Возможности использования электрофореза белков для оценки метаболизма лошадей (обзор литературы)
Аннотация
Обоснование. Электрофорез является распространённым и эффективным методом оценки белкового профиля человека и животных. Метод разделения белков с помощью электрофореза хорошо зарекомендовал себя с момента открытия и в течение нескольких десятилетий развивался и усовершенствовался. На современном этапе эта процедура не теряет актуальности и находит новые области применения.
Цель исследования. Изучить и проанализировать накопленный опыт в области применения методов детекции белков с помощью электрофореза, в частности для оценки метаболизма лошадей.
Материалы и методы. Литературный поиск производился по ключевым словам с использованием открытых баз данных: PubMed, eLibrary, Scopus, а также поисковой системы Академия Google. Были отобраны и проанализированы наиболее значимые работы по теме обзора.
Результаты. Молекулярная масса, размер и форма молекулы, а также её суммарный заряд – являются основными факторами, благодаря которым возможно разделение сложных смесей на отдельные фракции за счёт различия в скорости их движения. На успех разделения белковых смесей влияет не только природа протеинов, но и поддерживающая среда, которая должна соответствовать важным характеристикам: поддерживать оптимальный pH и пропускать молекулы с определённой скоростью. Методы детекции белков также разнообразны, как и методы разделения: неселективное окрашивание с помощью кумасси бриллиантового синего, амидо-черного 10Б, серебра, флуоресцентных красителей, и селективное с помощью иммунопреципитации или энзимоэлектрофореза.
Оценка метаболизма лошадей с помощью электрофореза распространяется практически на все области исследования: установление сезонных и возрастных изменений; анализ особенностей пород, субпопуляций и гибридов; оценка маркеров воспаления, некоторых патологий, таких, как язва, увеит, паразитарные и вирусные инфекции, миопатии, а также маркеров тренированности животных. В репродукции животных электрофорез может использоваться при оценке качества эякулята, для определения способности спермы к замораживанию, выявлении жизнеспособности сперматозоидов в том числе после криоконсервации, а также для выявления изменений во время жерёбости кобыл.
Заключение. Метод электрофореза находит широкое применение в практике оценки метаболизма человека и животных, в том числе лошадей. Имеет высокую степень значимости для анализа популяционных, возрастно-половых и сезонных различий лошадей, а также находит своё применение в оценке работоспособности животных и репродуктивных технологиях.
Информация о спонсорстве. Работа выполнена при финансовой поддержке Российского научного фонда, грант № 20-16-00101-П.
EDN: UOPHUM
Скачивания
Литература
Григорьева, Н. Н., & Григорьев, С. Н. (2022). Показатели аминокислотного состава крови якутской породы лошади. В Стратегия и перспективы развития агротехнологий и лесного комплекса Якутии до 2050 года: Сборник научных статей по материалам Всероссийской научно-практической конференции с международным участием, посвященной 100-летию образования Якутской АССР и 85-летию Первого президента РС(Я) М. Е. Николаева (Николаевские чтения) (с. 412-418). Якутск: Издательство «Знание-М». EDN: https://elibrary.ru/lnacaq
Григорьева, Н. Н., & Павлова, А. И. (2008). Некоторые гематологические показатели лошадей якутской породы по экотипам. Аграрный вестник Урала, 1(43), 50-52. EDN: https://elibrary.ru/iyqavz
Додохов, В. В., & Филиппова, Н. П. (2015). Полиморфизм белков сыворотки крови лошадей якутской породы. Потенциал современной науки, 4(12), 70-75. EDN: https://elibrary.ru/txnuwr
Завьялова, О. А., Марсянова, Ю. А., Иштулин, А. Ф., и др. (2021). Влияние металлов переменной валентности на окислительную модификацию аминокислотных остатков альбумина. Наука молодых (Eruditio Juvenium), 9(3), 369-376. https://doi.org/10.23888/HMJ202193369-376. EDN: https://elibrary.ru/dltlym
Марданлы, С. Г., Авдонина, А. С., & Затевалов, А. М. (2021). Иммунный блоттинг для выявления специфических иммуноглобулинов класса «M» к коронавирусу SARS-CoV-2. Известия ГГТУ. Медицина, фармация, 3, 45-53. EDN: https://elibrary.ru/rrmjll
Марсянова, Ю. А., Звягина, В. И., Бельских, Э. С., и др. (2024). Аргинин и сукцинат как факторы, поддерживающие окислительное фосфорилирование митохондрий при гипоксии. Известия ГГТУ. Медицина, фармация, 2, 10-18. https://doi.org/10.51620/2687-1521-2024-2-18-10-18. EDN: https://elibrary.ru/qhlioe
Марсянова, Ю. А., Звягина, В. И., & Соловых, Д. А. (2023). Влияние модуляции синтеза оксида азота (II) при хронической нормобарической гипоксии на изоферментный спектр лактатдегидрогеназы эпидидимиса крыс. Вопросы биологической, медицинской и фармацевтической химии, 26(1), 49-54. https://doi.org/10.29296/25877313-2023-01-09. EDN: https://elibrary.ru/ibjovn
Назаренко, Р. В., & Здановский, В. М. (2019). Методы селекции сперматозоидов для процедуры интрацитоплазматической инъекции сперматозоида в программах экстракорпорального оплодотворения (обзор литературы). Проблемы репродукции, 25(2), 83-89. https://doi.org/10.17116/repro20192502183. EDN: https://elibrary.ru/rvnrsh
Ниятшин, Ф. И., Долматова, И. Ю., & Ганиева, И. Н. (2015). Анализ генетической структуры лошадей башкирской породы по полиморфным белкам и ферментам крови. В Аграрная наука в инновационном развитии АПК: материалы международной научно-практической конференции, посвящённой 85-летию Башкирского государственного аграрного университета, в рамках XXV Международной специализированной выставки «Агрокомплекс-2015» (Часть II, с. 139-143). Уфа: Башкирский государственный аграрный университет. EDN: https://elibrary.ru/ubayil
Парахин, А. С., Габриелян, А. В., Деменин, В. Ю., и др. (2020). Применение комбинации методов очистки и анализа фракций белков на примере электрофоретического анализа амилолитических ферментов. В Фундаментальные и прикладные исследования в сфере естествознания и технических наук: гипотезы, идеи, результаты: Сборник научных трудов по материалам Международной научно-практической конференции (с. 24-28). Белгород: ООО «Агентство перспективных научных исследований». EDN: https://elibrary.ru/jcplnk
