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

Immunoglobulin 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 re[1]quires specialized methods. Development of chromatographic purification modes for immunoglobulin G (IgG) from the serum of horses hyperimmunized with rabies antigen will allow standardizing the technolo[1]gy 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, bio[1]technology 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).

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Publication Details

Journal
Bulletin of the Karaganda University “Biology medicine geography Series”
Published
2025-03-29
DOI
https://doi.org/10.31489/2025bmg1/36-43
Primary Topic
Rabies epidemiology and control
Type
article
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article

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

G.A. Bayandy, Yerkin Krykbayev, Nurlan Akhmetsadykov, E.Zh. Bitanova et al.
1 links
Bulletin of the Karaganda University “Biology medicine geography Series”
Rabies epidemiology and control
article

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

G.A. Bayandy, Yerkin Krykbayev, Nurlan Akhmetsadykov, E.Zh. Bitanova, Zh.N. Batanova, Anara Nurmukhambetova, D. Amankeldi
article en

Abstract

Immunoglobulin 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 re[1]quires specialized methods. Development of chromatographic purification modes for immunoglobulin G (IgG) from the serum of horses hyperimmunized with rabies antigen will allow standardizing the technolo[1]gy 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, bio[1]technology 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).

Bulletin of the Karaganda University “Biology medicine geography Series”Vol. 11730(1)
Openalex Percentile: Top 93%
Rabies epidemiology and control
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