Modes for chromatographic purification of immunoglobulin G (IgG) from the serum of horses hyperimmunized with rabies antigen.

dc.contributor.authorNurmukhambetova, A.B.
dc.contributor.authorBatanova, Zh.M.
dc.contributor.authorBayandy, G.A.
dc.contributor.authorKrykbayev, Y.A.
dc.contributor.authorBitanova, E.Zh.
dc.contributor.authorAkhmetsadykov, N.N.
dc.contributor.authorAmankeldi, D.S.
dc.date.accessioned2025-06-11T11:24:05Z
dc.date.available2025-06-11T11:24:05Z
dc.date.issued2025
dc.description.abstractImmunoglobulin G (IgG) plays a key role in the body’s immune response, its high specificity to antigens and effectiveness in neutralizing pathogens make it a valuable tool in medical and scientific research. Horses are a source of significant amounts of IgG, but their purification to a level suitable for clinical or scientific use requires specialized methods. Development of chromatographic purification modes for immunoglobulin G (IgG) from the serum of horses hyperimmunized with rabies antigen will allow standardizing the technology in accordance with international quality and safety standards for the production and control of immunobiological medicines, vaccines and diagnostic test systems. Development of step-by-step modes and procedures for chromatographic purification of the serum of horses hyperimmunized with rabies antigen from the CVS-11 strain, with an assessment of the efficiency of the purification technology, protein yield and purity. The study used serological methods for obtaining and preparing serum from hyperimmunized horses, as well as biotechnological methods of gel filtration, ion exchange chromatography and subsequent electrophoresis. The practical significance of the study may allow developing technologies for obtaining immunobiological preparations based on immunoglobulins, and can be used in the fields of medicine, biotechnology and scientific research that require the use of highly purified immunoglobulins. According to the presented purification technology, immunoglobulins weighing 150 kDa were obtained, which under reducing conditions are divided into 2 light chains (28 kDa) and 2 heavy chains (55 kDa).ru_RU
dc.identifier.citationModes for chromatographic purification of immunoglobulin G (IgG) from the serum of horses hyperimmunized with rabies antigen./Nurmukhambetova A.B. [et al.] // Bulletin of the Karaganda University. “Biology. Medicine. Geography” Series. — 2025. — Vol. 30 - Iss. 1(117). — 37-44pp.ru_RU
dc.identifier.issn2518-7201
dc.identifier.urihttps://rep.buketov.edu.kz//handle/data/20379
dc.language.isootherru_RU
dc.publisherKaragandy University of the name of acad. E.A. Buketovru_RU
dc.relation.ispartofseries“Biology. Medicine. Geography” Series;1(117)
dc.subjectimmunoglobulinru_RU
dc.subjectpurification technologyru_RU
dc.subjectchromatographyru_RU
dc.subjectrabiesru_RU
dc.subjectserumru_RU
dc.subjectrabies antigenru_RU
dc.subjecthyperimmunizationru_RU
dc.subjectantibodiesru_RU
dc.titleModes for chromatographic purification of immunoglobulin G (IgG) from the serum of horses hyperimmunized with rabies antigen.ru_RU
dc.typeArticleru_RU

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