Тарасенко, С. В., Натальский, А. А., Песков, О. Д., Богомолов, А. Ю., Никифоров, А. А., Авилушкина, Е. О., & Тараканов, П. В. (2021). Возможности ранней диагностики и прогнозирования осложнённых клинических форм хронического панкреатита. Российский медико-биологический вестник имени академика И. П. Павлова, 29(2), 267-275. https://doi.org/10.17816/PAVLOVJ34887. EDN: https://elibrary.ru/rrlcpk
Целовальникова, М. И. (2010). Возможность использования полиморфных белков и ферментов сыворотки крови при контроле происхождения лошадей карачаевской породы. Сельскохозяйственный журнал, 3(1), 96-97. EDN: https://elibrary.ru/nwawwb
Юров, Г. К., Алексеенкова, С. В., Диас Хименес, К. А., и др. (2013). Иммунологические методы диагностики инфекционной анемии лошадей. Российский ветеринарный журнал, 1, 28-30. EDN: https://elibrary.ru/pyedot
Adams, L. D., & Gallagher, S. R. (2005). Two-dimensional gel electrophoresis. Curr Protoc Immunol, chapter 8:8.5.1-8.5.24. https://doi.org/10.1002/0471142735.im0805s68
Agarwal, A., Barbăroșie, C., Ambar, R., et al. (2020). The Impact of Single- and Double-Strand DNA Breaks in Human Spermatozoa on Assisted Reproduction. Int J Mol Sci, 21(11), 3882. https://doi.org/10.3390/ijms21113882. EDN: https://elibrary.ru/phkedt
Agrícola, R., Carvalho, H., Barbosa, M., et al. (2008). Blood lymphocyte subpopulations, neutrophil phagocytosis and proteinogram during late pregnancy and postpartum in mares. Reprod Domest Anim, 43(2), 212-217. https://doi.org/10.1111/j.1439-0531.2007.00879.x
Arakawa, T., Nakagawa, M., Sakuma, C., et al. (2024). Electrophoresis, a transport technology that transitioned from moving boundary method to zone method. Eur Biophys J, 53(1-2), 1-13. https://doi.org/10.1007/s00249-023-01694-5. EDN: https://elibrary.ru/uaebpw
Belgrave, R. L., Dickey, M. M., Arheart, K. L., et al. (2013). Assessment of serum amyloid A testing of horses and its clinical application in a specialized equine practice. J Am Vet Med Assoc, 243(1), 113-119. https://doi.org/10.2460/javma.243.1.113
Bergström, K., Aspan, A., Landén, A., et al. (2012). The first nosocomial outbreak of methicillin-resistant Staphylococcus aureus in horses in Sweden. Acta Vet Scand, 54(1), 11. https://doi.org/10.1186/1751-0147-54-11. EDN: https://elibrary.ru/ghtefo
Bouwman, F. G., van Ginneken, M. M., Noben, J. P., et al. (2010). Differential expression of equine muscle biopsy proteins during normal training and intensified training in young standardbred horses using proteomics technology. Comp Biochem Physiol Part D Genomics Proteomics, 5(1), 55-64. https://doi.org/10.1016/j.cbd.2009.11.001
Bouwman, F. G., van Ginneken, M. M., van der Kolk, J. H., et al. (2010). Novel markers for tying-up in horses by proteomics analysis of equine muscle biopsies. Comp Biochem Physiol Part D Genomics Proteomics, 5(2), 178-183. https://doi.org/10.1016/j.cbd.2010.03.009
Brandon, C. I., Heusner, G. L., Caudle, A. B., et al. (1999). Two-dimensional polyacrylamide gel electrophoresis of equine seminal plasma proteins and their correlation with fertility. Theriogenology, 52(5), 863-873. https://doi.org/10.1016/S0093-691X(99)00178-8
Burnette, W. N. (1981). “Western blotting”: electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem, 112(2), 195-203. https://doi.org/10.1016/0003-2697(81)90281-5
Byard, J., Marshall, D. E., Houghton, E., et al. (1996). Novel approaches to the purification and identification of cytochrome P450 enzymes in the equine. Biochem Soc Trans, 24(2), 208S. https://doi.org/10.1042/bst024208s
Cannon-Carlson, S., & Tang, J. (1997). Modification of the Laemmli sodium dodecyl sulfate-polyacrylamide gel electrophoresis procedure to eliminate artifacts on reducing and nonreducing gels. Anal Biochem, 246(1), 146-148. https://doi.org/10.1006/abio.1997.2002
Choudhary, S., Kumaresan, A., Kumar, M., et al. (2017). Effect of recombinant and native buffalo OVGP1 on sperm functions and in vitro embryo development: a comparative study. J Anim Sci Biotechnol, 8, 69. https://doi.org/10.1186/s40104-017-0201-5. EDN: https://elibrary.ru/irphkt
Chubatsu, L. S., Gerhardt, E. C. M., & Souza, E. M. (2023). A simple preparation of prestained molecular markers for electrophoresis using inexpensive and readily available proteins. Anal Biochem, 1(676), 115231. https://doi.org/10.1016/j.ab.2023.115231. EDN: https://elibrary.ru/glbtcp
Collinder, E., Berge, G. N., Grønvold, B., et al. (2000). Influence of bacitracin on microbial functions in the gastrointestinal tract of horses. Equine Vet J, 32(4), 345-350. https://doi.org/10.2746/042516400777032165
Csako, G. (2019). Immunoelectrophoresis: A Method with Many Faces. Methods Mol Biol, 1855, 249-268. https://doi.org/10.1007/978-1-4939-8793-1_21
de Menezes, V. T., Queiroz, A. O., Gomes, M. A., et al. (2004). Trypanosoma evansi in inbred and Swiss-Webster mice: distinct aspects of pathogenesis. Parasitol Res, 94(3), 193-200. https://doi.org/10.1007/s00436-004-1207-4. EDN: https://elibrary.ru/qxpima
Dedet, J. P. (2000). Les leishmanioses: actualités [Leishmaniasis: update]. Presse Med, 29(18), 1019-1026.
Dezhabad, A., Dalimi, A., Hoghooghi Rad, N., et al. (2023). Secretory Excretory and Somatic Immunogenic Antigens Profiles of Adult Fasciola spp. Arch Razi Inst, 78(1), 435-443. https://doi.org/10.22092/ARI.2022.359262.2393
Dias, G. M., López, M. L., Ferreira, A. T., et al. (2014). Thiol-disulfide proteins of stallion epididymal spermatozoa. Anim Reprod Sci, 145(1-2), 29-39. https://doi.org/10.1016/j.anireprosci.2013.12.007
Ellenberger, C., Wilsher, S., Allen, W. R., et al. (2008). Immunolocalisation of the uterine secretory proteins uterocalin, uteroferrin and uteroglobin in the mare’s uterus and placenta throughout pregnancy. Theriogenology, 70(5), 746-757. https://doi.org/10.1016/j.theriogenology.2008.04.050
Ellison, R. S., & Jacobs, R. M. (1990). An attempt to determine the tissue origin of equine serum alkaline phosphatase by isoelectric focusing. Can J Vet Res, 54(1), 119-125.
