat. Meat science, 64(3), 239–247. https://doi.org/10.1016/S0309–1740(02)00183–3</mixed-citation></citation-alternatives></ref><ref id="cit18"><label>18</label><citation-alternatives><mixed-citation xml:lang="ru">Ellis, D.I., Broadhurst, D., Goodacre, R. (2004). Rapid and quantitative detection of the microbial spoilage of beef by Fourier transform infrared spectroscopy and machine learning. Analytica Chimica Acta, 514(2), 193–201. https://doi.org/10.1016/j.aca.2004.03.060</mixed-citation><mixed-citation xml:lang="en">Ellis, D.I., Broadhurst, D., Goodacre, R. (2004). Rapid and quantitative detection of the microbial spoilage of beef by Fourier transform infrared spectroscopy and machine learning. Analytica Chimica Acta, 514(2), 193–201. https://doi.org/10.1016/j.aca.2004.03.060</mixed-citation></citation-alternatives></ref><ref id="cit19"><label>19</label><citation-alternatives><mixed-citation xml:lang="ru">Kim, Y.H.B., Kemp, R., Samuelsson, L.M. (2016). Effects of dryaging on meat quality attributes and metabolite profiles of beef loins. Meat science, 111, 168–176. https://doi.org/10.1016/j.meatsci.2015.09.008</mixed-citation><mixed-citation xml:lang="en">Kim, Y.H.B., Kemp, R., Samuelsson, L.M. (2016). Effects of dryaging on meat quality attributes and metabolite profiles of beef loins. Meat science, 111, 168–176. https://doi.org/10.1016/j.meatsci.2015.09.008</mixed-citation></citation-alternatives></ref><ref id="cit20"><label>20</label><citation-alternatives><mixed-citation xml:lang="ru">Matsumoto, H., Haniu, H., Kurien, B.T., Komori, N. (2019). Two-dimensional gel electrophoresis by glass tube-based IEF and SDS-PAGE. Chapter in a book: Methods in Molecular Biology. Springer Nature, 2019. https://doi.org/10.1007/978–1–4939–8793–1_11</mixed-citation><mixed-citation xml:lang="en">Matsumoto, H., Haniu, H., Kurien, B.T., Komori, N. (2019). Two-dimensional gel electrophoresis by glass tube-based IEF and SDS-PAGE. Chapter in a book: Methods in Molecular Biology. Springer Nature, 2019. https://doi.org/10.1007/978–1–4939–8793–1_11</mixed-citation></citation-alternatives></ref><ref id="cit21"><label>21</label><citation-alternatives><mixed-citation xml:lang="ru">Akhremko, A., Vasilevskaya, E., Fedulova, L. (2020). Adaptation of two-dimensional electrophoresis for muscle 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">Akhremko, A., Vasilevskaya, E., Fedulova, L. (2020). Adaptation of two-dimensional electrophoresis for muscle 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="cit22"><label>22</label><citation-alternatives><mixed-citation xml:lang="ru">Vasilevskaya, E.R., Aryuzina, M.A., Vetrova, E.S. (2021). Saline extraction as a method of obtaining a mixture of biologically active compounds of protein nature from a porcine pancreas. Food Systems, 4(2), 97–105. https://doi.org/10.21323/2618–9771–2021–4–2–97–105 (In Russian)</mixed-citation><mixed-citation xml:lang="en">Vasilevskaya, E.R., Aryuzina, M.A., Vetrova, E.S. (2021). Saline extraction as a method of obtaining a mixture of biologically active compounds of protein nature from a porcine pancreas. Food Systems, 4(2), 97–105. https://doi.org/10.21323/2618–9771–2021–4–2–97–105 (In Russian)</mixed-citation></citation-alternatives></ref><ref id="cit23"><label>23</label><citation-alternatives><mixed-citation xml:lang="ru">Vasilevskaya, E.R., Aryuzina, M.A., Vetrova, E.S. (2021). Comparative study of technologies for extraction of biologically active substances from the raw material of animal origin. Theory and Practice of Meat Processing, 6(3), 226–235. https://doi.org/10.21323/2414–438X‑2021–6–3–226–235</mixed-citation><mixed-citation xml:lang="en">Vasilevskaya, E.R., Aryuzina, M.A., Vetrova, E.S. (2021). Comparative study of technologies for extraction of biologically active substances from the raw material of animal origin. Theory and Practice of Meat Processing, 6(3), 226–235. https://doi.org/10.21323/2414–438X‑2021–6–3–226–235</mixed-citation></citation-alternatives></ref><ref id="cit24"><label>24</label><citation-alternatives><mixed-citation xml:lang="ru">Montowska, M., Pospiech, E. (2012). Myosin light chain isoforms retain their species-specific electrophoretic mobility after processing, which enables differentiation between six species: 2DE analysis of minced meat and meat products made from beef, pork and poultry. Proteomics, 12(18), 2879–2889. https://doi.org/10.1002/pmic.201200043</mixed-citation><mixed-citation xml:lang="en">Montowska, M., Pospiech, E. (2012). Myosin light chain isoforms retain their species-specific electrophoretic mobility after processing, which enables differentiation between six species: 2DE analysis of minced meat and meat products made from beef, pork and poultry. Proteomics, 12(18), 2879–2889. https://doi.org/10.1002/pmic.201200043</mixed-citation></citation-alternatives></ref><ref id="cit25"><label>25</label><citation-alternatives><mixed-citation xml:lang="ru">Zvereva, E.A., Kovalev, L.I., Ivanov, A.V., Kovaleva, M.A., Zherdev, A.V., Shishkin, S.S., Lisitsyn, A.B. et al. (2015). Enzyme immunoassay and proteomic characterization of troponin I as a marker of mammalian muscle compounds in raw meat and some meat products. Meat Science, 105, 46–52. https://doi.org/10.1016/j.meatsci.2015.03.001</mixed-citation><mixed-citation xml:lang="en">Zvereva, E.A., Kovalev, L.I., Ivanov, A.V., Kovaleva, M.A., Zherdev, A.V., Shishkin, S.S., Lisitsyn, A.B. et al. (2015). Enzyme immunoassay and proteomic characterization of troponin I as a marker of mammalian muscle compounds in raw meat and some meat products. Meat Science, 105, 46–52. https://doi.org/10.1016/j.meatsci.2015.03.001</mixed-citation></citation-alternatives></ref><ref id="cit26"><label>26</label><citation-alternatives><mixed-citation xml:lang="ru">Akhremko, A., Fedulova, L. (2021). Comparative study of weaning pigs’ muscle proteins using two-dimensional electrophoresis. Potravinarstvo Slovak Journal of Food Sciences, 15, 52–57. https://doi.org/10.5219/1449</mixed-citation><mixed-citation xml:lang="en">Akhremko, A., Fedulova, L. (2021). Comparative study of weaning pigs’ muscle proteins using two-dimensional electrophoresis. Potravinarstvo Slovak Journal of Food Sciences, 15, 52–57. https://doi.org/10.5219/1449</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>
