Antigen-binding activity, structural characteristics and use of monoclonal antibodies to human alpha-1-microglobulin

Four monoclonal antibodies (mAbs), G6, F9, H8, and B2, against human alpha-1-microglobulin (A1M) have been produced and characterized. The parameters of affinity (Kp ~ 10⁹ M⁻¹), epitope specificity (the additively binding G6/F9, G6/H8, G6/B2, F9/H8, and F9/B2 pairs), and the observed effect of rever...

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Bibliographic Details
Published in:Applied biochemistry and microbiology 2009-05, Vol.45 (3), p.326-333
Main Authors: Serchenya, T. S, Pryadko, A. G, Sviridov, O. V
Format: Article
Language:English
Subjects:
Amino acids
Antigens
Biochemistry
Biomedical and Life Sciences
Biotechnology
Chemical agents
Chromatography
Enzymes
Immunoassay
Life Sciences
Medical Microbiology
Microbiology
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Summary:Four monoclonal antibodies (mAbs), G6, F9, H8, and B2, against human alpha-1-microglobulin (A1M) have been produced and characterized. The parameters of affinity (Kp ~ 10⁹ M⁻¹), epitope specificity (the additively binding G6/F9, G6/H8, G6/B2, F9/H8, and F9/B2 pairs), and the observed effect of reversibility of structural changes induced by chemical agents allow use of these mAbs in biospecific methods of A1M purification and quantitative determination. The application of mAbs to an A1M enzyme immunoassay (analytical sensitivity--0.5 μg/l) and one step isolation of pure A1M by immunoaffinity chromatography was described.
ISSN:0003-6838
1608-3024
DOI:10.1134/S0003683809030156