Franco, M. M., Santos, J. B., Mendonça, A. S., et al. (2016). Quick method for identifying horse (Equus caballus) and donkey (Equus asinus) hybrids. Genet Mol Res, 15(3), gmr.15038895. https://doi.org/10.4238/gmr.15038895
González, P. M., & Puntarulo, S. (2011). Iron and nitrosative metabolism in the Antarctic mollusc Laternula elliptica. Comp Biochem Physiol C Toxicol Pharmacol, 153(2), 243-250. https://doi.org/10.1016/j.cbpc.2010.11.003
Granstrom, D. E. (1995). Recent advances in the laboratory diagnosis of equine parasitic diseases. Vet Clin North Am Equine Pract, 11(3), 437-442. https://doi.org/10.1016/s0749-0739(17)30309-7
Grignard, E., Morin, J., Vernet, P., et al. (2005). GPX5 orthologs of the mouse epididymis-restricted and sperm-bound selenium-independent glutathione peroxidase are not expressed with the same quantitative and spatial characteristics in large domestic animals. Theriogenology, 64(4), 1016-1033. https://doi.org/10.1016/j.theriogenology.2005.01.008
Groschup, M., Müller, H. P., Weiss, R., et al. (1990). Studies of antigenic components in acid extracts of group C streptococci with special reference to Streptococcus equi. Zentralbl Bakteriol, 273(4), 459-470. https://doi.org/10.1016/s0934-8840(11)80453-6
He, H., Wang, L., Wang, X., & Zhang, M. (2024). Artificial intelligence in serum protein electrophoresis: history, state of the art, and perspective. Crit Rev Clin Lab Sci, 61(3), 226-240. https://doi.org/10.1080/10408363.2023.2274325
Jiménez-Trejo, F., Coronado-Mares, I., Boeta, M., et al. (2018). Identification of serotoninergic system components in stallion sperm. Histol Histopathol, 33(9), 951-958. https://doi.org/10.14670/HH-11-989
Jobim, M. I., Trein, C., Zirkler, H., et al. (2011). Two-dimensional polyacrylamide gel electrophoresis of equine seminal plasma proteins and their relation with semen freezability. Theriogenology, 76(4), 765-771. https://doi.org/10.1016/j.theriogenology.2011.04.010
Jung, H., Song, H., & Yoon, M. (2015). The KIT is a putative marker for differentiating spermatogonia in stallions. Anim Reprod Sci, 152, 39-46. https://doi.org/10.1016/j.anireprosci.2014.11.004
Kankavi, O., Ata, A., & Akif Ciftcioglu, M. (2006). Surfactant protein A and D in the reproductive tract of stallion. Theriogenology, 66(5), 1057-1064. https://doi.org/10.1016/j.theriogenology.2006.02.047
Kankavi, O., Ata, A., & Gungor, O. (2007). Surfactant proteins A and D in the genital tract of mares. Anim Reprod Sci, 98(3-4), 259-270. https://doi.org/10.1016/j.anireprosci.2006.03.009
Kankavi, O., & Roberts, M. S. (2004). Detection of surfactant protein A (SP-A) and surfactant protein D (SP-D) in equine synovial fluid with immunoblotting. Can J Vet Res, 68(2), 146-149
Kitaoka, Y., Hoshino, D., Mukai, K., et al. (2011). Effect of growth on monocarboxylate transporters and indicators of energy metabolism in the gluteus medius muscle of Thoroughbreds. Am J Vet Res, 72(8), 1107-1111. https://doi.org/10.2460/ajvr.72.8.1107
Kurien, B. T., & Scofield, R. H. (2006). Western blotting. Methods, 38(4), 283-293. https://doi.org/10.1016/j.ymeth.2005.11.007
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680-685. https://doi.org/10.1038/227680a0
Landsberger, M., & Brinkmeier, H. (2023). Immunoblot Analysis of DIGE-Based Proteomics. Methods Mol Biol, 2596, 429-443. https://doi.org/10.1007/978-1-0716-2831-7_29
Lee, C. H. (2017). A Simple Outline of Methods for Protein Isolation and Purification. Endocrinol Metab (Seoul), 32(1), 18-22. https://doi.org/10.3803/EnM.2017.32.1.18
López-Martínez, M. J., Lamy, E., Cerón, J. J., et al. (2024). Changes in the saliva proteome analysed by gel-proteomics in horses diagnosed with equine gastric ulcer syndrome (EGUS) at diagnosis and after successful treatment. Res Vet Sci, 167, 105112. https://doi.org/10.1016/j.rvsc.2023.105112. EDN: https://elibrary.ru/noxsyi
Machado, T. S., Correia da Silva, L. C., Baccarin, R. Y., et al. (2012). Synovial fluid chondroitin sulphate indicates abnormal joint metabolism in asymptomatic osteochondritic horses. Equine Vet J, 44(4), 404-411. https://doi.org/10.1111/j.2042-3306.2011.00539.x
Maher, A., Toaleb, N. I., & Shaapan, R. M. (2024). Human and camel cystic echinococcosis - a polyclonal antibody-based sandwich ELISA for its serodiagnosis with molecular identification. Vet Res Commun, 26. https://doi.org/10.1007/s11259-024-10375-3. EDN: https://elibrary.ru/almtgz
Martin, G. B., Mansion, F., Servais, A. C., et al. (2009). CE-MS method development for peptides analysis, especially hepcidin, an iron metabolism marker. Electrophoresis, 30(15), 2624-2631. https://doi.org/10.1002/elps.200800794
Martínez-Torrecuadrada, J. L., Díaz-Laviada, M., Roy, P., et al. (1997). Serologic markers in early stages of African horse sickness virus infection. J Clin Microbiol, 35(2), 531-535. https://doi.org/10.1128/jcm.35.2.531-535.1997
McDonagh, B. (2012). Diagonal electrophoresis for the detection of protein disulfides. Methods Mol Biol, 869, 309-315. https://doi.org/10.1007/978-1-61779-821-4_26
McGuire, T. R., & Weitkamp, L. R. (1980). Equine marker genes. Polymorphism for transferrin alleles, TfF1 and TfF2, in Thoroughbreds. Anim Blood Groups Biochem Genet, 11(2), 113-117. https://doi.org/10.1111/j.1365-2052.1980.tb01501.x
Mendoza, L., Gunawardhana, T., Batchelor, W., et al. (2019). Nanocellulose for gel electrophoresis. J Colloid Interface Sci, 540, 148-154. https://doi.org/10.1016/j.jcis.2019.01.017
Minden, J. (2007). Comparative proteomics and difference gel electrophoresis. Biotechniques, 43(6), 739-745. https://doi.org/10.2144/000112653
Miyata, H., Sugiura, T., Kai, M., et al. (1999). Muscle adaptation of Thoroughbred racehorses trained on a flat or sloped track. Am J Vet Res, 60(12), 1536-1539
Mizuno, Y., Ohba, Y., Fujita, H., et al. (1989). Activity staining of acylphosphatase after gel electrophoresis. Anal Biochem, 183(1), 46-49. https://doi.org/10.1016/0003-2697(89)90169-3
Naumenkova, V. A., Khrabrova, L. A., & Atroshchenko, M. M. (2023). Analysis of the interconnection of stallion semen indicators with genetic markers of proteins. Siberian Journal of Life Sciences and Agriculture, 15(4), 197-209. https://doi.org/10.12731/2658-6649-2023-15-4-197-209. EDN: https://elibrary.ru/hurkbr
Paltrinieri, S., Giordano, A., Villani, M., et al. (2008). Influence of age and foaling on plasma protein electrophoresis and serum amyloid A and their possible role as markers of equine neonatal septicaemia. Vet J, 176(3), 393-396. https://doi.org/10.1016/j.tvjl.2007.05.018
Poltep, K., Tesena, P., Yingchutrakul, Y., et al. (2018). Optimisation of a serum albumin removal protocol for use in a proteomic study to identify the protein biomarkers for silent gastric ulceration in horses. J Equine Sci, 29(3), 53-60. https://doi.org/10.1294/jes.29.53
Qiu, Y., Yang, H., Li, C., et al. (2020). Progress in Research on Sperm DNA Fragmentation. Med Sci Monit, 26, e918746. https://doi.org/10.12659/MSM.918746. EDN: https://elibrary.ru/uducde
Rappa, K. L., Rodriguez, H. F., Hakkarainen, G. C., et al. (2016). Sperm processing for advanced reproductive technologies: Where are we today? Biotechnol Adv, 34(5), 578-587. https://doi.org/10.1016/j.biotechadv.2016.01.007
Ren, G., Okerberg, C. K., & Mathews, S. T. (2012). Ultrasensitive protein detection and imaging: comparison of Lumitein™, ProteoSilver™, SYPRO® Ruby, and Coomassie® Brilliant Blue gel stains. Methods Mol Biol, 869, 621-632. https://doi.org/10.1007/978-1-61779-821-4_57
Rodríguez, M. C., Mussio, P. E., Villarraza, J., et al. (2023). Physicochemical Characterization of a Recombinant eCG and Comparative Studies with PMSG Commercial Preparations. Protein J, 42(1), 24-36. https://doi.org/10.1007/s10930-023-10092-x. EDN: https://elibrary.ru/zbvlvc
Sander, S. J., Joyner, P. H., Cray, C., et al. (2016). Acute phase proteins as a marker of respiratory inflammation in Przewalski’s horse (Equus Ferus Przewalskii). J Zoo Wildl Med, 47(2), 654-658. https://doi.org/10.1638/2015-0059.1
Schultze, A. E., Rohrbach, B. W., Fribourg, H. A., et al. (1999). Alterations in bovine serum biochemistry profiles associated with prolonged consumption of endophyte-infected tall fescue. Vet Hum Toxicol, 41(3), 133-139.
Shan, S., Tanaka, H., & Shoyama, Y. (2001). Enzyme-linked immunosorbent assay for glycyrrhizin using anti-glycyrrhizin monoclonal antibody and an eastern blotting technique for glucuronides of glycyrrhetic acid. Anal Chem, 73(24), 5784-90. https://doi.org/10.1021/ac0106997
Shibata, H., & Shibuya, A. (1995). Cholinesterase. Nihon Rinsho, 53(5), 1173-1177. (на японском языке)
Shin, J. A., Yang, Y. H., Kim, H. S., et al. (2002). Genetic polymorphism of the serum proteins of horses in Jeju. J Vet Sci, 3(4), 255-263.
Smith, B. J. (1984). SDS Polyacrylamide Gel Electrophoresis of Proteins. Methods Mol Biol, 41-55. https://doi.org/10.1385/0-89603-062-8
Souto, P. C., Fonseca, L. A. D., Orozco, A. M. O., et al. (2019). Acute-Phase Proteins of Healthy Horses and Horses Naturally Affected by Colic Syndrome. J Equine Vet Sci, 80, 1-4. https://doi.org/10.1016/j.jevs.2019.06.002
Tan, H. Y., Ng, T. W., & Liew, O. W. (2007). Effects of light spectrum in flatbed scanner densitometry of stained polyacrylamide gels. Biotechniques, 42(4), 474-478. https://doi.org/10.2144/0001124
Tesena, P., Yingchutrakul, Y., Roytrakul, S., et al. (2019). Searching for serum protein markers of equine squamous gastric disease using gel electrophoresis and mass spectrometry. Equine Vet J, 51(5), 581-586. https://doi.org/10.1111/evj.13068
Tomioka, Y., Nakagawa, M., Sakuma, C., et al. (2022). Analysis of bovine serum albumin unfolding in the absence and presence of ATP by SYPRO Orange staining of agarose native gel electrophoresis. Anal Biochem, 654, 114817. https://doi.org/10.1016/j.ab.2022.114817. EDN: https://elibrary.ru/gneuml
Tung, J. T., Fenton, J. I., Arnold, C., et al. (2002). Recombinant equine interleukin-1beta induces putative mediators of articular cartilage degradation in equine chondrocytes. Can J Vet Res, 66(1), 19-25.
Tung, J. T., Venta, P. J., Eberhart, S. W., et al. (2002). Effects of anti-arthritis preparations on gene expression and enzyme activity of cyclooxygenase-2 in cultured equine chondrocytes. Am J Vet Res, 63(8), 1134-1139. https://doi.org/10.2460/ajvr.2002.63.1134
van Ginneken, M. M., Keizer, H. A., Wijnberg, I. D., et al. (2004). Immunohistochemical identification and fiber type specific localization of protein kinase C isoforms in equine skeletal muscle. Am J Vet Res, 65(1), 69-73. https://doi.org/10.2460/ajvr.2004.65.69
Van Kuilenburg, A. B., Dekker, H. L., Van den Bogert, C., et al. (1991). Isoforms of human cytochrome-c oxidase. Subunit composition and steady-state kinetic properties. Eur J Biochem, 199(3), 615-622. https://doi.org/10.1111/j.1432-1033.1991.tb16162.x
Vincent, S. G., Cunningham, P. R., Stephens, N. L., et al. (1997). Quantitative densitometry of proteins stained with coomassie blue using a Hewlett Packard scanjet scanner and Scanplot software. Electrophoresis, 18(1), 67-71. https://doi.org/10.1002/elps.1150180114
Welsh, J. A., Jenkins, L. M., Kepley, J., et al. (2020). High Sensitivity Protein Gel Electrophoresis Label Compatible with Mass-Spectrometry. Biosensors (Basel), 10(11), 160. https://doi.org/10.3390/bios10110160. EDN: https://elibrary.ru/qkoihl
Zhang, L. H., & McManus, D. P. (1996). Purification and N-terminal amino acid sequencing of Echinococcus granulosus antigen 5. Parasite Immunol, 18(12), 597-606. https://doi.org/10.1046/j.1365-3024.1996.d01-42.x
Zinellu, A., Pasciu, V., Sotgia, S., et al. (2010). Capillary electrophoresis with laser-induced fluorescence detection for ATP quantification in spermatozoa and oocytes. Anal Bioanal Chem, 398(5), 2109-2116. https://doi.org/10.1007/s00216-010-4186-6
Zipplies, J. K., Hauck, S. M., Schoeffmann, S., et al. (2010). Kininogen in autoimmune uveitis: decrease in peripheral blood stream versus increase in target tissue. Invest Ophthalmol Vis Sci, 51(1), 375-382. https://doi.org/10.1167/iovs.09-4094
References
Grigorieva, N. N., & Grigoriev, S. N. (2022). Indicators of amino acid composition of blood in Yakut breed horses. In Strategy and prospects of development of agricultural technologies and forestry in Yakutia until 2050: Collection of scientific articles based on materials of the All-Russian scientific-practical conference with international participation dedicated to the 100th anniversary of the formation of the Yakut ASSR and the 85th anniversary of the First President of the RS(Y) M. E. Nikolaev (Nikolaev Readings) (pp. 412-418). Yakutsk: Publishing House «Znanie-M». EDN: https://elibrary.ru/lnacaq
Grigorieva, N. N., & Pavlova, A. I. (2008). Some hematological indicators of horses of Yakut breed by ecotypes. Agrarian Bulletin of the Urals, 1(43), 50-52. EDN: https://elibrary.ru/iyqavz
Dodokhov, V. V., & Filippova, N. P. (2015). Polymorphism of blood serum proteins in horses of Yakut breed. Potential of Modern Science, 4(12), 70-75. EDN: https://elibrary.ru/txnuwr
Zavyalova, O. A., Marsyanova, Yu. A., Ishtulin, A. F., et al. (2021). Effect of variable valence metals on oxidative modification of albumin amino acid residues. Science of the Young (Eruditio Juvenium), 9(3), 369-376. https://doi.org/10.23888/HMJ202193369-376. EDN: https://elibrary.ru/dltlym
Mardanly, S. G., Avdonina, A. S., & Zatevalov, A. M. (2021). Immune blotting for detection of specific immunoglobulins class «M» to SARS-CoV-2 coronavirus. Izvestiya GSTU. Medicine, Pharmacy, 3, 45-53. EDN: https://elibrary.ru/rrmjll
Marsyanova, Yu. A., Zvyagina, V. I., Belskikh, E. S., et al. (2024). Arginine and succinate as factors supporting mitochondrial oxidative phosphorylation under hypoxia. Izvestiya GSTU. Medicine, Pharmacy, 2, 10-18. https://doi.org/10.51620/2687-1521-2024-2-18-10-18. EDN: https://elibrary.ru/qhlioe
Marsyanova, Yu. A., Zvyagina, V. I., & Solovykh, D. A. (2023). Effect of modulation of nitric oxide (II) synthesis under chronic normobaric hypoxia on lactate dehydrogenase isoenzyme spectrum of rat epididymis. Problems of Biological, Medical and Pharmaceutical Chemistry, 26(1), 49-54. https://doi.org/10.29296/25877313-2023-01-09. EDN: https://elibrary.ru/ibjovn
Nazarenko, R. V., & Zdanovsky, V. M. (2019). Methods of sperm selection for intracytoplasmic sperm injection procedure in in vitro fertilization programs (literature review). Reproduction Issues, 25(2), 83-89. https://doi.org/10.17116/repro20192502183. EDN: https://elibrary.ru/rvnrsh
Niyatshin, F. I., Dolmatova, I. Yu., & Ganieva, I. N. (2015). Analysis of genetic structure of Bashkir breed horses by polymorphic proteins and blood enzymes. In Agricultural science in innovative development of agro-industrial complex: Materials of the international scientific-practical conference dedicated to the 85th anniversary of Bashkir State Agrarian University within the framework of the XXV International specialized exhibition «Agrocomplex-2015» (Part II, pp. 139-143). Ufa: Bashkir State Agrarian University. EDN: https://elibrary.ru/ubayil
Parakhin, A. S., Gabrielyan, A. V., Demenin, V. Yu., et al. (2020). Application of combination of protein fraction purification and analysis methods using the example of electrophoretic analysis of amylolytic enzymes. In Fundamental and applied research in natural sciences and technical sciences: hypotheses, ideas, results: Collection of scientific papers based on materials of the International scientific-practical conference (pp. 24-28). Belgorod: LLC «Agency for Advanced Scientific Research». EDN: https://elibrary.ru/jcplnk
Tarasenko, S. V., Natal’skiy, A. A., Peskov, O. D., Bogomolov, A. Yu., Nikiforov, A. A., Avilushkina, E. O., & Tarakanov, P. V. (2021). Possibilities of early diagnosis and prediction of complicated clinical forms of chronic pancreatitis. I. P. Pavlov Russian Medical and Biological Herald, 29(2), 267-275. https://doi.org/10.17816/PAVLOVJ34887. EDN: https://elibrary.ru/rrlcpk
Tseloval’nikova, M. I. (2010). Possibility of using polymorphic proteins and serum enzymes in origin control of Karachay breed horses. Agricultural Journal, 3(1), 96-97. EDN: https://elibrary.ru/nwawwb
Yurov, G. K., Alekseenkova, S. V., Diaz Jimenez, K. A., et al. (2013). Immunological methods for diagnosis of equine infectious anemia. Russian Veterinary Journal, 1, 28-30. EDN: https://elibrary.ru/pyedot
Adams, L. D., & Gallagher, S. R. (2005). Two-dimensional gel electrophoresis. Curr Protoc Immunol, chapter 8:8.5.1-8.5.24. https://doi.org/10.1002/0471142735.im0805s68
Agarwal, A., Barbăroșie, C., Ambar, R., et al. (2020). The Impact of Single- and Double-Strand DNA Breaks in Human Spermatozoa on Assisted Reproduction. Int J Mol Sci, 21(11), 3882. https://doi.org/10.3390/ijms21113882. EDN: https://elibrary.ru/phkedt
Agrícola, R., Carvalho, H., Barbosa, M., et al. (2008). Blood lymphocyte subpopulations, neutrophil phagocytosis and proteinogram during late pregnancy and postpartum in mares. Reprod Domest Anim, 43(2), 212-217. https://doi.org/10.1111/j.1439-0531.2007.00879.x
Arakawa, T., Nakagawa, M., Sakuma, C., et al. (2024). Electrophoresis, a transport technology that transitioned from moving boundary method to zone method. Eur Biophys J, 53(1-2), 1-13. https://doi.org/10.1007/s00249-023-01694-5. EDN: https://elibrary.ru/uaebpw
Belgrave, R. L., Dickey, M. M., Arheart, K. L., et al. (2013). Assessment of serum amyloid A testing of horses and its clinical application in a specialized equine practice. J Am Vet Med Assoc, 243(1), 113-119. https://doi.org/10.2460/javma.243.1.113
Bergström, K., Aspan, A., Landén, A., et al. (2012). The first nosocomial outbreak of methicillin-resistant Staphylococcus aureus in horses in Sweden. Acta Vet Scand, 54(1), 11. https://doi.org/10.1186/1751-0147-54-11. EDN: https://elibrary.ru/ghtefo
Bouwman, F. G., van Ginneken, M. M., Noben, J. P., et al. (2010). Differential expression of equine muscle biopsy proteins during normal training and intensified training in young standardbred horses using proteomics technology. Comp Biochem Physiol Part D Genomics Proteomics, 5(1), 55-64. https://doi.org/10.1016/j.cbd.2009.11.001
Bouwman, F. G., van Ginneken, M. M., van der Kolk, J. H., et al. (2010). Novel markers for tying-up in horses by proteomics analysis of equine muscle biopsies. Comp Biochem Physiol Part D Genomics Proteomics, 5(2), 178-183. https://doi.org/10.1016/j.cbd.2010.03.009
Brandon, C. I., Heusner, G. L., Caudle, A. B., et al. (1999). Two-dimensional polyacrylamide gel electrophoresis of equine seminal plasma proteins and their correlation with fertility. Theriogenology, 52(5), 863-873. https://doi.org/10.1016/S0093-691X(99)00178-8
Burnette, W. N. (1981). “Western blotting”: electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem, 112(2), 195-203. https://doi.org/10.1016/0003-2697(81)90281-5
Byard, J., Marshall, D. E., Houghton, E., et al. (1996). Novel approaches to the purification and identification of cytochrome P450 enzymes in the equine. Biochem Soc Trans, 24(2), 208S. https://doi.org/10.1042/bst024208s
Cannon-Carlson, S., & Tang, J. (1997). Modification of the Laemmli sodium dodecyl sulfate-polyacrylamide gel electrophoresis procedure to eliminate artifacts on reducing and nonreducing gels. Anal Biochem, 246(1), 146-148. https://doi.org/10.1006/abio.1997.2002
Choudhary, S., Kumaresan, A., Kumar, M., et al. (2017). Effect of recombinant and native buffalo OVGP1 on sperm functions and in vitro embryo development: a comparative study. J Anim Sci Biotechnol, 8, 69. https://doi.org/10.1186/s40104-017-0201-5. EDN: https://elibrary.ru/irphkt
Chubatsu, L. S., Gerhardt, E. C. M., & Souza, E. M. (2023). A simple preparation of prestained molecular markers for electrophoresis using inexpensive and readily available proteins. Anal Biochem, 1(676), 115231. https://doi.org/10.1016/j.ab.2023.115231. EDN: https://elibrary.ru/glbtcp
Collinder, E., Berge, G. N., Grønvold, B., et al. (2000). Influence of bacitracin on microbial functions in the gastrointestinal tract of horses. Equine Vet J, 32(4), 345-350. https://doi.org/10.2746/042516400777032165
Csako, G. (2019). Immunoelectrophoresis: A Method with Many Faces. Methods Mol Biol, 1855, 249-268. https://doi.org/10.1007/978-1-4939-8793-1_21
de Menezes, V. T., Queiroz, A. O., Gomes, M. A., et al. (2004). Trypanosoma evansi in inbred and Swiss-Webster mice: distinct aspects of pathogenesis. Parasitol Res, 94(3), 193-200. https://doi.org/10.1007/s00436-004-1207-4. EDN: https://elibrary.ru/qxpima
Dedet, J. P. (2000). Les leishmanioses: actualités [Leishmaniasis: update]. Presse Med, 29(18), 1019-1026.
Dezhabad, A., Dalimi, A., Hoghooghi Rad, N., et al. (2023). Secretory Excretory and Somatic Immunogenic Antigens Profiles of Adult Fasciola spp. Arch Razi Inst, 78(1), 435-443. https://doi.org/10.22092/ARI.2022.359262.2393
Dias, G. M., López, M. L., Ferreira, A. T., et al. (2014). Thiol-disulfide proteins of stallion epididymal spermatozoa. Anim Reprod Sci, 145(1-2), 29-39. https://doi.org/10.1016/j.anireprosci.2013.12.007
Ellenberger, C., Wilsher, S., Allen, W. R., et al. (2008). Immunolocalisation of the uterine secretory proteins uterocalin, uteroferrin and uteroglobin in the mare’s uterus and placenta throughout pregnancy. Theriogenology, 70(5), 746-757. https://doi.org/10.1016/j.theriogenology.2008.04.050
Ellison, R. S., & Jacobs, R. M. (1990). An attempt to determine the tissue origin of equine serum alkaline phosphatase by isoelectric focusing. Can J Vet Res, 54(1), 119-125.
Franco, M. M., Santos, J. B., Mendonça, A. S., et al. (2016). Quick method for identifying horse (Equus caballus) and donkey (Equus asinus) hybrids. Genet Mol Res, 15(3), gmr.15038895. https://doi.org/10.4238/gmr.15038895
González, P. M., & Puntarulo, S. (2011). Iron and nitrosative metabolism in the Antarctic mollusc Laternula elliptica. Comp Biochem Physiol C Toxicol Pharmacol, 153(2), 243-250. https://doi.org/10.1016/j.cbpc.2010.11.003
Granstrom, D. E. (1995). Recent advances in the laboratory diagnosis of equine parasitic diseases. Vet Clin North Am Equine Pract, 11(3), 437-442. https://doi.org/10.1016/s0749-0739(17)30309-7
Grignard, E., Morin, J., Vernet, P., et al. (2005). GPX5 orthologs of the mouse epididymis-restricted and sperm-bound selenium-independent glutathione peroxidase are not expressed with the same quantitative and spatial characteristics in large domestic animals. Theriogenology, 64(4), 1016-1033. https://doi.org/10.1016/j.theriogenology.2005.01.008
Groschup, M., Müller, H. P., Weiss, R., et al. (1990). Studies of antigenic components in acid extracts of group C streptococci with special reference to Streptococcus equi. Zentralbl Bakteriol, 273(4), 459-470. https://doi.org/10.1016/s0934-8840(11)80453-6
He, H., Wang, L., Wang, X., & Zhang, M. (2024). Artificial intelligence in serum protein electrophoresis: history, state of the art, and perspective. Crit Rev Clin Lab Sci, 61(3), 226-240. https://doi.org/10.1080/10408363.2023.2274325
Jiménez-Trejo, F., Coronado-Mares, I., Boeta, M., et al. (2018). Identification of serotoninergic system components in stallion sperm. Histol Histopathol, 33(9), 951-958. https://doi.org/10.14670/HH-11-989
Jobim, M. I., Trein, C., Zirkler, H., et al. (2011). Two-dimensional polyacrylamide gel electrophoresis of equine seminal plasma proteins and their relation with semen freezability. Theriogenology, 76(4), 765-771. https://doi.org/10.1016/j.theriogenology.2011.04.010
Jung, H., Song, H., & Yoon, M. (2015). The KIT is a putative marker for differentiating spermatogonia in stallions. Anim Reprod Sci, 152, 39-46. https://doi.org/10.1016/j.anireprosci.2014.11.004
Kankavi, O., Ata, A., & Akif Ciftcioglu, M. (2006). Surfactant protein A and D in the reproductive tract of stallion. Theriogenology, 66(5), 1057-1064. https://doi.org/10.1016/j.theriogenology.2006.02.047
Kankavi, O., Ata, A., & Gungor, O. (2007). Surfactant proteins A and D in the genital tract of mares. Anim Reprod Sci, 98(3-4), 259-270. https://doi.org/10.1016/j.anireprosci.2006.03.009
Kankavi, O., & Roberts, M. S. (2004). Detection of surfactant protein A (SP-A) and surfactant protein D (SP-D) in equine synovial fluid with immunoblotting. Can J Vet Res, 68(2), 146-149
Kitaoka, Y., Hoshino, D., Mukai, K., et al. (2011). Effect of growth on monocarboxylate transporters and indicators of energy metabolism in the gluteus medius muscle of Thoroughbreds. Am J Vet Res, 72(8), 1107-1111. https://doi.org/10.2460/ajvr.72.8.1107
Kurien, B. T., & Scofield, R. H. (2006). Western blotting. Methods, 38(4), 283-293. https://doi.org/10.1016/j.ymeth.2005.11.007
Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680-685. https://doi.org/10.1038/227680a0
Landsberger, M., & Brinkmeier, H. (2023). Immunoblot Analysis of DIGE-Based Proteomics. Methods Mol Biol, 2596, 429-443. https://doi.org/10.1007/978-1-0716-2831-7_29
Lee, C. H. (2017). A Simple Outline of Methods for Protein Isolation and Purification. Endocrinol Metab (Seoul), 32(1), 18-22. https://doi.org/10.3803/EnM.2017.32.1.18
López-Martínez, M. J., Lamy, E., Cerón, J. J., et al. (2024). Changes in the saliva proteome analysed by gel-proteomics in horses diagnosed with equine gastric ulcer syndrome (EGUS) at diagnosis and after successful treatment. Res Vet Sci, 167, 105112. https://doi.org/10.1016/j.rvsc.2023.105112. EDN: https://elibrary.ru/noxsyi
Machado, T. S., Correia da Silva, L. C., Baccarin, R. Y., et al. (2012). Synovial fluid chondroitin sulphate indicates abnormal joint metabolism in asymptomatic osteochondritic horses. Equine Vet J, 44(4), 404-411. https://doi.org/10.1111/j.2042-3306.2011.00539.x
Maher, A., Toaleb, N. I., & Shaapan, R. M. (2024). Human and camel cystic echinococcosis - a polyclonal antibody-based sandwich ELISA for its serodiagnosis with molecular identification. Vet Res Commun, 26. https://doi.org/10.1007/s11259-024-10375-3. EDN: https://elibrary.ru/almtgz
Martin, G. B., Mansion, F., Servais, A. C., et al. (2009). CE-MS method development for peptides analysis, especially hepcidin, an iron metabolism marker. Electrophoresis, 30(15), 2624-2631. https://doi.org/10.1002/elps.200800794
Martínez-Torrecuadrada, J. L., Díaz-Laviada, M., Roy, P., et al. (1997). Serologic markers in early stages of African horse sickness virus infection. J Clin Microbiol, 35(2), 531-535. https://doi.org/10.1128/jcm.35.2.531-535.1997
McDonagh, B. (2012). Diagonal electrophoresis for the detection of protein disulfides. Methods Mol Biol, 869, 309-315. https://doi.org/10.1007/978-1-61779-821-4_26
McGuire, T. R., & Weitkamp, L. R. (1980). Equine marker genes. Polymorphism for transferrin alleles, TfF1 and TfF2, in Thoroughbreds. Anim Blood Groups Biochem Genet, 11(2), 113-117. https://doi.org/10.1111/j.1365-2052.1980.tb01501.x
Mendoza, L., Gunawardhana, T., Batchelor, W., et al. (2019). Nanocellulose for gel electrophoresis. J Colloid Interface Sci, 540, 148-154. https://doi.org/10.1016/j.jcis.2019.01.017
Minden, J. (2007). Comparative proteomics and difference gel electrophoresis. Biotechniques, 43(6), 739-745. https://doi.org/10.2144/000112653
Miyata, H., Sugiura, T., Kai, M., et al. (1999). Muscle adaptation of Thoroughbred racehorses trained on a flat or sloped track. Am J Vet Res, 60(12), 1536-1539
Mizuno, Y., Ohba, Y., Fujita, H., et al. (1989). Activity staining of acylphosphatase after gel electrophoresis. Anal Biochem, 183(1), 46-49. https://doi.org/10.1016/0003-2697(89)90169-3
Naumenkova, V. A., Khrabrova, L. A., & Atroshchenko, M. M. (2023). Analysis of the interconnection of stallion semen indicators with genetic markers of proteins. Siberian Journal of Life Sciences and Agriculture, 15(4), 197-209. https://doi.org/10.12731/2658-6649-2023-15-4-197-209. EDN: https://elibrary.ru/hurkbr
Paltrinieri, S., Giordano, A., Villani, M., et al. (2008). Influence of age and foaling on plasma protein electrophoresis and serum amyloid A and their possible role as markers of equine neonatal septicaemia. Vet J, 176(3), 393-396. https://doi.org/10.1016/j.tvjl.2007.05.018
Poltep, K., Tesena, P., Yingchutrakul, Y., et al. (2018). Optimisation of a serum albumin removal protocol for use in a proteomic study to identify the protein biomarkers for silent gastric ulceration in horses. J Equine Sci, 29(3), 53-60. https://doi.org/10.1294/jes.29.53
Qiu, Y., Yang, H., Li, C., et al. (2020). Progress in Research on Sperm DNA Fragmentation. Med Sci Monit, 26, e918746. https://doi.org/10.12659/MSM.918746. EDN: https://elibrary.ru/uducde
Rappa, K. L., Rodriguez, H. F., Hakkarainen, G. C., et al. (2016). Sperm processing for advanced reproductive technologies: Where are we today? Biotechnol Adv, 34(5), 578-587. https://doi.org/10.1016/j.biotechadv.2016.01.007
Ren, G., Okerberg, C. K., & Mathews, S. T. (2012). Ultrasensitive protein detection and imaging: comparison of Lumitein™, ProteoSilver™, SYPRO® Ruby, and Coomassie® Brilliant Blue gel stains. Methods Mol Biol, 869, 621-632. https://doi.org/10.1007/978-1-61779-821-4_57
Rodríguez, M. C., Mussio, P. E., Villarraza, J., et al. (2023). Physicochemical Characterization of a Recombinant eCG and Comparative Studies with PMSG Commercial Preparations. Protein J, 42(1), 24-36. https://doi.org/10.1007/s10930-023-10092-x. EDN: https://elibrary.ru/zbvlvc
Sander, S. J., Joyner, P. H., Cray, C., et al. (2016). Acute phase proteins as a marker of respiratory inflammation in Przewalski’s horse (Equus Ferus Przewalskii). J Zoo Wildl Med, 47(2), 654-658. https://doi.org/10.1638/2015-0059.1
Schultze, A. E., Rohrbach, B. W., Fribourg, H. A., et al. (1999). Alterations in bovine serum biochemistry profiles associated with prolonged consumption of endophyte-infected tall fescue. Vet Hum Toxicol, 41(3), 133-139.
Shan, S., Tanaka, H., & Shoyama, Y. (2001). Enzyme-linked immunosorbent assay for glycyrrhizin using anti-glycyrrhizin monoclonal antibody and an eastern blotting technique for glucuronides of glycyrrhetic acid. Anal Chem, 73(24), 5784-90. https://doi.org/10.1021/ac0106997
Shibata, H., & Shibuya, A. (1995). Cholinesterase. Nihon Rinsho, 53(5), 1173-1177. (на японском языке)
Shin, J. A., Yang, Y. H., Kim, H. S., et al. (2002). Genetic polymorphism of the serum proteins of horses in Jeju. J Vet Sci, 3(4), 255-263.
Smith, B. J. (1984). SDS Polyacrylamide Gel Electrophoresis of Proteins. Methods Mol Biol, 41-55. https://doi.org/10.1385/0-89603-062-8
Souto, P. C., Fonseca, L. A. D., Orozco, A. M. O., et al. (2019). Acute-Phase Proteins of Healthy Horses and Horses Naturally Affected by Colic Syndrome. J Equine Vet Sci, 80, 1-4. https://doi.org/10.1016/j.jevs.2019.06.002
Tan, H. Y., Ng, T. W., & Liew, O. W. (2007). Effects of light spectrum in flatbed scanner densitometry of stained polyacrylamide gels. Biotechniques, 42(4), 474-478. https://doi.org/10.2144/0001124
Tesena, P., Yingchutrakul, Y., Roytrakul, S., et al. (2019). Searching for serum protein markers of equine squamous gastric disease using gel electrophoresis and mass spectrometry. Equine Vet J, 51(5), 581-586. https://doi.org/10.1111/evj.13068
Tomioka, Y., Nakagawa, M., Sakuma, C., et al. (2022). Analysis of bovine serum albumin unfolding in the absence and presence of ATP by SYPRO Orange staining of agarose native gel electrophoresis. Anal Biochem, 654, 114817. https://doi.org/10.1016/j.ab.2022.114817. EDN: https://elibrary.ru/gneuml
Tung, J. T., Fenton, J. I., Arnold, C., et al. (2002). Recombinant equine interleukin-1beta induces putative mediators of articular cartilage degradation in equine chondrocytes. Can J Vet Res, 66(1), 19-25.
Tung, J. T., Venta, P. J., Eberhart, S. W., et al. (2002). Effects of anti-arthritis preparations on gene expression and enzyme activity of cyclooxygenase-2 in cultured equine chondrocytes. Am J Vet Res, 63(8), 1134-1139. https://doi.org/10.2460/ajvr.2002.63.1134
van Ginneken, M. M., Keizer, H. A., Wijnberg, I. D., et al. (2004). Immunohistochemical identification and fiber type specific localization of protein kinase C isoforms in equine skeletal muscle. Am J Vet Res, 65(1), 69-73. https://doi.org/10.2460/ajvr.2004.65.69
Van Kuilenburg, A. B., Dekker, H. L., Van den Bogert, C., et al. (1991). Isoforms of human cytochrome-c oxidase. Subunit composition and steady-state kinetic properties. Eur J Biochem, 199(3), 615-622. https://doi.org/10.1111/j.1432-1033.1991.tb16162.x
Vincent, S. G., Cunningham, P. R., Stephens, N. L., et al. (1997). Quantitative densitometry of proteins stained with coomassie blue using a Hewlett Packard scanjet scanner and Scanplot software. Electrophoresis, 18(1), 67-71. https://doi.org/10.1002/elps.1150180114
Welsh, J. A., Jenkins, L. M., Kepley, J., et al. (2020). High Sensitivity Protein Gel Electrophoresis Label Compatible with Mass-Spectrometry. Biosensors (Basel), 10(11), 160. https://doi.org/10.3390/bios10110160. EDN: https://elibrary.ru/qkoihl
Zhang, L. H., & McManus, D. P. (1996). Purification and N-terminal amino acid sequencing of Echinococcus granulosus antigen 5. Parasite Immunol, 18(12), 597-606. https://doi.org/10.1046/j.1365-3024.1996.d01-42.x
Zinellu, A., Pasciu, V., Sotgia, S., et al. (2010). Capillary electrophoresis with laser-induced fluorescence detection for ATP quantification in spermatozoa and oocytes. Anal Bioanal Chem, 398(5), 2109-2116. https://doi.org/10.1007/s00216-010-4186-6
Zipplies, J. K., Hauck, S. M., Schoeffmann, S., et al. (2010). Kininogen in autoimmune uveitis: decrease in peripheral blood stream versus increase in target tissue. Invest Ophthalmol Vis Sci, 51(1), 375-382. https://doi.org/10.1167/iovs.09-4094
Copyright (c) 2025 Mikhail M. Atroshchenko, Yuliya A. Marsyanova

Это произведение доступно по лицензии Creative Commons «Attribution-NonCommercial-NoDerivatives» («Атрибуция — Некоммерческое использование — Без производных произведений») 4.0 Всемирная.